References

nid

Нефрология и диализ

Nephrology and Dialysis

1680-44222618-9801

Российское диализное общество

nid-1975

Research Article

ОБЗОРЫ И ЛЕКЦИИ

REVIEWS AND LECTURES

Апоптоз - физиология и патология (Обзор литературы)

Apoptosis - physiology and pathology

Паунова

С. С.

Paunova

S. S.

noemail@neicon.ru

Российский государственный медицинский университет, МоскваRussian Federation

2004

27062025

62132137

2025

Паунова С.С.

Paunova S.S.

Данная работа распространяется под лицензией Creative Commons Attribution 4.0.

This work is licensed under a Creative Commons Attribution 4.0 License.

https://journal.nephro.ru/jour/article/view/1975

Апоптоз, или запрограммированная гибель клетки (ЗГК), является естественным физиологическим процессом, представляющим собой основной компонент эмбриогенеза, морфогенеза и роста тканей, необходимый для поддержания нормального тканевого гомеостаза. Наряду с этим известна роль апоптоза в ряде патологических состояний, таких, как злокачественные новообразования, синдром приобретенного иммунодефицита, некоторые нейродегенеративные и аутоиммунные заболевания, инфекционные процессы. Апоптоз регулируется комплексом генетических, молекулярных, биохимических факторов, наиболее важными из которых являются рецепторы гибели клетки, каспазы, митохондрии, семейство Bcl-2 протоонкогенов, отдельные опухоль-подавляющие гены. Изучение молекулярного механизма апоптоза и его регуляции способствует более глубокому и полному пониманию патофизиологии множества заболеваний, что, в свою очередь, необходимо для выработки новых подходов к лечению этих состояний.

Apoptopsis (programmed cell death) occurs normally for maintenance of a tissue homeostasis and plays an important role in morphogenesis, embryogenesis and tissue growth. On the other hand apoptosis may be involved in different pathological processes such as malignancy, infectious diseases and autoimmune disorders. Apoptosis is regulated by various mediators. Caspases, death receptors, mitochondria, Bcl-2 protooncogenes and tumor suppressor genes are considered to be the most important of them. Advances in apoptosis regulation research suggest new options for therapy of wide range of human pathologies.

апоптозкаспазымитохондриисемейство Bcl-2 протоонкогеновFas (C95APO-1)-рецепторыTNF-рецепторы

References1

Галанкин В.Н., Токмаков А.М. Проблемы воспаления с позиций теории и практики. М.: УДН, 1991: 1-120.

Зайчик А.Ш., Чурилов Л.П. Основы общей патологии. СПб., 1999: 1-618.

Мохиль-Дейн А.Х., Белушкина Н.Н., Петрова У.Н. и др. Исследование уровня апоптоза и экспрессии Fas и Fas-L в лейкоцитах периферической крови у детей, больных системной красной волчанкой. Вопр. биол. мед. и фармац. химии 2003; 2: 28-32.

Новиков В.С. (ред.). Программированная клеточная гибель. СПб.: Наука, 1996: 1-276.

Adams J.M., Cory S. The Bcl-2 protein family: Arbiters of cell survival [review]. Science 1998; 281: 1322-1326.

Alnemri E.S., Livingston D.J., Nicholson D.W. et al. Human ICE/CED-3 protease nomenclature [letter]. Cell 1996; 87: 171.

Antonsson B., Conti F., Ciavatta A. et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997; 277: 370-372.

Arends M.J., Morris R.G., Wyllie A.H. Apoptosis. The role of the endonuclease. Am J Pathol 1990; 136: 593-608.

Ashkenazi A., Dixit V.M. Death receptors: Signaling and modulation. Science 1998; 281: 1305-1308.

Bauer G. Reactive oxygen and nitrogen species: Efficient, selective, and interactive signals during intercellular induction of apoptosis. Anticancer Res 2000; 20: 4115-4139.

Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORTl/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996; 85: 803-815.

