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Том 6 №2 2004 год - Нефрология и диализ

Апоптоз - физиология и патология (Обзор литературы)

Паунова С.С.

Аннотация: 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.

Для цитирования: Паунова С.С. Апоптоз - физиология и патология (Обзор литературы). Нефрология и диализ. 2004. 6(2):132-137. doi:

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Ключевые слова: апоптоз, каспазы, митохондрии, семейство Bcl-2 протоонкогенов, Fas (C95,APO-1)-рецепторы, TNF-рецепторы

Список литературы:

1. Галанкин В.Н., Токмаков А.М. Проблемы воспаления с позиций теории и практики. М.: УДН, 1991: 1-120.
2. Зайчик А.Ш., Чурилов Л.П. Основы общей патологии. СПб., 1999: 1-618.
3. 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.
4. Новиков В.С. (ред.). Программированная клеточная гибель. СПб.: Наука, 1996: 1-276.
5. Adams J.M., Cory S. The Bcl-2 protein family: Arbiters of cell survival [review]. Science 1998; 281: 1322-1326.
6. Alnemri E.S., Livingston D.J., Nicholson D.W. et al. Human ICE/CED-3 protease nomenclature [letter]. Cell 1996; 87: 171.
7. Antonsson B., Conti F., Ciavatta A. et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997; 277: 370-372.
8. Arends M.J., Morris R.G., Wyllie A.H. Apoptosis. The role of the endonuclease. Am J Pathol 1990; 136: 593-608.
9. Ashkenazi A., Dixit V.M. Death receptors: Signaling and modulation. Science 1998; 281: 1305-1308.
10. Bauer G. Reactive oxygen and nitrogen species: Efficient, selective, and interactive signals during intercellular induction of apoptosis. Anticancer Res 2000; 20: 4115-4139.
11. 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.
12. Bonegio R., Lieberthal W. Role of apoptosis in the pathogenesis of acute renal failure. Curr Opin Nephrol Hypertens 2002 May; 11 (3): 301-308.
13. 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.
14. Chertin B., Rolle U., Farkas, Puri P. The role of nitric oxide in reflux nephropathy. Pediatr Surg Int 2002; 18: 630-634.
15. 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.
16. 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.
17. Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. J Physiol 2000; 529 Pt 1: 11-21.
18. 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.
19. 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.
20. 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.
21. 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.
22. Evan G., Littlewood T. A matter of life and cell death. Science 1998; 281: 1317-1322.
23. 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.
24. 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.
25. Fraser A., Evan G. A license to kill. Cell 1996; 85: 781-784.
26. Gajewski T.F., Thompson C.B. Apoptosis meets signal transduction: Elimination of a BAD influence [comment]. Cell 1996; 87: 589-592.
27. 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.
28. Green D., Kroemer G. The central executioners of apoptosis: Caspases or mitochondria? Trends Cell Biol 1998; 8: 267-271.
29. Green D.R., Reed J.C. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
30. Greenberg A.H. Activation of apoptosis pathways by granzyme B. Cell Death Differ 1996; 3: 269-274.
31. 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.
32. Hague A., Moorghen M., Hicks D. et al. BCL-2 expression in human colorectal adenomas and carcinomas. Oncogene 1994; 9: 3367-3370.
33. Hansen R., Oren M. p53; from inductive signal to cellular effect. Curr Opin Genet Dev 1997; 7: 46-51.
34. Hauser P., Oberbauer R. Tubular apoptosis in the pathophysiology of renal disease, Wein Klin Wochenschr 2002 Aug 30; 114 (15-16): 671-677.
35. Heimbrook D.C., Oliff A. Therapeutic intervention and signaling. Curr Opin Cell Biol 1998; 10: 284-288.
36. Hersey P., Zhang X.D. Overcoming resistance of cancer cells to apoptosis. J Cell Physiol 2003 Jul; 196 (1): 9-18.
37. 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.
38. 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.
39. 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.
40. Humke E.W., Ni J., Dixit V.M. ERICE, a novel FLICE-activatable caspase. J Biol Chem 1998; 273: 15702-15707.
