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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">nid</journal-id><journal-title-group><journal-title xml:lang="ru">Нефрология и диализ</journal-title><trans-title-group xml:lang="en"><trans-title>Nephrology and Dialysis</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1680-4422</issn><issn pub-type="epub">2618-9801</issn><publisher><publisher-name>Российское диализное общество</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.28996/2618-9801-2018-2-150-169</article-id><article-id custom-type="elpub" pub-id-type="custom">nid-333</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОБЗОРЫ И ЛЕКЦИИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEWS AND LECTURES</subject></subj-group></article-categories><title-group><article-title>Роль почек в поддержании кальциевого и магниевого гомеостаза и при его нарушениях (Часть I)</article-title><trans-title-group xml:lang="en"><trans-title>Role of kidney in maintaining calcium and magnesium homeostasis and its disorders (Part I)</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Зверев</surname><given-names>Я. Ф.</given-names></name><name name-style="western" xml:lang="en"><surname>Zverev</surname><given-names>Ja. F.</given-names></name></name-alternatives><email xlink:type="simple">zver@agmu.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Брюханов</surname><given-names>В. М.</given-names></name><name name-style="western" xml:lang="en"><surname>Bryukhanov</surname><given-names>V. M.</given-names></name></name-alternatives><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Рыкунова</surname><given-names>А. Я.</given-names></name><name name-style="western" xml:lang="en"><surname>Rykunova</surname><given-names>A. Ya.</given-names></name></name-alternatives><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-2"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ГБОУ ВПО "Алтайский государственный медицинский университет" Минздрава РФ</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Altai state medical University</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>КГБУЗ "Краевая клиническая больница" Минздрава РФ</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Altai regional clinical Hospital</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2018</year></pub-date><pub-date pub-type="epub"><day>12</day><month>08</month><year>2024</year></pub-date><volume>20</volume><issue>2</issue><fpage>150</fpage><lpage>169</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Зверев Я.Ф., Брюханов В.М., Рыкунова А.Я., 2024</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="ru">Зверев Я.Ф., Брюханов В.М., Рыкунова А.Я.</copyright-holder><copyright-holder xml:lang="en">Zverev J.F., Bryukhanov V.M., Rykunova A.Y.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://journal.nephro.ru/jour/article/view/333">https://journal.nephro.ru/jour/article/view/333</self-uri><abstract><p>Обзор посвящен проблеме кальциевого и магниевого гомеостаза и его регуляции в организме человека. С учетом последних достижений молекулярной биологии рассматривается процесс пассивного и активного переноса Ca2+ и Mg2+ в различных органах, сложные процессы регуляции их кишечной абсорбции, костной минерализации, передвижения в различных отделах почки. Обсуждается роль клаудинов в обеспечении транспорта двухвалентных катионов в толстом восходящем отделе петли Генле. Рассматриваются особенности топологи клаудинов, обусловливающие функционирование плотных межклеточных контактов в канальцах почек и их значение для процесса парацеллюлярной реабсорбции Ca2+ и Mg2+. Описывается роль каналов семейства TRP в реабсорбции Ca2+ и Mg2+ в дистальных извитых канальцах. Подчеркивается особая роль каналов TRPV5 и TRPV6 в активном трансцеллюлярном переносе этих катионов, что имеет важное значение в регуляции кальциевого и магниевого гомеостаза. Приводятся современные взгляды на топологию и функциональное значение кальций-чувствительных рецепторов, локализованных в паращитовидных железах и нефроне, в регуляции внеклеточного уровня двухвалентных катионов. Отмечается появление агонистов и антагонистов кальций-чувствительных рецепторов и их потенциальная роль в коррекции нарушений кальциевого обмена. Обсуждаются вопросы регуляции почечного транспорта Ca2+ и Mg2+.</p></abstract><trans-abstract xml:lang="en"><p>The review is devoted to the problem of calcium and magnesium homeostasis and its regulation in the human body. Taking into account the latest achievements of molecular biology, the process of passive and active transport of Ca2+ and Mg2+ in the intestine, bones and renal tubules is considered. The role of claudine in the transport of divalent cations in the thick ascending limb of the Henle loop is discussed. The peculiarities of the topology of claudins are considered, which determine the functioning of dense intercellular contacts in the renal tubules and their significance for the process of paracellular reabsorption of Ca2+ and Mg2+. The role of the TRP family channels in the reabsorption of Ca2+ and Mg2+ in the distal nephron is described. The special role of TRPV5 and TRPV6 channels in the active transcellular transfer of these cations, which is of great importance in the regulation of calcium and magnesium homeostasis, is emphasized. Modern views on the role of calcium-sensitive receptors in the regulation of the extracellular level of divalent cations are given. Issues of regulation of renal transport of Ca2+ and Mg2+ are discussed.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>гомеостаз кальция и магния</kwd><kwd>почечный транспорт</kwd><kwd>клаудины</kwd><kwd>каналы семейства TRP</kwd><kwd>кальций-чувствительный рецептор</kwd><kwd>calcium and magnesium homeostasis</kwd><kwd>renal transport</kwd><kwd>claudine</kwd><kwd>TRP family channels</kwd><kwd>calcium-sensitive receptor</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Robertson W.G., Marshall R.W. Calcium measurements in serum and plasma - Total and ionized. CRC Crit. Rev. Clin. Lab. Sci. 1979; 11: 271-304.</mixed-citation><mixed-citation xml:lang="en">Robertson W.G., Marshall R.W. Calcium measurements in serum and plasma - Total and ionized. CRC Crit. Rev. Clin. Lab. Sci. 1979; 11: 271-304.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Брюханов В.М., Зверев Я.Ф. Гомеостаз кальция и магния в норме и при патологии. Барнаул, ИП Колмогоров И.А., 2014; 187 c.</mixed-citation><mixed-citation xml:lang="en">Брюханов В.М., Зверев Я.Ф. Гомеостаз кальция и магния в норме и при патологии. Барнаул, ИП Колмогоров И.А., 2014; 187 c.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Blaine J., Chonchol M., Levi M. Renal control of calcium, phosphate, and magnesium homeostasis. Clin. J. Am. Soc. Nephrol. 2015; 10: 1257-1272.</mixed-citation><mixed-citation xml:lang="en">Blaine J., Chonchol M., Levi M. Renal control of calcium, phosphate, and magnesium homeostasis. Clin. J. Am. Soc. Nephrol. 2015; 10: 1257-1272.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Dimke H., Hoenderop J.G., Bindels R.J. Hereditary tubular transport disorders: implica-tions for renal handling of Ca2+ and Mg2+. Clin. Sci. 2010; 118: 1-18.</mixed-citation><mixed-citation xml:lang="en">Dimke H., Hoenderop J.G., Bindels R.J. Hereditary tubular transport disorders: implica-tions for renal handling of Ca2+ and Mg2+. Clin. Sci. 2010; 118: 1-18.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Riccardi D, Brown E.M. Physiology and pathophysiology of the calcium-sensing receptor in the kidney. Am. J. Physiol. Renal Physiol. 2010; 298 (3): F485-F499.</mixed-citation><mixed-citation xml:lang="en">Riccardi D, Brown E.M. Physiology and pathophysiology of the calcium-sensing receptor in the kidney. Am. J. Physiol. Renal Physiol. 2010; 298 (3): F485-F499.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Peacock M. Calcium metabolism in health and disease. CJASN. 2010; (5 Suppl): S23-S30.</mixed-citation><mixed-citation xml:lang="en">Peacock M. Calcium metabolism in health and disease. CJASN. 2010; (5 Suppl): S23-S30.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Miller R.T. Control of renal calcium, phosphate, electrolyte, and water excretion by the calcium-sensing receptor. Best Practice &amp; Res Clin. Endocrinol. &amp; Metabolism. 2013; 27: 345:358.</mixed-citation><mixed-citation xml:lang="en">Miller R.T. Control of renal calcium, phosphate, electrolyte, and water excretion by the calcium-sensing receptor. Best Practice &amp; Res Clin. Endocrinol. &amp; Metabolism. 2013; 27: 345:358.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Na T., Peng J-B. TRPV5: A Ca2+ channel for the fine-tuning of Ca2+ reabsorption. In: Mammalian Transient Receptor Potential (TRP) Cation Channels. Nilius B., Flockerzi V. eds. Handbook of Experimental Pharmacology 222. Springer-Verlag. Berlin Heidelberg. 2014; P. 322-357.</mixed-citation><mixed-citation xml:lang="en">Na T., Peng J-B. TRPV5: A Ca2+ channel for the fine-tuning of Ca2+ reabsorption. In: Mammalian Transient Receptor Potential (TRP) Cation Channels. Nilius B., Flockerzi V. eds. Handbook of Experimental Pharmacology 222. Springer-Verlag. Berlin Heidelberg. 2014; P. 322-357.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Bronner F., Pansu D. Nutritional aspects of calcium absorption. J. Nutr. 1999; 129: 9-12.</mixed-citation><mixed-citation xml:lang="en">Bronner F., Pansu D. Nutritional aspects of calcium absorption. J. Nutr. 1999; 129: 9-12.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">McCormick CC. Passive diffusion does not play a major role in the absorption of dietary calcium in normal adults. J. Nutr. 2001; 132: 3428-3430.</mixed-citation><mixed-citation xml:lang="en">McCormick CC. Passive diffusion does not play a major role in the absorption of dietary calcium in normal adults. J. Nutr. 2001; 132: 3428-3430.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Bianco S.D., Peng J.R., Takanaga H. et al. Marked disturbance of calcium homeostasis in mice with targeted disruption of the Trpv6 calcium channel gene. J. Bone Miner. Res.2007; 22: 274-285.</mixed-citation><mixed-citation xml:lang="en">Bianco S.D., Peng J.R., Takanaga H. et al. Marked disturbance of calcium homeostasis in mice with targeted disruption of the Trpv6 calcium channel gene. J. Bone Miner. Res.2007; 22: 274-285.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Benn B.S., Ajibade D., Porta A. et al. Active intestinal calcium transport in the absence of transient receptor potential vanilloid type 6 and calbindin-D9k. Endocrinology. 2008; 149: 3196-3205.</mixed-citation><mixed-citation xml:lang="en">Benn B.S., Ajibade D., Porta A. et al. Active intestinal calcium transport in the absence of transient receptor potential vanilloid type 6 and calbindin-D9k. Endocrinology. 2008; 149: 3196-3205.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Wasserman R.H., Fullmer C.S. Vitamin D and intestinal calcium transport: facts speculations and hypotheses. J. Nutr. 1995; 125: 1971S-1979S.</mixed-citation><mixed-citation xml:lang="en">Wasserman R.H., Fullmer C.S. Vitamin D and intestinal calcium transport: facts speculations and hypotheses. J. Nutr. 1995; 125: 1971S-1979S.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., van Leeuwen J.P., van der Eerden B.C. et al. Renal Ca2+ wasting hyperabsorption and reduced bone thickness in mice lacking TRPV5. J. Clin. Invest. 2003; 112: 1906-1914.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., van Leeuwen J.P., van der Eerden B.C. et al. Renal Ca2+ wasting hyperabsorption and reduced bone thickness in mice lacking TRPV5. J. Clin. Invest. 2003; 112: 1906-1914.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Keller J., Schinke T. The role of the gastrointestinal tract in calcium homeostasis and bone remodeling. Osteoporos. Int. 2013; 24: 27137-2748.</mixed-citation><mixed-citation xml:lang="en">Keller J., Schinke T. The role of the gastrointestinal tract in calcium homeostasis and bone remodeling. Osteoporos. Int. 2013; 24: 27137-2748.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Talmage R.V., Mobley H.T. Calcium homeostasis: Reassessement of the actions of para-thyroid hormone. Gen. Comp. Endocrinol. 2008; 156: 1-8.</mixed-citation><mixed-citation xml:lang="en">Talmage R.V., Mobley H.T. Calcium homeostasis: Reassessement of the actions of para-thyroid hormone. Gen. Comp. Endocrinol. 2008; 156: 1-8.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">van der Eerden B.C., Hoenderop J.G., de Vries T.J. et al. The epithelial Ca2+ channel TRPV5 is essential for proper osteoclastic bone resorption. Proc. Natl. Acad. Sci. U S A 2005; 102 (48): 17507-17512.