Bonegio R., Lieberthal W. Role of apoptosis in the pathogenesis of acute renal failure. Curr Opin Nephrol Hypertens 2002 May; 11 (3): 301-308.

Bossy W.E., Newmeyer D.D., Green D.R. Mitochondrial cytochrome C release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 1998; 17: 37-49.

Chertin B., Rolle U., Farkas, Puri P. The role of nitric oxide in reflux nephropathy. Pediatr Surg Int 2002; 18: 630-634.

Chevalier R.L., Smith C.D., Wolstenholme J., Kraevski S., Reed J.C. Chronic ureteral obstruction in the rat suppresses renal tubular Bcl-2 and stimulates apoptosis. Exp Nephrol 2000 Mar-Apr; 8 (2): 115-122.

Cleary M.L., Smith S.D., Sklar J. Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14; 18) translocation. Cell 1986; 47: 19-28.

Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. J Physiol 2000; 529 Pt 1: 11-21.

Di Leonardo A., Linke S.P., Clarkin K., Wahl G.M. DNA damage triggers a prolonged p53-dependent Gl arrest and long-term induction of Cipl in normal human fibroblasts. Genes Dev 1994; 8: 2540-2551.

Drappa J., Vaishnaw A.K., Sullivan K.E. et al. Fas gene mutations in the Canale-Smith syndrome, an inherited lymphoproliferative disorder associated with autoimmunity. N Engl J Med 1996; 335: 1643-1649.

El Mouedden M., Guy Laurent G., Mingeot-Leclercq M.-P. et al. Apoptosis in renal proximal tubules of rats treated with low doses of aminoglycosides, Antimicrobial Agents and Chemotherapy 2000 March; 44 (3): 665-675.

Ellis R.E., Jacobson D.M., Horvitz H.R. Genes required for the engulfment of cell corpses during programmed cell death in Caenorhabditis elegans. Genetics 1991; 129: 79-94.

Evan G., Littlewood T. A matter of life and cell death. Science 1998; 281: 1317-1322.

Fisher T.C., Milner A.E., Gregory C.D. et al. Bcl-2 modulation of apoptosis induced by anticancer drugs: Resistance to thymidylate stress is independent of classical resistance pathways. Cancer Res 1993; 53: 3321-3326.

Flemming W. Ueber die Bildung von Richtungsfiguren in Sa’ugethier-eiern beim Untergang Graaf’scher Follikel [German]. Archiv fur Anatomic und Physiologic 1885; 221-244.

Fraser A., Evan G. A license to kill. Cell 1996; 85: 781-784.

Gajewski T.F., Thompson C.B. Apoptosis meets signal transduction: Elimination of a BAD influence [comment]. Cell 1996; 87: 589-592.

Georgescu L., Vakkalanka R.K., Elkon K.B., Crow M.K. Interleukin-10 promotes activation-induced cell death of SLE lymphocytes mediated by Fas ligand. J Clin Invest 1997; 100: 2622-2633.

Green D., Kroemer G. The central executioners of apoptosis: Caspases or mitochondria? Trends Cell Biol 1998; 8: 267-271.

Green D.R., Reed J.C. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.

Greenberg A.H. Activation of apoptosis pathways by granzyme B. Cell Death Differ 1996; 3: 269-274.

Grodzicky T., Elkon K.B. Apoptosis:a case where too much or to little can lead to autoimmunity. The Mount Sinaj J Med 2002; 69 (4): 208-219.

Hague A., Moorghen M., Hicks D. et al. BCL-2 expression in human colorectal adenomas and carcinomas. Oncogene 1994; 9: 3367-3370.

Hansen R., Oren M. p53; from inductive signal to cellular effect. Curr Opin Genet Dev 1997; 7: 46-51.

Hauser P., Oberbauer R. Tubular apoptosis in the pathophysiology of renal disease, Wein Klin Wochenschr 2002 Aug 30; 114 (15-16): 671-677.