41. Israels L., Israels E. Apoptosis. The Oncologist Aug 1999; 4 (4): 332-339.
42. 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.
43. Kashihara N., Sugiyama H., Makino H. Mechanism for induction of apoptosis and glomerular diseases. Nephrol Dial Transplant 1999; 14 (suppl 1): 52-54.
44. Kashihara N., Sugiyama H., Makino H. Implication of apoptosis in progression of renal disease. Contrib Nephrol 2003; 139: 156-172.
45. 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.
46. 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.
47. Kroemer G. The protooncogene Bcl-2 and its role in regulating apoptosis. Nat Med 1997; 3: 614-620.
48. 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.
49. Li J., Billiar T.R. The role of nitric oxide in apoptosis. Semin Perinatol 2000; 24: 46-50.
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.
51. Liaudet L., Soriano F.G., Szabo C. Biology of nitric oxide signaling. Crit Care Med 2000; 28 (Suppl): N37-N52.
52. 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.
53. 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.
54. Mannick J.B., Hausladen A., Liu L. et al. Fas-induced caspase denitrosylation. Science 1999; 284: 651-654.
55. Margulis L. Archaeal-eubacterial mergers in the origin of Eukarya: Phylogenetic classification of life. Proc Natl Acad Sci USA 1996; 93: 1071-1076.
56. 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.
57. 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.
58. Nagata S., Golstein P. The Fas death factor. Science 1995; 267:1449-1456.
59. Nagata S. Apoptosis by death factor. Cell 1997; 88: 355-365.
60. 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.
61. Nicholson D.W., Thornberry N.A. Apoptosis. Life and death decisions. Science 2003 Jan 10; 299 (5604): 214-215.
62. Nicholson D.W., Thornberry N.A. Caspases: Killer proteases. Trends Biochem Sci 1997; 22: 299-306.
63. 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.
64. Perfettini J.L., Gissot M., Souque P., Ojcius D.M. Modulation of apoptosis during infection with Chlamydia. Methods Enzymol 2002; 358: 334-344.
65. 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.
66. 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.
67. Reed J.C. Bcl-2 family proteins. Oncogene 1998; 17: 3225-3226.
68. 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.
69. Salmaso C., Olive D., Pesce G., Bagnasco M. Costimulatory molecules and autoimmune thyroid diseases. Autoimmunity 2002 May; 35 (3): 159-167.
70. Savill J., Fadok V., Henson P., Haslett C. Phagocyte recognition of cells undergoing apoptosis [review]. Immunol Today 1993; 14: 131-136.
71. Savill J., Fadok V. Corpse clearance defines the meaning of cell death. Nature 2000; 407: 784-788.
72. 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.
73. Sherr C.J. Cancer cell cycles. Science 1996; 274: 1672-1677.
74. 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.
75. Singh V.K., Mehrotra S., Narayan P. et al. Modulation of autoimmune diseases by nitric oxide. Immunol Res 2000; 22: 1-19.
76. 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.
77. Steller H. Mechanisms and genes of cellular suicide. Science 1995; 267: 1445-1449.
78. 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.
79. Tartaglia L.A., Goeddel D.V. Two TNF receptors. Immunol Today 1992; 13: 151-153.
80. Thome M., Schneider P., Hofmann K. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 1997; 386: 517-521.
81. Thornberry N.A., Lazebnik Y. Caspases: Enemies within. Science 1998; 281: 1312-1316.
82. 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.
83. 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.
84. Tsujimoto Y., Shimizu S. Bcl-2 family: Life-or-death switch. FEES Lett 2000; 466: 6-10.
85. 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.
86. 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.
87. Zamora R., Vodovotz Y., Billiar T.R. Inducible nitric oxide synthase and inflammatory diseases. Mol Med 2000; 6: 347-373.
88. Zamzami N., Susin S.A., Marchetti P. et al. Mitochondrial control of nuclear apoptosis. J Exp Med 1996; 183: 1533-1544.

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