</mixed-citation><mixed-citation xml:lang="en">van der Eerden B.C., Hoenderop J.G., de Vries T.J. et al. The epithelial Ca2+ channel TRPV5 is essential for proper osteoclastic bone resorption. Proc. Natl. Acad. Sci. U S A 2005; 102 (48): 17507-17512.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Masuyama R., Vriens J., Voets T. et al. TRPV4-mediated calcium influx regulates terminal differentiation of osteoclasts. Cell. Metab. 2008; 8 (3): 257-265.</mixed-citation><mixed-citation xml:lang="en">Masuyama R., Vriens J., Voets T. et al. TRPV4-mediated calcium influx regulates terminal differentiation of osteoclasts. Cell. Metab. 2008; 8 (3): 257-265.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Dimke H., Hoenderop J.G., Bindels R.J.M. Molecular basis of epithelial Ca2+ and Mg2+ transport: insights from the TRP channel family. J. Physiol. 2011; 589: 1535-1542.</mixed-citation><mixed-citation xml:lang="en">Dimke H., Hoenderop J.G., Bindels R.J.M. Molecular basis of epithelial Ca2+ and Mg2+ transport: insights from the TRP channel family. J. Physiol. 2011; 589: 1535-1542.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Suki W.N. Calcium transport in the nephron. Am. J. Physiol. 1979; 237: F1-F6.</mixed-citation><mixed-citation xml:lang="en">Suki W.N. Calcium transport in the nephron. Am. J. Physiol. 1979; 237: F1-F6.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Seldin D.W. Renal handling of calcium. Nephron. 1999; 81 (Suppl 1): 2-7.</mixed-citation><mixed-citation xml:lang="en">Seldin D.W. Renal handling of calcium. Nephron. 1999; 81 (Suppl 1): 2-7.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Ng R.C., Rouse D., Suki W.N. Calcium transport in the rabbit superficial proximal convoluted tubule. J. Clin. Invest. 1984; 74: 834-842.</mixed-citation><mixed-citation xml:lang="en">Ng R.C., Rouse D., Suki W.N. Calcium transport in the rabbit superficial proximal convoluted tubule. J. Clin. Invest. 1984; 74: 834-842.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Le Grimellec C. Micropuncture study along the proximal convoluted tubule. Electrolyte reabsorption in first convolutions. Pflugers Arch. 1975; 354: 133-150.</mixed-citation><mixed-citation xml:lang="en">Le Grimellec C. Micropuncture study along the proximal convoluted tubule. Electrolyte reabsorption in first convolutions. Pflugers Arch. 1975; 354: 133-150.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Suki W.N., Schwettmann R.S., Rector F.C., Seldin D.W. Effect of chronic mineralocorticoid administration on calcium excretion in the rat. Am. J. Physiol. 1968; 215: 71-74.</mixed-citation><mixed-citation xml:lang="en">Suki W.N., Schwettmann R.S., Rector F.C., Seldin D.W. Effect of chronic mineralocorticoid administration on calcium excretion in the rat. Am. J. Physiol. 1968; 215: 71-74.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Hou J., Rajagopal M., Yu A.S.L. Claudins and the kidney volume 75: annual review of physiology. Annu. Rev. Physiol. 2013; 75: 479-501.</mixed-citation><mixed-citation xml:lang="en">Hou J., Rajagopal M., Yu A.S.L. Claudins and the kidney volume 75: annual review of physiology. Annu. Rev. Physiol. 2013; 75: 479-501.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Muto S., Hata M., Taniguchi J. et al. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc. Natl. Acad. Sci. U S A. 2010; 107: 8011-8016.</mixed-citation><mixed-citation xml:lang="en">Muto S., Hata M., Taniguchi J. et al. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc. Natl. Acad. Sci. U S A. 2010; 107: 8011-8016.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Felsenfeld A., Rodriguez M., Levine B. New insights in regulation of calcium homeostasis. Curr. Opin. Nephrol. Hypertens. 2013; 22 (4): 371-376.</mixed-citation><mixed-citation xml:lang="en">Felsenfeld A., Rodriguez M., Levine B. New insights in regulation of calcium homeostasis. Curr. Opin. Nephrol. Hypertens. 2013; 22 (4): 371-376.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Hou J. New light on the role of claudins in the kidney. Organogenesis. 2012; 8 (1): 1-9.</mixed-citation><mixed-citation xml:lang="en">Hou J. New light on the role of claudins in the kidney. Organogenesis. 2012; 8 (1): 1-9.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Bleich V., Shan Q., Himmerkus N. Calcium regulation of tight junction permeability. Ann. N. Y. Acad. Sci. 2012; 1258: 93-99.</mixed-citation><mixed-citation xml:lang="en">Bleich V., Shan Q., Himmerkus N. Calcium regulation of tight junction permeability. Ann. N. Y. Acad. Sci. 2012; 1258: 93-99.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Yu A.S.L. Claudins and the kidney. J. Am. Soc. Nephrol. 2015; 26: 11-19.</mixed-citation><mixed-citation xml:lang="en">Yu A.S.L. Claudins and the kidney. J. Am. Soc. Nephrol. 2015; 26: 11-19.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Machen T.E., Erlij D., Wooding F.B. Permeable junctional complexes. The movement of lanthanum across rabbit gallbladder and intestine. J. Cell. Biol. 1972; 54: 302-312.</mixed-citation><mixed-citation xml:lang="en">Machen T.E., Erlij D., Wooding F.B. Permeable junctional complexes. The movement of lanthanum across rabbit gallbladder and intestine. J. Cell. Biol. 1972; 54: 302-312.</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Марков А.Г. Белки плотных контактов клаудины: молекулярное звено парацеллюлярного транспорта. Рос. физиол. журн. им. И.М.Сеченова. 2013; 99 (2): 175-195.</mixed-citation><mixed-citation xml:lang="en">Марков А.Г. Белки плотных контактов клаудины: молекулярное звено парацеллюлярного транспорта. Рос. физиол. журн. им. И.М.Сеченова. 2013; 99 (2): 175-195.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Furuse M., Fujita K., Hiiragi T. et al. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occluding. J. Cell. Biol. 1998; 141: 1539-1550.</mixed-citation><mixed-citation xml:lang="en">Furuse M., Fujita K., Hiiragi T. et al. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occluding. J. Cell. Biol. 1998; 141: 1539-1550.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Mineta K., Yamamoto Y., Yamazaki Y. et al. Predicted expansion of the claudin multigene family. FEBS Lett. 2011; 585: 606-612.</mixed-citation><mixed-citation xml:lang="en">Mineta K., Yamamoto Y., Yamazaki Y. et al. Predicted expansion of the claudin multigene family. FEBS Lett. 2011; 585: 606-612.</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Tsukita S., Furuse M., Itoh M. Multifunctional strands in tight junctions. Nat. Rev. Mol. Cell. Biol. 2001; 2: 285-293.</mixed-citation><mixed-citation xml:lang="en">Tsukita S., Furuse M., Itoh M. Multifunctional strands in tight junctions. Nat. Rev. Mol. Cell. Biol. 2001; 2: 285-293.</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Lal-Nag M., Morin P.J. The claudins. Genome Biol. 2009; 10 (8): 235 (Published online) URL: 10.1186/gb-2009-10-8-235.</mixed-citation><mixed-citation xml:lang="en">Lal-Nag M., Morin P.J. The claudins. Genome Biol. 2009; 10 (8): 235 (Published online) URL: 10.1186/gb-2009-10-8-235.</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Günzel D., Yu A.S.L. Function and regulation of claudins in the thick ascending limb of Henle. Pflugers Arch. 2009; 458 (1): 77-88.</mixed-citation><mixed-citation xml:lang="en">Günzel D., Yu A.S.L. Function and regulation of claudins in the thick ascending limb of Henle. Pflugers Arch. 2009; 458 (1): 77-88.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Angelow S., Ahlstrom R., Yu A.S.L. Biology of claudins. Am. J. Physiol. Renal Physiol. 2008; 295: 867-876.</mixed-citation><mixed-citation xml:lang="en">Angelow S., Ahlstrom R., Yu A.S.L. Biology of claudins. Am. J. Physiol. Renal Physiol. 2008; 295: 867-876.</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Terry S., Nie M., Matter K., Balda M.S. Rho signaling and tight junction functions. Physiology. 2010; 25: 16-26.</mixed-citation><mixed-citation xml:lang="en">Terry S., Nie M., Matter K., Balda M.S. Rho signaling and tight junction functions. Physiology. 2010; 25: 16-26.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">McCarthy K.M., Francis S.A., McCormack J.M. et al. Inducible expression of claudin-1-myc but not occluding-VSV-G results in aberrant tight junction strand formation in MDCK cells. J. Cell. Sci. 2000; 113 (Pt 19): 3387-3398.</mixed-citation><mixed-citation xml:lang="en">McCarthy K.M., Francis S.A., McCormack J.M. et al. Inducible expression of claudin-1-myc but not occluding-VSV-G results in aberrant tight junction strand formation in MDCK cells. J. Cell. Sci. 2000; 113 (Pt 19): 3387-3398.</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Itallie C.M., Fanning A.S., Anderson J.M. eversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am. J. Physiol. Renal Physiol. 2003; 285: F1078-F1084.</mixed-citation><mixed-citation xml:lang="en">Itallie C.M., Fanning A.S., Anderson J.M. eversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am. J. Physiol. Renal Physiol. 2003; 285: F1078-F1084.</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Yu A.S., Enck A.H., Lencer W.I., Schneeberger E.E. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J. Biol. Chem. 2003; 278: 17350-17359.</mixed-citation><mixed-citation xml:lang="en">Yu A.S., Enck A.H., Lencer W.I., Schneeberger E.E. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J. Biol. Chem. 2003; 278: 17350-17359.</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Wen H., Watry D.D., Marcondes M.C., Fox H.S. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 2004; 24: 8408-8417.</mixed-citation><mixed-citation xml:lang="en">Wen H., Watry D.D., Marcondes M.C., Fox H.S. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 2004; 24: 8408-8417.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Angelow S., El-Husseini R., Kanzawa S.A., Yu A.S. Renal localization and function of the tight junction protein, claudin-19. Am. J. Physiol. Renal Physiol. 2007; 293: F166-F177.</mixed-citation><mixed-citation xml:lang="en">Angelow S., El-Husseini R., Kanzawa S.A., Yu A.S. Renal localization and function of the tight junction protein, claudin-19. Am. J. Physiol. Renal Physiol. 2007; 293: F166-F177.</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Nakano Y., Kim S.H., Kim H.M. et al. A claudin-9-based ion permeability barrier is essential for hearing. PLOS Genet. 2009; 5: e1000610 (Published online) URL: 10.1371/journal.pgen.1000610.</mixed-citation><mixed-citation xml:lang="en">Nakano Y., Kim S.H., Kim H.M. et al. A claudin-9-based ion permeability barrier is essential for hearing. PLOS Genet. 2009; 5: e1000610 (Published online) URL: 10.1371/journal.pgen.1000610.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Simon D.B., Lu Y., Choate K.A. et al. Paracellin-1, a renal tight junction protein, required for paracellular Mg2+ resorption. Science. 1999; 285: 103-106.</mixed-citation><mixed-citation xml:lang="en">Simon D.B., Lu Y., Choate K.A. et al. Paracellin-1, a renal tight junction protein, required for paracellular Mg2+ resorption. Science. 1999; 285: 103-106.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Kiuchi-Saishin Y., Gotoh S., Furuse M. et al. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 2002; 13: 875-886.</mixed-citation><mixed-citation xml:lang="en">Kiuchi-Saishin Y., Gotoh S., Furuse M. et al. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 2002; 13: 875-886.</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Konrad M., Schaller A., Seelow D. et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular in-volvement. Am. J. Hum. Genet. 2006; 79: 949-957.</mixed-citation><mixed-citation xml:lang="en">Konrad M., Schaller A., Seelow D. et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular in-volvement. Am. J. Hum. Genet. 2006; 79: 949-957.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Ohta H., Adachi H., Takiguchi M. et al. Restricted localization of claudin-16 at the tight junction in the thick ascending limb of Henle’s loop together with claudins 3, 4 and 10 in bovine nephrons. J. Vet. Med. Sci. 2006; 68: 453-463.</mixed-citation><mixed-citation xml:lang="en">Ohta H., Adachi H., Takiguchi M. et al. Restricted localization of claudin-16 at the tight junction in the thick ascending limb of Henle’s loop together with claudins 3, 4 and 10 in bovine nephrons. J. Vet. Med. Sci. 2006; 68: 453-463.</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Van Itallie C.M., Rogan S., Yu A.S. et al. Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities. Am. J. Physiol. Renal Physiol. 2006; 291: F1288-F1299.</mixed-citation><mixed-citation xml:lang="en">Van Itallie C.M., Rogan S., Yu A.S. et al. Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities. Am. J. Physiol. Renal Physiol. 2006; 291: F1288-F1299.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Angelow S., Yu A.S.L. Claudins and paracellular transport: an update. Curr. Opin. Nephrol.Hypertens. 2007; 16: 459-464.</mixed-citation><mixed-citation xml:lang="en">Angelow S., Yu A.S.L. Claudins and paracellular transport: an update. Curr. Opin. Nephrol.Hypertens. 2007; 16: 459-464.</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Muto S, Hata M., Taniguchi J. et al. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc. Natl. Acad. Sci. U S A. 2010; 107: 8011-8016.</mixed-citation><mixed-citation xml:lang="en">Muto S, Hata M., Taniguchi J. et al. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc. Natl. Acad. Sci. U S A. 2010; 107: 8011-8016.</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Colegio O.R., Itallie C., Rahner C., Anderson J.M. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell. Physiol. 2003; 284: C1346-C1354.</mixed-citation><mixed-citation xml:lang="en">Colegio O.R., Itallie C., Rahner C., Anderson J.M. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell. Physiol. 2003; 284: C1346-C1354.</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Colegio O.R., Itallie C.M., McCrea H.J. et al. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am. J. Physiol. Cell. Physiol. 2002; 283: C142-C147.</mixed-citation><mixed-citation xml:lang="en">Colegio O.R., Itallie C.M., McCrea H.J. et al. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am. J. Physiol. Cell. Physiol. 2002; 283: C142-C147.</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Hou J., Renigunta A., Gomes A.S. et al.Claudin-16 and claudin-19 interaction is required for their assembly into tight junction and for renal reabsorption of magnesium. Proc. Natl. Acad. Sci. U S A. 2009; 106 (36): 15350-15355.</mixed-citation><mixed-citation xml:lang="en">Hou J., Renigunta A., Gomes A.S. et al.Claudin-16 and claudin-19 interaction is required for their assembly into tight junction and for renal reabsorption of magnesium. Proc. Natl. Acad. Sci. U S A. 2009; 106 (36): 15350-15355.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Gong Y., Renigunta V., Himmerkus N. et al. Claudin-14 regulates renal Ca++ transport in response to CaSR signaling via a novel microRNA pathway. EMBO J. 2012; 31 (8): 1999-2012.</mixed-citation><mixed-citation xml:lang="en">Gong Y., Renigunta V., Himmerkus N. et al. Claudin-14 regulates renal Ca++ transport in response to CaSR signaling via a novel microRNA pathway. EMBO J. 2012; 31 (8): 1999-2012.</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Ben-Yosef T., Belyantseva I.A., Saunders T.L. et al. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum. Mol. Genet. 2003; 12: 2049-2061.</mixed-citation><mixed-citation xml:lang="en">Ben-Yosef T., Belyantseva I.A., Saunders T.L. et al. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum. Mol. Genet. 2003; 12: 2049-2061.</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Elkouby-Naor L., Abassi Z., Lagziel A. et al. Double gene deletion reveals lack of cooperation between claudin11 and claudin 14 tight junction proteins. Cell. Tissue Res. 2008; 333: 427-438.</mixed-citation><mixed-citation xml:lang="en">Elkouby-Naor L., Abassi Z., Lagziel A. et al. Double gene deletion reveals lack of cooperation between claudin11 and claudin 14 tight junction proteins. Cell. Tissue Res. 2008; 333: 427-438.</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Enck A.H., Berger U.V., Yu A.S. Claudin-2 is selectively expressed in proximal nephron in mouse kidney. Am. J. Physiol. Renal Physiol. 2001; 281: F966-F974.</mixed-citation><mixed-citation xml:lang="en">Enck A.H., Berger U.V., Yu A.S. Claudin-2 is selectively expressed in proximal nephron in mouse kidney. Am. J. Physiol. Renal Physiol. 2001; 281: F966-F974.</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Yu A.S., Cheng M.H., Angelow S. et al. Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site. J. Gen. Physiol. 2009; 133: 111-127.</mixed-citation><mixed-citation xml:lang="en">Yu A.S., Cheng M.H., Angelow S. et al. Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site. J. Gen. Physiol. 2009; 133: 111-127.</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Reilly R.F., Ellison D.H. Mammalian distal tubule: physiology, pathophysiology, and molecular anatomy. Physiol. Rev. 2000; 80: 277-313.</mixed-citation><mixed-citation xml:lang="en">Reilly R.F., Ellison D.H. Mammalian distal tubule: physiology, pathophysiology, and molecular anatomy. Physiol. Rev. 2000; 80: 277-313.</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Agus Z.S., Chiu P.J., Goldberg M. Regulation of urinary calcium excretion in the rat. Am. J. Physiol. 1977; 232: F545-F549.</mixed-citation><mixed-citation xml:lang="en">Agus Z.S., Chiu P.J., Goldberg M. Regulation of urinary calcium excretion in the rat. Am. J. Physiol. 1977; 232: F545-F549.</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G.J., Bindels R.J.M. Epithelial Ca2+ and Mg2+ channels in health and disease. JASN. 2005; 16 (1): 15-26.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G.J., Bindels R.J.M. Epithelial Ca2+ and Mg2+ channels in health and disease. JASN. 2005; 16 (1): 15-26.</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Романенко С.В., Костюк П.Г., Костюк Е.П. Трансмембранна кальцiєва сигналiзацiя - роль у ноцицепцiї. Журн. Акад. Мед. Наук України. 2008; 14 (1): 3-25.</mixed-citation><mixed-citation xml:lang="en">Романенко С.В., Костюк П.Г., Костюк Е.П. Трансмембранна кальцiєва сигналiзацiя - роль у ноцицепцiї. Журн. Акад. Мед. Наук України. 2008; 14 (1): 3-25.</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Васильева И.О., Негуляев Ю.А., Марахова И.И., Семенова СБ. TRPV5 и TRPV6 кальциевые каналы в Т клетках человека. Цитология. 2008; 50 (11): 953-957.</mixed-citation><mixed-citation xml:lang="en">Васильева И.О., Негуляев Ю.А., Марахова И.И., Семенова СБ. TRPV5 и TRPV6 кальциевые каналы в Т клетках человека. Цитология. 2008; 50 (11): 953-957.</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Voets T., Prenen J., Vriens J. et al. Molecular determinants of permeation through the cation channel TRPV4. J. Biol. Chem. 2002; 277 (37): 33704-33710.</mixed-citation><mixed-citation xml:lang="en">Voets T., Prenen J., Vriens J. et al. Molecular determinants of permeation through the cation channel TRPV4. J. Biol. Chem. 2002; 277 (37): 33704-33710.</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., Bindels R.J. Calciotropic and magnesiotropic TRP channels. Physiology (Bethesda). 2008; 23: 32-40.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., Bindels R.J. Calciotropic and magnesiotropic TRP channels. Physiology (Bethesda). 2008; 23: 32-40.</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., van der Kemp A.W., Hartoq A. et al. Molecular identification of the apical Ca2+ channel in 1,25-dihydroxyvitamin D3-responsive epithelia. J. Biol.Chem. 1999; 274 (13): 8375-8378.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., van der Kemp A.W., Hartoq A. et al. Molecular identification of the apical Ca2+ channel in 1,25-dihydroxyvitamin D3-responsive epithelia. J. Biol.Chem. 1999; 274 (13): 8375-8378.</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Peng J.B., Chen X.Z., Berger U.V. et al. Molecular cloning and characterization of channel-like transporter mediating intestinal calcium absorption. J. Biol. Chem. 1999; 274 (32): 22739-22746.</mixed-citation><mixed-citation xml:lang="en">Peng J.B., Chen X.Z., Berger U.V. et al. Molecular cloning and characterization of channel-like transporter mediating intestinal calcium absorption. J. Biol. Chem. 1999; 274 (32): 22739-22746.</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Muller D., Hoenderop J.G., Merkx G.F. et al. Gene structure and chromosomal mapping of human epithelial calcium channel. Biochem. Biophys. Res. Commun. 2000; 275: 47-52.</mixed-citation><mixed-citation xml:lang="en">Muller D., Hoenderop J.G., Merkx G.F. et al. Gene structure and chromosomal mapping of human epithelial calcium channel. Biochem. Biophys. Res. Commun. 2000; 275: 47-52.</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Peng J.B., Brown E.M., Hediger M.A. Structural conservation of the genes encoding CaT1, CaT2 and related cation channels. Genomics. 2001; 76: 99-109.</mixed-citation><mixed-citation xml:lang="en">Peng J.B., Brown E.M., Hediger M.A. Structural conservation of the genes encoding CaT1, CaT2 and related cation channels. Genomics. 2001; 76: 99-109.</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Weber K., Erben R.G., Rump A., Adamski J. Gene structure and regulation of the murine epithelial calcium channels ECaC1 and 2. J. Physiol (Lond). 2001; 537: 747-761.</mixed-citation><mixed-citation xml:lang="en">Weber K., Erben R.G., Rump A., Adamski J. Gene structure and regulation of the murine epithelial calcium channels ECaC1 and 2. J. Physiol (Lond). 2001; 537: 747-761.</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Nijenhuis T., Hoenderop J.G.J., van der Kemp A.W.C.M., Bindels R.J.M. Localization and regulation of the epithelial Ca2+ channel TRPV6 in the kidney. J. Am. Soc.Nephrol. 2003; 14 (11): 2731-2740.</mixed-citation><mixed-citation xml:lang="en">Nijenhuis T., Hoenderop J.G.J., van der Kemp A.W.C.M., Bindels R.J.M. Localization and regulation of the epithelial Ca2+ channel TRPV6 in the kidney. J. Am. Soc.Nephrol. 2003; 14 (11): 2731-2740.</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Voets T., Janssens A., Droogmans G., Nilius B. Outer pore architecture of a Ca2+-selective TRP channel. J. Biol. Chem. 2004; 279: 15223-15230.</mixed-citation><mixed-citation xml:lang="en">Voets T., Janssens A., Droogmans G., Nilius B. Outer pore architecture of a Ca2+-selective TRP channel. J. Biol. Chem. 2004; 279: 15223-15230.</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., Nilius B., Bindels R.J. Molecular mechanisms of active Ca2+ reabsorption in the distal nephron. Annu. Rev. Physiol. 2002; 64: 529-549.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., Nilius B., Bindels R.J. Molecular mechanisms of active Ca2+ reabsorption in the distal nephron. Annu. Rev. Physiol. 2002; 64: 529-549.</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Lambers T.T., Mahieu F., Oancea E. et al. Calbindin D28k dynamically controls TRPV5-mediated Ca2+ transport. EMBO J. 2006; 25: 2978-2988.</mixed-citation><mixed-citation xml:lang="en">Lambers T.T., Mahieu F., Oancea E. et al. Calbindin D28k dynamically controls TRPV5-mediated Ca2+ transport. EMBO J. 2006; 25: 2978-2988.</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Lee C-T., Ng H-Y., Lee Y-T. et al. The role of calbindin-D28k on renal calcium and magnesium handling during treatment with loop and thiazide diuretics. Am. J. Physiol. Renal Physiol. 2016; 310: F230-F236.</mixed-citation><mixed-citation xml:lang="en">Lee C-T., Ng H-Y., Lee Y-T. et al. The role of calbindin-D28k on renal calcium and magnesium handling during treatment with loop and thiazide diuretics. Am. J. Physiol. Renal Physiol. 2016; 310: F230-F236.</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Bindels R.J., Hartog A., Timmermans J., Van Os C.H. Active Ca2+ transport in primary cultures of rabbit kidney CCD: Stimulation by 1,25-dihydroxyvitamin D3 and PTH. Am. J. Physiol. 1991; 261 (5 Pt 2): F799-F807.</mixed-citation><mixed-citation xml:lang="en">Bindels R.J., Hartog A., Timmermans J., Van Os C.H. Active Ca2+ transport in primary cultures of rabbit kidney CCD: Stimulation by 1,25-dihydroxyvitamin D3 and PTH. Am. J. Physiol. 1991; 261 (5 Pt 2): F799-F807.</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Gesek F.A., Friedman P.A. Calcitonin stimulates calcium transport in distal convoluted tubule cells. Am. J. Physiol. 1993; 264 (4 Pt 2): F744-F751.</mixed-citation><mixed-citation xml:lang="en">Gesek F.A., Friedman P.A. Calcitonin stimulates calcium transport in distal convoluted tubule cells. Am. J. Physiol. 1993; 264 (4 Pt 2): F744-F751.</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Friedman P.A., Coutermarsh B.A., Kennedy S.M., Gesek FA. Parathyroid hormone stimulation of calcium transport is mediated by dual signaling mechanisms involving protein ki-nase A and protein kinase C. Endocrinology. 1996; 137 (1): 13-20.</mixed-citation><mixed-citation xml:lang="en">Friedman P.A., Coutermarsh B.A., Kennedy S.M., Gesek FA. Parathyroid hormone stimulation of calcium transport is mediated by dual signaling mechanisms involving protein ki-nase A and protein kinase C. Endocrinology. 1996; 137 (1): 13-20.