Heimbrook D.C., Oliff A. Therapeutic intervention and signaling. Curr Opin Cell Biol 1998; 10: 284-288.

Hersey P., Zhang X.D. Overcoming resistance of cancer cells to apoptosis. J Cell Physiol 2003 Jul; 196 (1): 9-18.

Hortelano S., Alvarez A.M., Bosca L. Nitric oxide induces tyrosine nitration and release of cytochrome C preceding an increase of mitochondrial transmembrane potential in macrophages. FASEB J 1999; 13: 2311-2317.

Hsu H., Xiong J., Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell 1995; 81: 495-504.

Hsu H., Shu H.B., Pan M.G., Goeddel D.V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 1996; 84: 299-308.

Humke E.W., Ni J., Dixit V.M. ERICE, a novel FLICE-activatable caspase. J Biol Chem 1998; 273: 15702-15707.

Israels L., Israels E. Apoptosis. The Oncologist Aug 1999; 4 (4): 332-339.

Jurgensmeier J.M., Xie Z., Deveraux Q. et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc Natl Acad Sci USA 1998; 95: 4997-5002.

Kashihara N., Sugiyama H., Makino H. Mechanism for induction of apoptosis and glomerular diseases. Nephrol Dial Transplant 1999; 14 (suppl 1): 52-54.

Kashihara N., Sugiyama H., Makino H. Implication of apoptosis in progression of renal disease. Contrib Nephrol 2003; 139: 156-172.

Kerr J.F., Wyllie A.H., Currie A.R. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26: 239-257.

Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome C from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 1132-1136.

Kroemer G. The protooncogene Bcl-2 and its role in regulating apoptosis. Nat Med 1997; 3: 614-620.

Leon L.R., Kozak W., Kluger M.J. Role of IL-10 in inflammation. Studies using cytokine knockout mice. Ann N Y Acad Sci 1998; 856: 69-75.

Li J., Billiar T.R. The role of nitric oxide in apoptosis. Semin Perinatol 2000; 24: 46-50.

Li P., Nijhawan D., Budihardjo I. et al. Cytochrome С and dATP-dependent formation of Apaf-l/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-489.

Liaudet L., Soriano F.G., Szabo C. Biology of nitric oxide signaling. Crit Care Med 2000; 28 (Suppl): N37-N52.

Lowe S.W., Schmitt E.M., Smith S.W. et al. p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 1993; 362: 847-849.

Lutz J., Zou H., Antus B., Heemanu U. Apoptosis and treatment of chronic allograft nephropathy with everolimus. Transplantation 2003 Aug 15; 76 (3): 508-515.

Mannick J.B., Hausladen A., Liu L. et al. Fas-induced caspase denitrosylation. Science 1999; 284: 651-654.

Margulis L. Archaeal-eubacterial mergers in the origin of Eukarya: Phylogenetic classification of life. Proc Natl Acad Sci USA 1996; 93: 1071-1076.

McDonnell T.J., Troncoso P., Brisbay S.M. et al. Expression of the protooncogene bcl-2 in the prostate and its association with emergence of androgen-independent prostate cancer. Cancer Res 1992; 52: 6940-6944.

Muzio M., Stockwell B.R., Stennicke H.R. et al. An induced proximity model for caspase-8 activation. J Biol Chem 1998; 273: 2926-2930.

Nagata S., Golstein P. The Fas death factor. Science 1995; 267:1449-1456.

Nagata S. Apoptosis by death factor. Cell 1997; 88: 355-365.

Nash P.B., Purner M.B., Leon R.P., Clarke P., Duke R.C., Curiel T.J. Toxoplasma gondii-Infected Cells Are Resistant to Multiple Inducers of Apoptosis. J Immunol Feb160, 1998: 1824-1830.

Nicholson D.W., Thornberry N.A. Apoptosis. Life and death decisions. Science 2003 Jan 10; 299 (5604): 214-215.