</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Peng J.B., Zhuang L., Berger U.V. et al. CaT1 expression correlates with tumor grade in prostate cancer. Biochem. Biophys. Res. Commun. 2001; 282 (3): 729-734.</mixed-citation><mixed-citation xml:lang="en">Peng J.B., Zhuang L., Berger U.V. et al. CaT1 expression correlates with tumor grade in prostate cancer. Biochem. Biophys. Res. Commun. 2001; 282 (3): 729-734.</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Van Cromphaut S.J., Dewerchin M., Hoenderop J.G. et al. Duodenal calcium absorption in vitamin D receptor-knockout mice: Functional and molecular aspects. Proc. Natl. Acad. Sci. U S A. 2001; 98 (23): 13324-13329.</mixed-citation><mixed-citation xml:lang="en">Van Cromphaut S.J., Dewerchin M., Hoenderop J.G. et al. Duodenal calcium absorption in vitamin D receptor-knockout mice: Functional and molecular aspects. Proc. Natl. Acad. Sci. U S A. 2001; 98 (23): 13324-13329.</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Van Cromphaut S.J., Rummens K., Stockmans I. et al. Intestinal calcium transporter genes are upregulated by estrogens and the reproductive cycle trough vitamin D receptor-independent mechanisms. J. Bone Miner. Res. 2003; 18 (10): 1725-1736.</mixed-citation><mixed-citation xml:lang="en">Van Cromphaut S.J., Rummens K., Stockmans I. et al. Intestinal calcium transporter genes are upregulated by estrogens and the reproductive cycle trough vitamin D receptor-independent mechanisms. J. Bone Miner. Res. 2003; 18 (10): 1725-1736.</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., Dardenne O., van Abel M. et al. Modulation of renal Ca2+ transport protein genes by dietary Ca2+ and 25-hydroxyvitamin D3-1α-hydroxylase knockout mice. FASEB J. 2002; 16 (11): 1398-1406.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., Dardenne O., van Abel M. et al. Modulation of renal Ca2+ transport protein genes by dietary Ca2+ and 25-hydroxyvitamin D3-1α-hydroxylase knockout mice. FASEB J. 2002; 16 (11): 1398-1406.</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Hoenderop J.G., Chon H., Gkika D. et al. Regulation of gene expression by dietary Ca2+ in kidneys of 25-hydroxyvitamin D3-1α-hydroxylase knockout mice. Kidney Int. 2004; 65 (2): 531-539.</mixed-citation><mixed-citation xml:lang="en">Hoenderop J.G., Chon H., Gkika D. et al. Regulation of gene expression by dietary Ca2+ in kidneys of 25-hydroxyvitamin D3-1α-hydroxylase knockout mice. Kidney Int. 2004; 65 (2): 531-539.</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Van Abel M., Hoenderop J.G., Dardenne O. et al. 1,25-dihydroxyvitamin D3-independent stimulatory effect of estrogen on the expression of ECaC1 in the kidney. J. Am. Soc. Nephrol. 2002; 13 (8): 2102-2109.</mixed-citation><mixed-citation xml:lang="en">Van Abel M., Hoenderop J.G., Dardenne O. et al. 1,25-dihydroxyvitamin D3-independent stimulatory effect of estrogen on the expression of ECaC1 in the kidney. J. Am. Soc. Nephrol. 2002; 13 (8): 2102-2109.</mixed-citation></citation-alternatives></ref><ref id="cit87"><label>87</label><citation-alternatives><mixed-citation xml:lang="ru">Boros S., Bindels R.J., Hoenderop J.G. Active Ca2+ reabsorption in the connecting tubule. Pflugers Arch. 2009; 458 (1): 99-109.</mixed-citation><mixed-citation xml:lang="en">Boros S., Bindels R.J., Hoenderop J.G. Active Ca2+ reabsorption in the connecting tubule. Pflugers Arch. 2009; 458 (1): 99-109.</mixed-citation></citation-alternatives></ref><ref id="cit88"><label>88</label><citation-alternatives><mixed-citation xml:lang="ru">Hsu Y.J., Dimke H., Schoeher J.P. et al. Testosterone increases urinary calcium excretion and inhibits expression of renal calcium transport proteins. Kidney Int. 2010; 77 (7): 601-608.</mixed-citation><mixed-citation xml:lang="en">Hsu Y.J., Dimke H., Schoeher J.P. et al. Testosterone increases urinary calcium excretion and inhibits expression of renal calcium transport proteins. Kidney Int. 2010; 77 (7): 601-608.</mixed-citation></citation-alternatives></ref><ref id="cit89"><label>89</label><citation-alternatives><mixed-citation xml:lang="ru">Brown E.M., Gamba G., Riccardi D. et al. Cloning and characterization of an extracellular Ca2+-sensing receptor from bovine parathyroid. Nature. 1993; 366: 575-580.</mixed-citation><mixed-citation xml:lang="en">Brown E.M., Gamba G., Riccardi D. et al. Cloning and characterization of an extracellular Ca2+-sensing receptor from bovine parathyroid. Nature. 1993; 366: 575-580.</mixed-citation></citation-alternatives></ref><ref id="cit90"><label>90</label><citation-alternatives><mixed-citation xml:lang="ru">Tfelt-Hansen J., Brown E.M. The calcium-sensing receptor in normal physiology and pathophysiology: a review. Crit. Rev. Clin. Lab. Sci. 2005; 42: 35-70.</mixed-citation><mixed-citation xml:lang="en">Tfelt-Hansen J., Brown E.M. The calcium-sensing receptor in normal physiology and pathophysiology: a review. Crit. Rev. Clin. Lab. Sci. 2005; 42: 35-70.</mixed-citation></citation-alternatives></ref><ref id="cit91"><label>91</label><citation-alternatives><mixed-citation xml:lang="ru">Nemeth E.F., Steffey M.E., Hammerland L.G. et al. Calcimimetics with potent and selective activity on the parathyroid calcium receptor. Proc. Natl. Acad. Sci. U S A. 1998; 95: 4040-4045.</mixed-citation><mixed-citation xml:lang="en">Nemeth E.F., Steffey M.E., Hammerland L.G. et al. Calcimimetics with potent and selective activity on the parathyroid calcium receptor. Proc. Natl. Acad. Sci. U S A. 1998; 95: 4040-4045.</mixed-citation></citation-alternatives></ref><ref id="cit92"><label>92</label><citation-alternatives><mixed-citation xml:lang="ru">Fudge N.J., Kovacs C.S. Physiological studies in heterozygous calcium sensing receptor (CaSR) gene-ablated mice confirm that the CaSR regulates calcitonin release in vivo. BMC Physiol. 2004; 4: 5.</mixed-citation><mixed-citation xml:lang="en">Fudge N.J., Kovacs C.S. Physiological studies in heterozygous calcium sensing receptor (CaSR) gene-ablated mice confirm that the CaSR regulates calcitonin release in vivo. BMC Physiol. 2004; 4: 5.</mixed-citation></citation-alternatives></ref><ref id="cit93"><label>93</label><citation-alternatives><mixed-citation xml:lang="ru">Brauner-Osborne H., Wellendorph P., Jensen A.A. Structure, pharmacology and therapeutic prospects of family C G-protein coupled receptors. Curr. Drug Targets. 2007; 8: 169-184.</mixed-citation><mixed-citation xml:lang="en">Brauner-Osborne H., Wellendorph P., Jensen A.A. Structure, pharmacology and therapeutic prospects of family C G-protein coupled receptors. Curr. Drug Targets. 2007; 8: 169-184.</mixed-citation></citation-alternatives></ref><ref id="cit94"><label>94</label><citation-alternatives><mixed-citation xml:lang="ru">Aida K., Koishi S., Tawata M., Onaya T. Molecular cloning of a putative Ca(2+)-sensing receptor cDNA from human kidney. Biochem. Biophys. Res. Commun. 1995; 214 (2): 524-529.</mixed-citation><mixed-citation xml:lang="en">Aida K., Koishi S., Tawata M., Onaya T. Molecular cloning of a putative Ca(2+)-sensing receptor cDNA from human kidney. Biochem. Biophys. Res. Commun. 1995; 214 (2): 524-529.</mixed-citation></citation-alternatives></ref><ref id="cit95"><label>95</label><citation-alternatives><mixed-citation xml:lang="ru">Janicic N., Soliman E., Pausova Z. et al. Mapping of the calcium-sensing receptor gene (CASR) to human chromosome 3q13.3-21 by fluorescence in situ hybridization, and localization to rat chromosome 11 and mouse chromosome 16. Mamm. Genome. 1995; 6 (11): 798-801.</mixed-citation><mixed-citation xml:lang="en">Janicic N., Soliman E., Pausova Z. et al. Mapping of the calcium-sensing receptor gene (CASR) to human chromosome 3q13.3-21 by fluorescence in situ hybridization, and localization to rat chromosome 11 and mouse chromosome 16. Mamm. Genome. 1995; 6 (11): 798-801.</mixed-citation></citation-alternatives></ref><ref id="cit96"><label>96</label><citation-alternatives><mixed-citation xml:lang="ru">Garrett J.E., Capuano I.V., Hammerland L.G. et al. Molecular cloning and functional expression of human parathyroid calcium receptor cDNAs. J. Biol. Chem. 1995; 270 (21): 12919-12925.</mixed-citation><mixed-citation xml:lang="en">Garrett J.E., Capuano I.V., Hammerland L.G. et al. Molecular cloning and functional expression of human parathyroid calcium receptor cDNAs. J. Biol. Chem. 1995; 270 (21): 12919-12925.</mixed-citation></citation-alternatives></ref><ref id="cit97"><label>97</label><citation-alternatives><mixed-citation xml:lang="ru">Silve C., Petrel C., Leroy C. et al. Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor J. Biol. Chem. 2005; 280: 37917-37923.</mixed-citation><mixed-citation xml:lang="en">Silve C., Petrel C., Leroy C. et al. Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor J. Biol. Chem. 2005; 280: 37917-37923.</mixed-citation></citation-alternatives></ref><ref id="cit98"><label>98</label><citation-alternatives><mixed-citation xml:lang="ru">Huang C., Miller R.T. The calcium-sensing receptor and its interacting proteins. J. Cell. Mol. Med. 2007; 11: 923-934.</mixed-citation><mixed-citation xml:lang="en">Huang C., Miller R.T. The calcium-sensing receptor and its interacting proteins. J. Cell. Mol. Med. 2007; 11: 923-934.</mixed-citation></citation-alternatives></ref><ref id="cit99"><label>99</label><citation-alternatives><mixed-citation xml:lang="ru">Conigrave A.D., Mun H.C., Brennan S.C. Physiological significance of l-amino acid sensing by extracellular Ca2+-sensing receptors. Biochem. Soc. Trans. 2007; 35: 1195-1198.</mixed-citation><mixed-citation xml:lang="en">Conigrave A.D., Mun H.C., Brennan S.C. Physiological significance of l-amino acid sensing by extracellular Ca2+-sensing receptors. Biochem. Soc. Trans. 2007; 35: 1195-1198.</mixed-citation></citation-alternatives></ref><ref id="cit100"><label>100</label><citation-alternatives><mixed-citation xml:lang="ru">Hu J., Spiegel A.M. Naturally occurring mutations in the extracellular Ca2+-sensing receptor: implications for its structure and function. Trends Endocrinol. Metab. 2003; 14: 282-288.</mixed-citation><mixed-citation xml:lang="en">Hu J., Spiegel A.M. Naturally occurring mutations in the extracellular Ca2+-sensing receptor: implications for its structure and function. Trends Endocrinol. Metab. 2003; 14: 282-288.</mixed-citation></citation-alternatives></ref><ref id="cit101"><label>101</label><citation-alternatives><mixed-citation xml:lang="ru">Gowen M., Stroup G.B., Dodds R.A. et al. Antagonizing the parathyroid calcium receptor stimulates parathyroid hormone secretion and bone formation in osteopenic rats. J. Clin. Invest. 2000; 105: 1595-1604.</mixed-citation><mixed-citation xml:lang="en">Gowen M., Stroup G.B., Dodds R.A. et al. Antagonizing the parathyroid calcium receptor stimulates parathyroid hormone secretion and bone formation in osteopenic rats. J. Clin. Invest. 2000; 105: 1595-1604.</mixed-citation></citation-alternatives></ref><ref id="cit102"><label>102</label><citation-alternatives><mixed-citation xml:lang="ru">Brown E.M. Clinical lessons from the calcium-sensing receptor. Nat. Clin. Pract. Endocrinol. Metab. 2007; 3: 122-133.</mixed-citation><mixed-citation xml:lang="en">Brown E.M. Clinical lessons from the calcium-sensing receptor. Nat. Clin. Pract. Endocrinol. Metab. 2007; 3: 122-133.</mixed-citation></citation-alternatives></ref><ref id="cit103"><label>103</label><citation-alternatives><mixed-citation xml:lang="ru">Mithal A., Kifor O., Kifor I. et al. The reduced responsiveness of cultured bovine parathyroid cells to extracellular Ca2+ is associated with marked reduction in the expression of extracellular Ca(2+)-sensing receptor messenger ribonucleic acid and protein. Endocrinology. 1995; 136 (7): 3087-3092.</mixed-citation><mixed-citation xml:lang="en">Mithal A., Kifor O., Kifor I. et al. The reduced responsiveness of cultured bovine parathyroid cells to extracellular Ca2+ is associated with marked reduction in the expression of extracellular Ca(2+)-sensing receptor messenger ribonucleic acid and protein. Endocrinology. 1995; 136 (7): 3087-3092.</mixed-citation></citation-alternatives></ref><ref id="cit104"><label>104</label><citation-alternatives><mixed-citation xml:lang="ru">Garfia B., Canadillas S., Canalejo A. et al. Regulation of parathyroid vitamin D receptor expression by extracellular calcium. J. Am. Soc. Nephrol. 2002; 13: 2945-2952.</mixed-citation><mixed-citation xml:lang="en">Garfia B., Canadillas S., Canalejo A. et al. Regulation of parathyroid vitamin D receptor expression by extracellular calcium. J. Am. Soc. Nephrol. 2002; 13: 2945-2952.</mixed-citation></citation-alternatives></ref><ref id="cit105"><label>105</label><citation-alternatives><mixed-citation xml:lang="ru">Riccardi D., Hall A.E., Chattopadhyay N. et al. Localization of extracellular Ca2+/polyvalent cation-sensing protein in rat kidney. Am. J. Physiol. Renal Physiol. 1998; 274: F611-F622.</mixed-citation><mixed-citation xml:lang="en">Riccardi D., Hall A.E., Chattopadhyay N. et al. Localization of extracellular Ca2+/polyvalent cation-sensing protein in rat kidney. Am. J. Physiol. Renal Physiol. 1998; 274: F611-F622.</mixed-citation></citation-alternatives></ref><ref id="cit106"><label>106</label><citation-alternatives><mixed-citation xml:lang="ru">Riccardi D., Lee W.C., Lee K. et al. Localization of the extracellular Ca2+-sensing receptor and PTH/PTHrP receptor in rat kidney. Am. J. Physiol. Renal Fluid Electrolyte Physiol. 1996; 271: F951-F956.</mixed-citation><mixed-citation xml:lang="en">Riccardi D., Lee W.C., Lee K. et al. Localization of the extracellular Ca2+-sensing receptor and PTH/PTHrP receptor in rat kidney. Am. J. Physiol. Renal Fluid Electrolyte Physiol. 1996; 271: F951-F956.</mixed-citation></citation-alternatives></ref><ref id="cit107"><label>107</label><citation-alternatives><mixed-citation xml:lang="ru">Topala C.N., Schoeber J.P., Searchfield L.E. Activation of the Ca2+-sensing receptor stimulates the activity of the epithelial Ca2+ channel TRPV5. Cell. Calcium 2009; 45: 331-339.</mixed-citation><mixed-citation xml:lang="en">Topala C.N., Schoeber J.P., Searchfield L.E. Activation of the Ca2+-sensing receptor stimulates the activity of the epithelial Ca2+ channel TRPV5. Cell. Calcium 2009; 45: 331-339.</mixed-citation></citation-alternatives></ref><ref id="cit108"><label>108</label><citation-alternatives><mixed-citation xml:lang="ru">Renkema K.Y., Velic A., Dijkman H.B. et al. The calcium-sensing receptor promotes urinary acidification to prevent nephrolithiasis. J. Am. Soc. Nephrol. 2009; 20: 1705-1713.</mixed-citation><mixed-citation xml:lang="en">Renkema K.Y., Velic A., Dijkman H.B. et al. The calcium-sensing receptor promotes urinary acidification to prevent nephrolithiasis. J. Am. Soc. Nephrol. 2009; 20: 1705-1713.</mixed-citation></citation-alternatives></ref><ref id="cit109"><label>109</label><citation-alternatives><mixed-citation xml:lang="ru">Beierwaltes W.H. The role of calcium in the regulation of renin secretion. Am. J. Physiol. Renal Physiol. 2010; 298: F1-F11.</mixed-citation><mixed-citation xml:lang="en">Beierwaltes W.H. The role of calcium in the regulation of renin secretion. Am. J. Physiol. Renal Physiol. 2010; 298: F1-F11.</mixed-citation></citation-alternatives></ref><ref id="cit110"><label>110</label><citation-alternatives><mixed-citation xml:lang="ru">Egbuna O., Quinn S., Kantham L. et al. The full-length calcium-sensing receptor dampens the calcemic response to 1 alpha, 25(OH)2 vitamin D3 in vivo independent of parathyroid hormone. Am. J. Physiol. Renal Physiol. 2009; 297: F720-F728.</mixed-citation><mixed-citation xml:lang="en">Egbuna O., Quinn S., Kantham L. et al. The full-length calcium-sensing receptor dampens the calcemic response to 1 alpha, 25(OH)2 vitamin D3 in vivo independent of parathyroid hormone. Am. J. Physiol. Renal Physiol. 2009; 297: F720-F728.</mixed-citation></citation-alternatives></ref><ref id="cit111"><label>111</label><citation-alternatives><mixed-citation xml:lang="ru">Riccardi D., Traebert M., Ward D.T. et al. Dietary phosphate and parathyroid hormone alter the expression of calcium-sensing receptor (CaR) and the Na+-dependent Pi transporter (NaPi-2) in the rat proximal tubule. Pflugers Arch. 2000; 441: 379-387.</mixed-citation><mixed-citation xml:lang="en">Riccardi D., Traebert M., Ward D.T. et al. Dietary phosphate and parathyroid hormone alter the expression of calcium-sensing receptor (CaR) and the Na+-dependent Pi transporter (NaPi-2) in the rat proximal tubule. Pflugers Arch. 2000; 441: 379-387.</mixed-citation></citation-alternatives></ref><ref id="cit112"><label>112</label><citation-alternatives><mixed-citation xml:lang="ru">Canaff L., Hendy G.N. Human calcium-sensing receptor gene. Vitamin D response elements in promoters P1 and P2 confer transcriptional responsiveness to 1,25-dihydrovitamin D. J. Biol. Chem. 2002; 277: 30337-30350.</mixed-citation><mixed-citation xml:lang="en">Canaff L., Hendy G.N. Human calcium-sensing receptor gene. Vitamin D response elements in promoters P1 and P2 confer transcriptional responsiveness to 1,25-dihydrovitamin D. J. Biol. Chem. 2002; 277: 30337-30350.</mixed-citation></citation-alternatives></ref><ref id="cit113"><label>113</label><citation-alternatives><mixed-citation xml:lang="ru">Wang W.H., Lu M., Hebert S.C. Cytochrome P-450 metabolites mediate extracellular Ca2+-induced inhibition of apical K+ channels in the TAL. Am. J. Physiol. Cell. Physiol. 1996; 271: C103-C111.</mixed-citation><mixed-citation xml:lang="en">Wang W.H., Lu M., Hebert S.C. Cytochrome P-450 metabolites mediate extracellular Ca2+-induced inhibition of apical K+ channels in the TAL. Am. J. Physiol. Cell. Physiol. 1996; 271: C103-C111.</mixed-citation></citation-alternatives></ref><ref id="cit114"><label>114</label><citation-alternatives><mixed-citation xml:lang="ru">Sands J.M., Naruse M., Baum M. et al. Apical extracellular calcium/polyvalent cation-sensing receptor regulates vasopressinelicited water permeability in rat kidney inner medullary collecting duct. J. Clin. Invest. 1997; 99: 1399-1405.</mixed-citation><mixed-citation xml:lang="en">Sands J.M., Naruse M., Baum M. et al. Apical extracellular calcium/polyvalent cation-sensing receptor regulates vasopressinelicited water permeability in rat kidney inner medullary collecting duct. J. Clin. Invest. 1997; 99: 1399-1405.</mixed-citation></citation-alternatives></ref><ref id="cit115"><label>115</label><citation-alternatives><mixed-citation xml:lang="ru">Valenti G., Procino G., Tamma G. et al. Minireview: aquaporin 2 trafficking. Endocrinology. 2005; 146: 5063-5070.</mixed-citation><mixed-citation xml:lang="en">Valenti G., Procino G., Tamma G. et al. Minireview: aquaporin 2 trafficking. Endocrinology. 2005; 146: 5063-5070.</mixed-citation></citation-alternatives></ref><ref id="cit116"><label>116</label><citation-alternatives><mixed-citation xml:lang="ru">Pearce S.H., Williamson C., Kifor O. et al. A familial syndrome of hypocalcemia with hypercalciuria due to mutations in the calcium-sensing receptor. N. Engl. J. Med. 1996; 335: 1115-1122.</mixed-citation><mixed-citation xml:lang="en">Pearce S.H., Williamson C., Kifor O. et al. A familial syndrome of hypocalcemia with hypercalciuria due to mutations in the calcium-sensing receptor. N. Engl. J. Med. 1996; 335: 1115-1122.</mixed-citation></citation-alternatives></ref><ref id="cit117"><label>117</label><citation-alternatives><mixed-citation xml:lang="ru">Alfadda T.I., Saleh A.M.A., Houiller P., Geibel J.P. Calcium-sensing receptor 20 years later. Am. J. Physiol. Cell. Physiol. 2014; 307: C221-C231.</mixed-citation><mixed-citation xml:lang="en">Alfadda T.I., Saleh A.M.A., Houiller P., Geibel J.P. Calcium-sensing receptor 20 years later. Am. J. Physiol. Cell. Physiol. 2014; 307: C221-C231.</mixed-citation></citation-alternatives></ref><ref id="cit118"><label>118</label><citation-alternatives><mixed-citation xml:lang="ru">Kantham L., Quinn S.J., Egbuna O.I. et al. The calcium-sensing receptor (CaSR) defends against hypercalcemia independently of its regulation of parathyroid hormone secretion. Am. J. Physiol. Endocrinol. Metab. 2009; 94: 4749-4756.</mixed-citation><mixed-citation xml:lang="en">Kantham L., Quinn S.J., Egbuna O.I. et al. The calcium-sensing receptor (CaSR) defends against hypercalcemia independently of its regulation of parathyroid hormone secretion. Am. J. Physiol. Endocrinol. Metab. 2009; 94: 4749-4756.</mixed-citation></citation-alternatives></ref><ref id="cit119"><label>119</label><citation-alternatives><mixed-citation xml:lang="ru">Geibel J.P., Hebert S.C. The function and roles of the extracellular Ca2+-sensing receptor along the gastrointestinal tract. Annu. Rev. Physiol. 2009; 71: 205-217.</mixed-citation><mixed-citation xml:lang="en">Geibel J.P., Hebert S.C. The function and roles of the extracellular Ca2+-sensing receptor along the gastrointestinal tract. Annu. Rev. Physiol. 2009; 71: 205-217.</mixed-citation></citation-alternatives></ref><ref id="cit120"><label>120</label><citation-alternatives><mixed-citation xml:lang="ru">Quarles L.D., Hartle J.E 2., Siddhanti S.R. et al. A distinct cation-sensing mechanism in MC3T3-E1 osteoblasts functionally related to the calcium receptor. J. Bone Miner. Res. 1997; 12 (3): 393-402.</mixed-citation><mixed-citation xml:lang="en">Quarles L.D., Hartle J.E 2., Siddhanti S.R. et al. A distinct cation-sensing mechanism in MC3T3-E1 osteoblasts functionally related to the calcium receptor. J. Bone Miner. Res. 1997; 12 (3): 393-402.</mixed-citation></citation-alternatives></ref><ref id="cit121"><label>121</label><citation-alternatives><mixed-citation xml:lang="ru">Kameda T., Mano H., Yamada Y. et al. Calcium-sensing receptor in mature osteoclasts, which are bone-resorbing cells. Biochem. Biophys. Res. Commun. 1998; 245 (2): 419-422.</mixed-citation><mixed-citation xml:lang="en">Kameda T., Mano H., Yamada Y. et al. Calcium-sensing receptor in mature osteoclasts, which are bone-resorbing cells. Biochem. Biophys. Res. Commun. 1998; 245 (2): 419-422.</mixed-citation></citation-alternatives></ref><ref id="cit122"><label>122</label><citation-alternatives><mixed-citation xml:lang="ru">Yamaguchi T., Kifor O., Chattopadhyay N., Brown E.M. Expression of extracellular calcium (Ca2+o)-sensing receptor in the clonal osteoblast-like cell lines, UMR-106 and SAOS-2. Biochem. Biophys. Res. Commun. 1998; 243 (3): 753-757.</mixed-citation><mixed-citation xml:lang="en">Yamaguchi T., Kifor O., Chattopadhyay N., Brown E.M. Expression of extracellular calcium (Ca2+o)-sensing receptor in the clonal osteoblast-like cell lines, UMR-106 and SAOS-2. Biochem. Biophys. Res. Commun. 1998; 243 (3): 753-757.</mixed-citation></citation-alternatives></ref><ref id="cit123"><label>123</label><citation-alternatives><mixed-citation xml:lang="ru">Dvorak M.M., Siddiqua A., Ward D.T. et al. Physiological changes in extracellular calcium concentration directly control osteoblast function in the absence of calciotropic hormones. Proc. Natl. Acad. Sci. U S A. 2004; 101: 5140-5145.</mixed-citation><mixed-citation xml:lang="en">Dvorak M.M., Siddiqua A., Ward D.T. et al. Physiological changes in extracellular calcium concentration directly control osteoblast function in the absence of calciotropic hormones. Proc. Natl. Acad. Sci. U S A. 2004; 101: 5140-5145.</mixed-citation></citation-alternatives></ref><ref id="cit124"><label>124</label><citation-alternatives><mixed-citation xml:lang="ru">Chang W., Tu C., Chen T.H. et al. The extracellular calcium-sensing receptor (CaSR) is a critical modulator of skeletal development. Sci. Signal. 2008; 1 (35): 1-13.</mixed-citation><mixed-citation xml:lang="en">Chang W., Tu C., Chen T.H. et al. The extracellular calcium-sensing receptor (CaSR) is a critical modulator of skeletal development. Sci. Signal. 2008; 1 (35): 1-13.</mixed-citation></citation-alternatives></ref><ref id="cit125"><label>125</label><citation-alternatives><mixed-citation xml:lang="ru">Kovacs C.S., Ho-Pao C.L., Hunzelman J.L. et al. Regulation of murine fetal-placental calcium metabolism by the calcium-sensing receptor. J. Clin. Invest. 1998; 101: 2812-2820.</mixed-citation><mixed-citation xml:lang="en">Kovacs C.S., Ho-Pao C.L., Hunzelman J.L. et al. Regulation of murine fetal-placental calcium metabolism by the calcium-sensing receptor. J. Clin. Invest. 1998; 101: 2812-2820.</mixed-citation></citation-alternatives></ref><ref id="cit126"><label>126</label><citation-alternatives><mixed-citation xml:lang="ru">VanHouten J., Dann P., McGeoch G. et al. The calcium-sensing receptor regulates mammary gland parathyroid hormone-related protein production and calcium transport. J. Clin. Invest. 2004; 113: 598-608.</mixed-citation><mixed-citation xml:lang="en">VanHouten J., Dann P., McGeoch G. et al. The calcium-sensing receptor regulates mammary gland parathyroid hormone-related protein production and calcium transport. J. Clin. Invest. 2004; 113: 598-608.</mixed-citation></citation-alternatives></ref><ref id="cit127"><label>127</label><citation-alternatives><mixed-citation xml:lang="ru">McNeil S.E., Hobson S.A., Nipper V., Rodland K.D. Functional calcium-sensing receptors in rat fibroblasts are required for activation of SRC kinase and mitogen-activated protein kinase in response to extracellular calcium. J. Biol. Chem. 1998; 273 (2): 1114-1120.