Nicholson D.W., Thornberry N.A. Caspases: Killer proteases. Trends Biochem Sci 1997; 22: 299-306.

Nitsch D.D., Ghilardi N., Muhl H. et al. Apoptosis and expression of inducible nitric oxide synthase are mutually exclusive in renal mesangial cells. Am J Pathol 1997; 150: 889-900.

Perfettini J.L., Gissot M., Souque P., Ojcius D.M. Modulation of apoptosis during infection with Chlamydia. Methods Enzymol 2002; 358: 334-344.

Petit P.X., Susin S.A., Zamzami N. et al. Mitochondria and programmed cell death: Back to the future. FEES Lett 1996; 396: 7-13.

Pomerantz J., Schreiber A.N., Liegeois N.J. et al. The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2’s inhibition of p53. Cell 1998; 92: 713-723.

Reed J.C. Bcl-2 family proteins. Oncogene 1998; 17: 3225-3226.

Rotonda J., Nicholson D.W., Fazil K.M. et al. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat Struct Biol 1996; 3: 619-625.

Salmaso C., Olive D., Pesce G., Bagnasco M. Costimulatory molecules and autoimmune thyroid diseases. Autoimmunity 2002 May; 35 (3): 159-167.

Savill J., Fadok V., Henson P., Haslett C. Phagocyte recognition of cells undergoing apoptosis [review]. Immunol Today 1993; 14: 131-136.

Savill J., Fadok V. Corpse clearance defines the meaning of cell death. Nature 2000; 407: 784-788.

Sertachius E., Sundelin B., Eklof A.C. et al. Pyelonephritis provokes growth retardation and apoptosis in infant rat renal cortex. Kidney Int 1997 Jun; 51 (6): 1855-1862.

Sherr C.J. Cancer cell cycles. Science 1996; 274: 1672-1677.

Simonian P.L., Grillot D.A., Nunez G. Bcl-2 and Bel-XL can differentially block chemotherapy-induced cell death. Blood 1997; 90: 1208-1216.

Singh V.K., Mehrotra S., Narayan P. et al. Modulation of autoimmune diseases by nitric oxide. Immunol Res 2000; 22: 1-19.

Smith C.A., Farrah T., Goodwin R.G. The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death. Cell 1994; 76: 959-962.

Steller H. Mechanisms and genes of cellular suicide. Science 1995; 267: 1445-1449.

Strasser A., Huang D.C., Vaux D.L. The role of the bcl-2/ced-9 gene family in cancer and general implications of defects in cell death control for tumourоgenesis and resistance to chemotherapy. Biochim Biophys Acta 1997; 1333: F151-F178.

Tartaglia L.A., Goeddel D.V. Two TNF receptors. Immunol Today 1992; 13: 151-153.

Thome M., Schneider P., Hofmann K. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 1997; 386: 517-521.

Thornberry N.A., Lazebnik Y. Caspases: Enemies within. Science 1998; 281: 1312-1316.

Thornberry N.A., Rano T.A., Peterson E.P. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 1997; 272: 17907-17911.

Tsujimoto Y., Gorham J., Cossman J. et al. The t(14; 18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining. Science 1985; 229: 1390-1393.

Tsujimoto Y., Shimizu S. Bcl-2 family: Life-or-death switch. FEES Lett 2000; 466: 6-10.

Uren A.G., Coulson E.J., Vaux D.L. Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts. Trends Biochem Sci 1998; 23: 159-162.

Yang X., Khosravi F.R., Chang H.Y., Baltimore D. Daxx, a novel Fas-binding protein that activates INK and apoptosis. Cell 1997; 89: 1067-1076.

Zamora R., Vodovotz Y., Billiar T.R. Inducible nitric oxide synthase and inflammatory diseases. Mol Med 2000; 6: 347-373.

Zamzami N., Susin S.A., Marchetti P. et al. Mitochondrial control of nuclear apoptosis. J Exp Med 1996; 183: 1533-1544.

The authors declare that there are no conflicts of interest present.