</mixed-citation><mixed-citation xml:lang="en">McNeil S.E., Hobson S.A., Nipper V., Rodland K.D. Functional calcium-sensing receptors in rat fibroblasts are required for activation of SRC kinase and mitogen-activated protein kinase in response to extracellular calcium. J. Biol. Chem. 1998; 273 (2): 1114-1120.</mixed-citation></citation-alternatives></ref><ref id="cit128"><label>128</label><citation-alternatives><mixed-citation xml:lang="ru">Bikle D.D., Ratnam A., Mauro T. et al. Changes in calcium responsiveness and handling during keratinocyte differentiation. Potential role of the calcium receptor. J. Clin. Invest. 1996; 97 (4): 1085-1093.</mixed-citation><mixed-citation xml:lang="en">Bikle D.D., Ratnam A., Mauro T. et al. Changes in calcium responsiveness and handling during keratinocyte differentiation. Potential role of the calcium receptor. J. Clin. Invest. 1996; 97 (4): 1085-1093.</mixed-citation></citation-alternatives></ref><ref id="cit129"><label>129</label><citation-alternatives><mixed-citation xml:lang="ru">Chakrabarty S., Wang H., Canaff L. et al. Calcium sensing receptor in human colon carcinoma: interaction with Ca(2+) and 1,25-dihydroxyvitamin D(3). Cancer Res. 2005; 65 (2): 493-498.</mixed-citation><mixed-citation xml:lang="en">Chakrabarty S., Wang H., Canaff L. et al. Calcium sensing receptor in human colon carcinoma: interaction with Ca(2+) and 1,25-dihydroxyvitamin D(3). Cancer Res. 2005; 65 (2): 493-498.</mixed-citation></citation-alternatives></ref><ref id="cit130"><label>130</label><citation-alternatives><mixed-citation xml:lang="ru">Chattopadhyay N., Ye C., Singh D.P. et al. Expression of extracellular calcium-sensing receptor by human lens epithelial cells. Biochem. Biophys. Res. Commun. 1997; 233 (3): 801-805.</mixed-citation><mixed-citation xml:lang="en">Chattopadhyay N., Ye C., Singh D.P. et al. Expression of extracellular calcium-sensing receptor by human lens epithelial cells. Biochem. Biophys. Res. Commun. 1997; 233 (3): 801-805.</mixed-citation></citation-alternatives></ref><ref id="cit131"><label>131</label><citation-alternatives><mixed-citation xml:lang="ru">Lin K.I., Chattopadhyay N., Bai M. et al. Elevated extracellular calcium can prevent apoptosis via the calcium-sensing receptor. Biochem. Biophys. Res. Commun. 1998; 249 (2): 325-331.</mixed-citation><mixed-citation xml:lang="en">Lin K.I., Chattopadhyay N., Bai M. et al. Elevated extracellular calcium can prevent apoptosis via the calcium-sensing receptor. Biochem. Biophys. Res. Commun. 1998; 249 (2): 325-331.</mixed-citation></citation-alternatives></ref><ref id="cit132"><label>132</label><citation-alternatives><mixed-citation xml:lang="ru">Van Den Hurk M.J., Jenks B.G., Roubos E.W., Scheenen W.J. The extracellular calcium-sensing receptor increases the number of calcium steps and action currents in pituitary melanotrope cells. Neurosci. Lett. 2005; 377 (2): 125-129.</mixed-citation><mixed-citation xml:lang="en">Van Den Hurk M.J., Jenks B.G., Roubos E.W., Scheenen W.J. The extracellular calcium-sensing receptor increases the number of calcium steps and action currents in pituitary melanotrope cells. Neurosci. Lett. 2005; 377 (2): 125-129.</mixed-citation></citation-alternatives></ref><ref id="cit133"><label>133</label><citation-alternatives><mixed-citation xml:lang="ru">Kato M., Dai R., Imamure M. et al. Calcium-evoked insulin release from insulinoma cells is mediated via calcium-sensing receptor. Surgery. 1997; 122 (6): 1203-1211.</mixed-citation><mixed-citation xml:lang="en">Kato M., Dai R., Imamure M. et al. Calcium-evoked insulin release from insulinoma cells is mediated via calcium-sensing receptor. Surgery. 1997; 122 (6): 1203-1211.</mixed-citation></citation-alternatives></ref><ref id="cit134"><label>134</label><citation-alternatives><mixed-citation xml:lang="ru">Ray J.M., Squires P.E., Curtis S.B. et al. Expression of calcium sensing receptor on human antral gastrin cells in culture. J. Clin. Invest. 1997; 99 (10): 2328-2333.</mixed-citation><mixed-citation xml:lang="en">Ray J.M., Squires P.E., Curtis S.B. et al. Expression of calcium sensing receptor on human antral gastrin cells in culture. J. Clin. Invest. 1997; 99 (10): 2328-2333.</mixed-citation></citation-alternatives></ref><ref id="cit135"><label>135</label><citation-alternatives><mixed-citation xml:lang="ru">Canaff L., Petit J.L., Kisiel M. et al. Extracellular calcium-sensing receptor is expressed in rat hepatocytes coupling to intracellular calcium mobilization and stimulation of bile flow. J. Biol. Chem. 2001; 276 (6): 4070-4079.</mixed-citation><mixed-citation xml:lang="en">Canaff L., Petit J.L., Kisiel M. et al. Extracellular calcium-sensing receptor is expressed in rat hepatocytes coupling to intracellular calcium mobilization and stimulation of bile flow. J. Biol. Chem. 2001; 276 (6): 4070-4079.</mixed-citation></citation-alternatives></ref><ref id="cit136"><label>136</label><citation-alternatives><mixed-citation xml:lang="ru">D’Souza-Li L. The calcium-sensing receptor and related diseases. Arq. Bras. Endocrinol. Metab. 2006; 50 (4): 628-639.</mixed-citation><mixed-citation xml:lang="en">D’Souza-Li L. The calcium-sensing receptor and related diseases. Arq. Bras. Endocrinol. Metab. 2006; 50 (4): 628-639.</mixed-citation></citation-alternatives></ref><ref id="cit137"><label>137</label><citation-alternatives><mixed-citation xml:lang="ru">Jahnen-Dechent W., Ketteler M. Magnesium basics. Clin. Kidney J. 2012; 5 (Suppl 1): i3-i14.</mixed-citation><mixed-citation xml:lang="en">Jahnen-Dechent W., Ketteler M. Magnesium basics. Clin. Kidney J. 2012; 5 (Suppl 1): i3-i14.</mixed-citation></citation-alternatives></ref><ref id="cit138"><label>138</label><citation-alternatives><mixed-citation xml:lang="ru">de Baaij J.H.F., Hoenderop J.G.J., Bindels R.J. Magnesium in man: implications for health and disease. Physiol. Rev. 2015; 95. 1-46.</mixed-citation><mixed-citation xml:lang="en">de Baaij J.H.F., Hoenderop J.G.J., Bindels R.J. Magnesium in man: implications for health and disease. Physiol. Rev. 2015; 95. 1-46.</mixed-citation></citation-alternatives></ref><ref id="cit139"><label>139</label><citation-alternatives><mixed-citation xml:lang="ru">Спасов А.А. Магний в медицинской практике. Волгоград, Отрок, 2000; 272 c.</mixed-citation><mixed-citation xml:lang="en">Спасов А.А. Магний в медицинской практике. Волгоград, Отрок, 2000; 272 c.</mixed-citation></citation-alternatives></ref><ref id="cit140"><label>140</label><citation-alternatives><mixed-citation xml:lang="ru">Fine K.D., Santa Ana C.A., Porter J.L., Fordtran J.S. Intestinal absorption of magnesium from food and supplements. J. Clin. Invest. 1991; 88: 396-402.</mixed-citation><mixed-citation xml:lang="en">Fine K.D., Santa Ana C.A., Porter J.L., Fordtran J.S. Intestinal absorption of magnesium from food and supplements. J. Clin. Invest. 1991; 88: 396-402.</mixed-citation></citation-alternatives></ref><ref id="cit141"><label>141</label><citation-alternatives><mixed-citation xml:lang="ru">Kerstan D., Quamme G. Physiology and pathophysiology of intestinal absorption of magnesium. In: Massry SG, Morii H, Nishizawa Y, eds. Calcium in internal medicine. Springer-Verlag London, 2002; 171-183.</mixed-citation><mixed-citation xml:lang="en">Kerstan D., Quamme G. Physiology and pathophysiology of intestinal absorption of magnesium. In: Massry SG, Morii H, Nishizawa Y, eds. Calcium in internal medicine. Springer-Verlag London, 2002; 171-183.</mixed-citation></citation-alternatives></ref><ref id="cit142"><label>142</label><citation-alternatives><mixed-citation xml:lang="ru">Konrad M., Weber S. Recent advances in molecular genetics of hereditary magnesium-losing disorders. J. Am. Soc. Nephrol. 2003; 14 (1): 249-260.</mixed-citation><mixed-citation xml:lang="en">Konrad M., Weber S. Recent advances in molecular genetics of hereditary magnesium-losing disorders. J. Am. Soc. Nephrol. 2003; 14 (1): 249-260.</mixed-citation></citation-alternatives></ref><ref id="cit143"><label>143</label><citation-alternatives><mixed-citation xml:lang="ru">Schlingmann K.P., Weber S., Peters M. et al. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family. Nat. Genet. 2002; 31 (2): 166-170.</mixed-citation><mixed-citation xml:lang="en">Schlingmann K.P., Weber S., Peters M. et al. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family. Nat. Genet. 2002; 31 (2): 166-170.</mixed-citation></citation-alternatives></ref><ref id="cit144"><label>144</label><citation-alternatives><mixed-citation xml:lang="ru">Walder R.Y., Landau D., Meyer P. et al. Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia. Nat. Genet. 2002; 31 (2): 171-174.</mixed-citation><mixed-citation xml:lang="en">Walder R.Y., Landau D., Meyer P. et al. Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia. Nat. Genet. 2002; 31 (2): 171-174.</mixed-citation></citation-alternatives></ref><ref id="cit145"><label>145</label><citation-alternatives><mixed-citation xml:lang="ru">Ryazanova L.V., Rondon L.J., Zierler S. et al. TRPM7 is essential for Mg(2+) homeostasis in mammals. Nat. Commun. 2010; 1: 109.</mixed-citation><mixed-citation xml:lang="en">Ryazanova L.V., Rondon L.J., Zierler S. et al. TRPM7 is essential for Mg(2+) homeostasis in mammals. Nat. Commun. 2010; 1: 109.</mixed-citation></citation-alternatives></ref><ref id="cit146"><label>146</label><citation-alternatives><mixed-citation xml:lang="ru">Boskey A.L., Rimnac C.M., Bansal M. et al. Effect of short-term hypomagnesemia on the chemical and mechanical properties of rat bone. J. Orthop. Res. 1992; 10 (6): 774-783.</mixed-citation><mixed-citation xml:lang="en">Boskey A.L., Rimnac C.M., Bansal M. et al. Effect of short-term hypomagnesemia on the chemical and mechanical properties of rat bone. J. Orthop. Res. 1992; 10 (6): 774-783.</mixed-citation></citation-alternatives></ref><ref id="cit147"><label>147</label><citation-alternatives><mixed-citation xml:lang="ru">Kenney M.A., McCoy H., Williams L. Effects of magnesium deficiency on strength, mass, and composition of rat femur. Calcif. Tissue Int. 1994; 54 (1): 44-49.</mixed-citation><mixed-citation xml:lang="en">Kenney M.A., McCoy H., Williams L. Effects of magnesium deficiency on strength, mass, and composition of rat femur. Calcif. Tissue Int. 1994; 54 (1): 44-49.</mixed-citation></citation-alternatives></ref><ref id="cit148"><label>148</label><citation-alternatives><mixed-citation xml:lang="ru">Liu C., Yeh J., Alola J. Magnesium directly stimulates osteoblast proliferation. J. Bone Miner. Res. 1988; 3: S104.</mixed-citation><mixed-citation xml:lang="en">Liu C., Yeh J., Alola J. Magnesium directly stimulates osteoblast proliferation. J. Bone Miner. Res. 1988; 3: S104.</mixed-citation></citation-alternatives></ref><ref id="cit149"><label>149</label><citation-alternatives><mixed-citation xml:lang="ru">Rude R.K., Gruber H.E., Norton H.J. et al. Bone loss induced by dietary magnesium reduction to 10% of the nutrient requirement in rats is associated with increased release of sub-stance P and tumor necrosis factor-alpha. J. Nutr. 2004; 134: 79-85.</mixed-citation><mixed-citation xml:lang="en">Rude R.K., Gruber H.E., Norton H.J. et al. Bone loss induced by dietary magnesium reduction to 10% of the nutrient requirement in rats is associated with increased release of sub-stance P and tumor necrosis factor-alpha. J. Nutr. 2004; 134: 79-85.</mixed-citation></citation-alternatives></ref><ref id="cit150"><label>150</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A. Laboratory evaluation of magnesium status. Renal function and free intracellular magnesium concentration. Clin. Lab. Med. 1993; 13: 209-223.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A. Laboratory evaluation of magnesium status. Renal function and free intracellular magnesium concentration. Clin. Lab. Med. 1993; 13: 209-223.</mixed-citation></citation-alternatives></ref><ref id="cit151"><label>151</label><citation-alternatives><mixed-citation xml:lang="ru">Kelepouris E., Agus Z.S. Hypomagnesemia: renal magnesium handling. Semin. Nephrol. 1998; 18: 58-73.</mixed-citation><mixed-citation xml:lang="en">Kelepouris E., Agus Z.S. Hypomagnesemia: renal magnesium handling. Semin. Nephrol. 1998; 18: 58-73.</mixed-citation></citation-alternatives></ref><ref id="cit152"><label>152</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A., de Rouffignac C. Epithelial magnesium transport and regulation by the kidney. Front. Biosci. 2000; 5: D694-D711.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A., de Rouffignac C. Epithelial magnesium transport and regulation by the kidney. Front. Biosci. 2000; 5: D694-D711.</mixed-citation></citation-alternatives></ref><ref id="cit153"><label>153</label><citation-alternatives><mixed-citation xml:lang="ru">Leliévre-Pegorier M., Merlet-Bénichou C., Roinel N., de Rouffignac C. Developmental pattern of water and electrolyte transport in the superficial nephron. Am. J. Physiol. 1983; 244: F15-F21.</mixed-citation><mixed-citation xml:lang="en">Leliévre-Pegorier M., Merlet-Bénichou C., Roinel N., de Rouffignac C. Developmental pattern of water and electrolyte transport in the superficial nephron. Am. J. Physiol. 1983; 244: F15-F21.</mixed-citation></citation-alternatives></ref><ref id="cit154"><label>154</label><citation-alternatives><mixed-citation xml:lang="ru">Wong N.L., Whiting S.J., Mizgala C.L., Quamme G.A. Electrolyte handling by the superficial nephron of the rabbit. Am. J. Physiol. 1986; 250: F590-F595.</mixed-citation><mixed-citation xml:lang="en">Wong N.L., Whiting S.J., Mizgala C.L., Quamme G.A. Electrolyte handling by the superficial nephron of the rabbit. Am. J. Physiol. 1986; 250: F590-F595.</mixed-citation></citation-alternatives></ref><ref id="cit155"><label>155</label><citation-alternatives><mixed-citation xml:lang="ru">Satoh J., Romero M.F. Ma2+ transport in the kidney. BioMetals. 2002; 15: 285-295.</mixed-citation><mixed-citation xml:lang="en">Satoh J., Romero M.F. Ma2+ transport in the kidney. BioMetals. 2002; 15: 285-295.</mixed-citation></citation-alternatives></ref><ref id="cit156"><label>156</label><citation-alternatives><mixed-citation xml:lang="ru">Suki W.N., Rouse D., Ng R.C., Kokko J.P. Calcium transport in the thick ascending limb of Henle. Heterogeneity of function in the medullary and cortical segments. J. Clin. Invest. 1980; 66: 1004-1009.</mixed-citation><mixed-citation xml:lang="en">Suki W.N., Rouse D., Ng R.C., Kokko J.P. Calcium transport in the thick ascending limb of Henle. Heterogeneity of function in the medullary and cortical segments. J. Clin. Invest. 1980; 66: 1004-1009.</mixed-citation></citation-alternatives></ref><ref id="cit157"><label>157</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A. Effect of furosemide on calcium and magnesium transport in the rat nephron. Am. J. Physiol. 1981; 241: F340-F347.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A. Effect of furosemide on calcium and magnesium transport in the rat nephron. Am. J. Physiol. 1981; 241: F340-F347.</mixed-citation></citation-alternatives></ref><ref id="cit158"><label>158</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A. Renal magnesium handling: New insights in understanding old problems. Kidney Int. 1997; 52: 1180-1195.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A. Renal magnesium handling: New insights in understanding old problems. Kidney Int. 1997; 52: 1180-1195.</mixed-citation></citation-alternatives></ref><ref id="cit159"><label>159</label><citation-alternatives><mixed-citation xml:lang="ru">Konrad M., Schaller A., Seelow D. et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am. J. Hum. Genet. 2006; 79: 949-957.</mixed-citation><mixed-citation xml:lang="en">Konrad M., Schaller A., Seelow D. et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am. J. Hum. Genet. 2006; 79: 949-957.</mixed-citation></citation-alternatives></ref><ref id="cit160"><label>160</label><citation-alternatives><mixed-citation xml:lang="ru">Efrati E., Arsentiev-Rosenfeld J., Zelikovic I. The human paracellin-1gene (hPCLN-1): renal epithelial cell-specific expression and regulation. Am. J. Physiol. Renal. Physiol. 2005; 288 (2): F272-F283.</mixed-citation><mixed-citation xml:lang="en">Efrati E., Arsentiev-Rosenfeld J., Zelikovic I. The human paracellin-1gene (hPCLN-1): renal epithelial cell-specific expression and regulation. Am. J. Physiol. Renal. Physiol. 2005; 288 (2): F272-F283.</mixed-citation></citation-alternatives></ref><ref id="cit161"><label>161</label><citation-alternatives><mixed-citation xml:lang="ru">Breiderhoff T., Himmerkus N., Stuiver M. et al. Deletion of claudin-10 (Cldn 10) in the thick ascending limb impairs paracellular sodium permeability and leads to hyper-magnesemia and nephrocalcinosis. Proc. Natl. Acad. Sci. U S A. 2012; 109: 14241-14246.</mixed-citation><mixed-citation xml:lang="en">Breiderhoff T., Himmerkus N., Stuiver M. et al. Deletion of claudin-10 (Cldn 10) in the thick ascending limb impairs paracellular sodium permeability and leads to hyper-magnesemia and nephrocalcinosis. Proc. Natl. Acad. Sci. U S A. 2012; 109: 14241-14246.</mixed-citation></citation-alternatives></ref><ref id="cit162"><label>162</label><citation-alternatives><mixed-citation xml:lang="ru">Wright F.S. Increasing magnitude of electrical potential along the renal distal tubule. Am. J. Physiol. 1971; 220: 624-638.</mixed-citation><mixed-citation xml:lang="en">Wright F.S. Increasing magnitude of electrical potential along the renal distal tubule. Am. J. Physiol. 1971; 220: 624-638.</mixed-citation></citation-alternatives></ref><ref id="cit163"><label>163</label><citation-alternatives><mixed-citation xml:lang="ru">Malnic G., Giebisch G. Some electrical properties of distal tubular epithelium in the rat. Am. J. Physiol. 1972; 223: 797-808.</mixed-citation><mixed-citation xml:lang="en">Malnic G., Giebisch G. Some electrical properties of distal tubular epithelium in the rat. Am. J. Physiol. 1972; 223: 797-808.</mixed-citation></citation-alternatives></ref><ref id="cit164"><label>164</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A., Dirks J.H. Intraluminal and contraluminal magnesium on magnesium and calcium transfer in the rat nephron. Am. J. Physiol. 1980; 238: F187-F198.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A., Dirks J.H. Intraluminal and contraluminal magnesium on magnesium and calcium transfer in the rat nephron. Am. J. Physiol. 1980; 238: F187-F198.</mixed-citation></citation-alternatives></ref><ref id="cit165"><label>165</label><citation-alternatives><mixed-citation xml:lang="ru">Dai L.J., Ritchie G., Kerstan D. et al. Magnesium transport in the renal distal convoluted tubule. Physiol. Rev. 2001; 81 (1): 51-84.</mixed-citation><mixed-citation xml:lang="en">Dai L.J., Ritchie G., Kerstan D. et al. Magnesium transport in the renal distal convoluted tubule. Physiol. Rev. 2001; 81 (1): 51-84.</mixed-citation></citation-alternatives></ref><ref id="cit166"><label>166</label><citation-alternatives><mixed-citation xml:lang="ru">Grubbs R.D. Inracellular magnesium and magnesium buffering. BioMetals. 2002; 15: 251-259.</mixed-citation><mixed-citation xml:lang="en">Grubbs R.D. Inracellular magnesium and magnesium buffering. BioMetals. 2002; 15: 251-259.</mixed-citation></citation-alternatives></ref><ref id="cit167"><label>167</label><citation-alternatives><mixed-citation xml:lang="ru">Voets T., Nilius B., Hoefs S. et al. TRPM6 forms the Mg2+ influx channel involved in intestinal and renal Mg2+ absorption. J. Biol. Chem. 2004; 279: 19-25.</mixed-citation><mixed-citation xml:lang="en">Voets T., Nilius B., Hoefs S. et al. TRPM6 forms the Mg2+ influx channel involved in intestinal and renal Mg2+ absorption. J. Biol. Chem. 2004; 279: 19-25.</mixed-citation></citation-alternatives></ref><ref id="cit168"><label>168</label><citation-alternatives><mixed-citation xml:lang="ru">Schlingmann K.P., Weber S., Peters M. et al. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family. Nat. Genet. 2002; 31 (2): 166-170.</mixed-citation><mixed-citation xml:lang="en">Schlingmann K.P., Weber S., Peters M. et al. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family. Nat. Genet. 2002; 31 (2): 166-170.</mixed-citation></citation-alternatives></ref><ref id="cit169"><label>169</label><citation-alternatives><mixed-citation xml:lang="ru">Walder R.Y., Landau D., Meyer P. et al. Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia. Nat. Genet. 2002; 31 (2): 171-174.</mixed-citation><mixed-citation xml:lang="en">Walder R.Y., Landau D., Meyer P. et al. Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia. Nat. Genet. 2002; 31 (2): 171-174.</mixed-citation></citation-alternatives></ref><ref id="cit170"><label>170</label><citation-alternatives><mixed-citation xml:lang="ru">Runnels L.W., Yue L., Clapham D.E. TRP-PLIK, a bifunctional protein with kinase and ion channel activities. Science 2001; 291 (5506): 1043-1047.</mixed-citation><mixed-citation xml:lang="en">Runnels L.W., Yue L., Clapham D.E. TRP-PLIK, a bifunctional protein with kinase and ion channel activities. Science 2001; 291 (5506): 1043-1047.</mixed-citation></citation-alternatives></ref><ref id="cit171"><label>171</label><citation-alternatives><mixed-citation xml:lang="ru">Chubanov V., Gudermann T., Schlingmann K.P. Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis. Pflugers Arch. 2005; 451 (1): 228-234.</mixed-citation><mixed-citation xml:lang="en">Chubanov V., Gudermann T., Schlingmann K.P. Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis. Pflugers Arch. 2005; 451 (1): 228-234.</mixed-citation></citation-alternatives></ref><ref id="cit172"><label>172</label><citation-alternatives><mixed-citation xml:lang="ru">Schlingmann K.P., Waldegger S., Konrad M. et al. TRPM6 and TRPM7 - Gatekeepers of human magnesium metabolism. Biochim. Biophys. Acta. 2007; 1772 (8): 813-821.</mixed-citation><mixed-citation xml:lang="en">Schlingmann K.P., Waldegger S., Konrad M. et al. TRPM6 and TRPM7 - Gatekeepers of human magnesium metabolism. Biochim. Biophys. Acta. 2007; 1772 (8): 813-821.</mixed-citation></citation-alternatives></ref><ref id="cit173"><label>173</label><citation-alternatives><mixed-citation xml:lang="ru">Groenestege W.M., Thébault S., van der Wijst J. et al. Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia. J. Clin. Invest. 2007; 117 (8): 2260-2267.</mixed-citation><mixed-citation xml:lang="en">Groenestege W.M., Thébault S., van der Wijst J. et al. Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia. J. Clin. Invest. 2007; 117 (8): 2260-2267.</mixed-citation></citation-alternatives></ref><ref id="cit174"><label>174</label><citation-alternatives><mixed-citation xml:lang="ru">Glaudemans B., Knoers N.V., Hoenderop J.G., Bindels R.J. New molecular players facilitating Mg(2+) reabsorption in the distal convoluted tubules. Kidney Int. 2010; 77 (1): 17-22.</mixed-citation><mixed-citation xml:lang="en">Glaudemans B., Knoers N.V., Hoenderop J.G., Bindels R.J. New molecular players facilitating Mg(2+) reabsorption in the distal convoluted tubules. Kidney Int. 2010; 77 (1): 17-22.</mixed-citation></citation-alternatives></ref><ref id="cit175"><label>175</label><citation-alternatives><mixed-citation xml:lang="ru">Pham P-C.T., Pham P-A.T., Pham S.V. et al. Hypomagnesemia: a clinical perspective. Int. J. Nephrol. Renovasc. Dis. 2014; 7: 219-230.</mixed-citation><mixed-citation xml:lang="en">Pham P-C.T., Pham P-A.T., Pham S.V. et al. Hypomagnesemia: a clinical perspective. Int. J. Nephrol. Renovasc. Dis. 2014; 7: 219-230.</mixed-citation></citation-alternatives></ref><ref id="cit176"><label>176</label><citation-alternatives><mixed-citation xml:lang="ru">Glaudemans B., van der Wijst J., Scola R.H. et al. A missense mutation in the Kv1.1 voltage-gated potassium channel-encoding gene KCNA1 is linked to human autosomal dominant hypomagnesemia. J. Clin. Invest. 2009; 119 (4): 936-942.</mixed-citation><mixed-citation xml:lang="en">Glaudemans B., van der Wijst J., Scola R.H. et al. A missense mutation in the Kv1.1 voltage-gated potassium channel-encoding gene KCNA1 is linked to human autosomal dominant hypomagnesemia. J. Clin. Invest. 2009; 119 (4): 936-942.</mixed-citation></citation-alternatives></ref><ref id="cit177"><label>177</label><citation-alternatives><mixed-citation xml:lang="ru">Romani A.M.P. Cellular magnesium homeostasis. Arch. Biochem. Biophys. 2011; 512 (1): 1-23.</mixed-citation><mixed-citation xml:lang="en">Romani A.M.P. Cellular magnesium homeostasis. Arch. Biochem. Biophys. 2011; 512 (1): 1-23.</mixed-citation></citation-alternatives></ref><ref id="cit178"><label>178</label><citation-alternatives><mixed-citation xml:lang="ru">Günther T., Vormann J., Förster R. Regulation of intracellular magnesium by Mg2+ efflux. Biochem. Biophys. Res. Commun. 1984; 119 (1): 124-131.</mixed-citation><mixed-citation xml:lang="en">Günther T., Vormann J., Förster R. Regulation of intracellular magnesium by Mg2+ efflux. Biochem. Biophys. Res. Commun. 1984; 119 (1): 124-131.</mixed-citation></citation-alternatives></ref><ref id="cit179"><label>179</label><citation-alternatives><mixed-citation xml:lang="ru">Günther T., Vormann J. Mg2+ efflux is accomplished by an amiloride-sensitive Na+/Mg2+ antiport. Biochem. Biophys. Res. Commun. 1985; 130 (2): 540-545.</mixed-citation><mixed-citation xml:lang="en">Günther T., Vormann J. Mg2+ efflux is accomplished by an amiloride-sensitive Na+/Mg2+ antiport. Biochem. Biophys. Res. Commun. 1985; 130 (2): 540-545.</mixed-citation></citation-alternatives></ref><ref id="cit180"><label>180</label><citation-alternatives><mixed-citation xml:lang="ru">Féray J.C., Garay R. A Na+-stimulated Mg2+-transport system in human red blood cells. Biochem. Biophys. Acta. 1986; 856 (1): 76-84.</mixed-citation><mixed-citation xml:lang="en">Féray J.C., Garay R. A Na+-stimulated Mg2+-transport system in human red blood cells. Biochem. Biophys. Acta. 1986; 856 (1): 76-84.</mixed-citation></citation-alternatives></ref><ref id="cit181"><label>181</label><citation-alternatives><mixed-citation xml:lang="ru">Lüdi H., Schatzmann H.J. Some properties of a system for sodium-dependent outward movement of magnesium from metabolizing human red blood cells. J.Physiol. 1987; 390: 367-382.</mixed-citation><mixed-citation xml:lang="en">Lüdi H., Schatzmann H.J. Some properties of a system for sodium-dependent outward movement of magnesium from metabolizing human red blood cells. J.Physiol. 1987; 390: 367-382.</mixed-citation></citation-alternatives></ref><ref id="cit182"><label>182</label><citation-alternatives><mixed-citation xml:lang="ru">Flatman P.W., Smith L.M. Magnesium transport in ferret red cells. J. Physiol. 1990; 431: 11-25.</mixed-citation><mixed-citation xml:lang="en">Flatman P.W., Smith L.M. Magnesium transport in ferret red cells. J. Physiol. 1990; 431: 11-25.</mixed-citation></citation-alternatives></ref><ref id="cit183"><label>183</label><citation-alternatives><mixed-citation xml:lang="ru">Xu W., Willis J.S. Sodium transport through the amiloride-sensitive Na-Mg pathway of hamster red cells. J. Membr. Biol. 1994; 141 (3): 277-287.</mixed-citation><mixed-citation xml:lang="en">Xu W., Willis J.S. Sodium transport through the amiloride-sensitive Na-Mg pathway of hamster red cells. J. Membr. Biol. 1994; 141 (3): 277-287.</mixed-citation></citation-alternatives></ref><ref id="cit184"><label>184</label><citation-alternatives><mixed-citation xml:lang="ru">Romani A., Mafella C., Scarpa A. Regulation of magnesium uptake and release in the heart and in isolated ventricular myocytes. Circ. Res. 1993; 72 (6): 1139-1148.</mixed-citation><mixed-citation xml:lang="en">Romani A., Mafella C., Scarpa A. Regulation of magnesium uptake and release in the heart and in isolated ventricular myocytes. Circ. Res. 1993; 72 (6): 1139-1148.</mixed-citation></citation-alternatives></ref><ref id="cit185"><label>185</label><citation-alternatives><mixed-citation xml:lang="ru">Fagan T.E., Romani A. Activation of Na(+)- and Ca(2+)-dependent Mg(2+) extrusion by alpha(1)- and beta-adrenergic agonists in rat liver cells. Am. J. Physiol. Gastrointest. Liver Physiol. 2000; 279 (5): G943-G950.</mixed-citation><mixed-citation xml:lang="en">Fagan T.E., Romani A. Activation of Na(+)- and Ca(2+)-dependent Mg(2+) extrusion by alpha(1)- and beta-adrenergic agonists in rat liver cells. Am. J. Physiol. Gastrointest. Liver Physiol. 2000; 279 (5): G943-G950.</mixed-citation></citation-alternatives></ref><ref id="cit186"><label>186</label><citation-alternatives><mixed-citation xml:lang="ru">Günther T., Vormann J. Activation of Na+/Mg2+ antiport in thymocytes by cAMP. FEBS Lett. 1992; 297 (1-2): 132-134.</mixed-citation><mixed-citation xml:lang="en">Günther T., Vormann J. Activation of Na+/Mg2+ antiport in thymocytes by cAMP. FEBS Lett. 1992; 297 (1-2): 132-134.</mixed-citation></citation-alternatives></ref><ref id="cit187"><label>187</label><citation-alternatives><mixed-citation xml:lang="ru">Wolf F.I., Di Francesco A., Covacci V. et al. Regulation of intracellular magnesium in ascites cells: involvement of different regulatory pathways. Arch. Biochem. Biophys. 1996; 331 (2): 194-200.</mixed-citation><mixed-citation xml:lang="en">Wolf F.I., Di Francesco A., Covacci V. et al. Regulation of intracellular magnesium in ascites cells: involvement of different regulatory pathways. Arch. Biochem. Biophys. 1996; 331 (2): 194-200.</mixed-citation></citation-alternatives></ref><ref id="cit188"><label>188</label><citation-alternatives><mixed-citation xml:lang="ru">Fagan T.E., Romani A. alpha(1)-Adrenoceptor-induced Mg2+ extrusion from rat hepatocytes occurs via Na+-dependent transport mechanism. Am. J. Physiol. Gastrointest. Liver Physiol. 2001; 280 (6): G1145-G1156.</mixed-citation><mixed-citation xml:lang="en">Fagan T.E., Romani A. alpha(1)-Adrenoceptor-induced Mg2+ extrusion from rat hepatocytes occurs via Na+-dependent transport mechanism. Am. J. Physiol. Gastrointest. Liver Physiol. 2001; 280 (6): G1145-G1156.</mixed-citation></citation-alternatives></ref><ref id="cit189"><label>189</label><citation-alternatives><mixed-citation xml:lang="ru">Cefaratti C., Romani A.M. Functional characterization of two distinct Mg(2+) extrusion mechanisms in cardiac sarcolemmal vesicles. Mol. Cell. Biochem. 2007; 303 (1-2): 63-72.</mixed-citation><mixed-citation xml:lang="en">Cefaratti C., Romani A.M. Functional characterization of two distinct Mg(2+) extrusion mechanisms in cardiac sarcolemmal vesicles. Mol. Cell. Biochem. 2007; 303 (1-2): 63-72.</mixed-citation></citation-alternatives></ref><ref id="cit190"><label>190</label><citation-alternatives><mixed-citation xml:lang="ru">Cefaratti C., Ruse C. Protein kinase A dependent phosphorylation activates Mg2+ efflux in the basolateral region of the liver. Mol. Cell. Biochim. 2007; 297 (1-2): 209-214.</mixed-citation><mixed-citation xml:lang="en">Cefaratti C., Ruse C. Protein kinase A dependent phosphorylation activates Mg2+ efflux in the basolateral region of the liver. Mol. Cell. Biochim. 2007; 297 (1-2): 209-214.</mixed-citation></citation-alternatives></ref><ref id="cit191"><label>191</label><citation-alternatives><mixed-citation xml:lang="ru">Günther T. Mechanisms and regulation of Mg2+ efflux and Mg2+ influx. Miner, Electrolyte Metab. 1993; 19 (4-5): 259-265.</mixed-citation><mixed-citation xml:lang="en">Günther T. Mechanisms and regulation of Mg2+ efflux and Mg2+ influx. Miner, Electrolyte Metab. 1993; 19 (4-5): 259-265.</mixed-citation></citation-alternatives></ref><ref id="cit192"><label>192</label><citation-alternatives><mixed-citation xml:lang="ru">Ebel H., Hollstein M., Gunther T. Role on the choline exchanger in Na(+)-independent Mg(2+) efflux from rat erythrocytes. Biochim. Biophys. Acta. 2002; 1559 (2): 135-144.</mixed-citation><mixed-citation xml:lang="en">Ebel H., Hollstein M., Gunther T. Role on the choline exchanger in Na(+)-independent Mg(2+) efflux from rat erythrocytes. Biochim. Biophys. Acta. 2002; 1559 (2): 135-144.</mixed-citation></citation-alternatives></ref><ref id="cit193"><label>193</label><citation-alternatives><mixed-citation xml:lang="ru">Stuiver M., Lainez S., Will C. et al. CNNM2, encoding a basolateral protein required for renal Mg2+ handling, is mutated in dominant hypomagnesemia. Am. J. Hum. Genet. 2011; 88 (3): 333-343.</mixed-citation><mixed-citation xml:lang="en">Stuiver M., Lainez S., Will C. et al. CNNM2, encoding a basolateral protein required for renal Mg2+ handling, is mutated in dominant hypomagnesemia. Am. J. Hum. Genet. 2011; 88 (3): 333-343.</mixed-citation></citation-alternatives></ref><ref id="cit194"><label>194</label><citation-alternatives><mixed-citation xml:lang="ru">de Baaij J.H., Stuiver M., Meij I.C. et al. Membrane topology and intracellular processing of cyclin M2 (CNNM2). J. Biol. Chem. 2012; 287 (17): 13644-13655.</mixed-citation><mixed-citation xml:lang="en">de Baaij J.H., Stuiver M., Meij I.C. et al. Membrane topology and intracellular processing of cyclin M2 (CNNM2). J. Biol. Chem. 2012; 287 (17): 13644-13655.</mixed-citation></citation-alternatives></ref><ref id="cit195"><label>195</label><citation-alternatives><mixed-citation xml:lang="ru">Wang C.Y., Shi J.D., Yang P. et al. Molecular cloning and characterization of a novel gene family of four ancient conserved domain proteins (ACDP). Gene. 2003; 306: 37-44.</mixed-citation><mixed-citation xml:lang="en">Wang C.Y., Shi J.D., Yang P. et al. Molecular cloning and characterization of a novel gene family of four ancient conserved domain proteins (ACDP). Gene. 2003; 306: 37-44.</mixed-citation></citation-alternatives></ref><ref id="cit196"><label>196</label><citation-alternatives><mixed-citation xml:lang="ru">Wang C.Y., Yang P., Shi J.D. et al. Molecular cloning and characterization of the mouse Acdp gene family. BMC Genomics. 2004; 5: 7.</mixed-citation><mixed-citation xml:lang="en">Wang C.Y., Yang P., Shi J.D. et al. Molecular cloning and characterization of the mouse Acdp gene family. BMC Genomics. 2004; 5: 7.</mixed-citation></citation-alternatives></ref><ref id="cit197"><label>197</label><citation-alternatives><mixed-citation xml:lang="ru">Goytain A., Quamme G.A. Functional characterization of ACDP2 (ancient conserved domain protein, a divalent metal transporter. Physiol. Genomics. 2005; 22: 382-389.</mixed-citation><mixed-citation xml:lang="en">Goytain A., Quamme G.A. Functional characterization of ACDP2 (ancient conserved domain protein, a divalent metal transporter. Physiol. Genomics. 2005; 22: 382-389.</mixed-citation></citation-alternatives></ref><ref id="cit198"><label>198</label><citation-alternatives><mixed-citation xml:lang="ru">Quamme G.A. Control of magnesium transport in the thick ascending limb. Am. J. Physiol. 1989; 256: F197-F210.</mixed-citation><mixed-citation xml:lang="en">Quamme G.A. Control of magnesium transport in the thick ascending limb. Am. J. Physiol. 1989; 256: F197-F210.</mixed-citation></citation-alternatives></ref><ref id="cit199"><label>199</label><citation-alternatives><mixed-citation xml:lang="ru">Dai L.J., Quamme G.A. Intracellular Mg2+ and magnesium depletion in isolated renal thick ascending limb cells. J. Clin. Invest. 1991; 88: 1255-1264.</mixed-citation><mixed-citation xml:lang="en">Dai L.J., Quamme G.A. Intracellular Mg2+ and magnesium depletion in isolated renal thick ascending limb cells. J. Clin. Invest. 1991; 88: 1255-1264.</mixed-citation></citation-alternatives></ref><ref id="cit200"><label>200</label><citation-alternatives><mixed-citation xml:lang="ru">Dai L.J., Bapty B.W., Ritchie G., Quamme G.A. PGE2 stimulates Mg2+ uptake in mouse distal convoluted tubule cells. Am. J. Physiol. Renal Physiol. 1998. 275: F833-F839.</mixed-citation><mixed-citation xml:lang="en">Dai L.J., Bapty B.W., Ritchie G., Quamme G.A. PGE2 stimulates Mg2+ uptake in mouse distal convoluted tubule cells. Am. J. Physiol. Renal Physiol. 1998. 275: F833-F839.</mixed-citation></citation-alternatives></ref><ref id="cit201"><label>201</label><citation-alternatives><mixed-citation xml:lang="ru">Dai L.J., Bapty B.W., Ritchie G. et al.Insulin stimulates Mg2+ uptake in mouse distal convoluted tubule cells. Am. J. Physiol. Renal Physiol. 1999. 277: F907-F913.</mixed-citation><mixed-citation xml:lang="en">Dai L.J., Bapty B.W., Ritchie G. et al.Insulin stimulates Mg2+ uptake in mouse distal convoluted tubule cells. Am. J. Physiol. Renal Physiol. 1999. 277: F907-F913.</mixed-citation></citation-alternatives></ref><ref id="cit202"><label>202</label><citation-alternatives><mixed-citation xml:lang="ru">Yang T., Hassan S., Huang Y.G. et al. Expression of PTHrP, PTH/PTHrP receptor and Ca2+ sensing receptor along the rat nephron. Am. J. Physiol. Renal Physiol. 1997; 272: F751-F758.</mixed-citation><mixed-citation xml:lang="en">Yang T., Hassan S., Huang Y.G. et al. Expression of PTHrP, PTH/PTHrP receptor and Ca2+ sensing receptor along the rat nephron. Am. J. Physiol. Renal Physiol. 1997; 272: F751-F758.</mixed-citation></citation-alternatives></ref><ref id="cit203"><label>203</label><citation-alternatives><mixed-citation xml:lang="ru">Bapty B.W., Dai L.J, Ritchie G. et al. Extracellular Mg2+ and Ca2+ sensing in mouse distal convoluted tubule cells. Kidney Int. 1998; 53: 583-592.</mixed-citation><mixed-citation xml:lang="en">Bapty B.W., Dai L.J, Ritchie G. et al. Extracellular Mg2+ and Ca2+ sensing in mouse distal convoluted tubule cells. Kidney Int. 1998; 53: 583-592.</mixed-citation></citation-alternatives></ref><ref id="cit204"><label>204</label><citation-alternatives><mixed-citation xml:lang="ru">Braüner-Osborne H., Jensen A.A., Sheppard P.O. et al. The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain. J. Biol. Chem. 1999; 274 (26): 18382-18386.</mixed-citation><mixed-citation xml:lang="en">Braüner-Osborne H., Jensen A.A., Sheppard P.O. et al. The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain. J. Biol. Chem. 1999; 274 (26): 18382-18386.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
