Apoptosis in normal and pathological conditions
- Authors: Grigoriev M.Y.1, Imyanitov E.N.1, Hanson K.P.1
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Affiliations:
- N. N. Petrov Institute of Oncology
- Issue: Vol 3, No 3 (2003)
- Pages: 3-11
- Section: Reviews
- Published: 31.08.2003
- URL: https://journals.eco-vector.com/MAJ/article/view/693592
- ID: 693592
Cite item
Abstract
Apoptosis is a physiological, actively regulated cell death. Its biological role is outstandingly important, since it serves as defense mechanism aimed to eliminate from the body useless or potentially dangerous cells, and functions in tight balance with proliferation and differentiation processes. Research on programmed cell death has become a very active area in modern biology. Besides a visible fundamental impact into the understanding of mechanisms of cellular homeostasis, studies on apoptosis are gaining an increasing significance for the applied medical science.
About the authors
M. Yu. Grigoriev
N. N. Petrov Institute of Oncology
Author for correspondence.
Email: shabanov@mail.rcom.ru
Russian Federation, St. Petersburg
E. N. Imyanitov
N. N. Petrov Institute of Oncology
Email: shabanov@mail.rcom.ru
Russian Federation, St. Petersburg
K. P. Hanson
N. N. Petrov Institute of Oncology
Email: shabanov@mail.rcom.ru
член-корреспондент РАМН
Russian Federation, St. PetersburgReferences
- Звонарева Н. Б., Сейлиев А. А., Колюбаева С. Н. и др. Исследование механизма гибели тимоцитов при воздействии сверхвысоких доз г-излучения // Радиобиология. 1987. Т. 27. Вып. 3. С. 319-323.
- Adams J. M., Cory S. The Bcl-2 protein family: arbiters of cell survival // Science. 1998. Vol. 281. P. 1322-1326.
- Alnemri E. S., Livingston D. J., Nicholson D. W. et al. Human ICE/CED-3 protease nomenclature //Cell. 1996. Vol. 87. P. 171.
- Arends M. J., Morris R. G., Wyllie A. H. Apoptosis: The role of the endonuclease // Am. J. Pathol. 1990. Vol. 136. P. 593-598.
- Ashkenazi A., Dixit V. M. Death receptors: signaling and modulation // Science. 1998. Vol. 281. P. 1305-1308.
- Borisova E. A., Chukhlovin A. V., Seiliev A. A. et al. Degree of chromatin fragmentation and frequency of nuclear pyknosis in Percoll-fractionated thymocytes of irradiated rats // Int. J. Radiat. Biol. 1987. Vol. 51. P. 421-428.
- Cardone M. H, Roy N., Stennicke N. R. et al. Regulation of cell death protease caspase-9 by phosphorylation // Science. 1998. Vol. 282. P. 1318-1321.
- Chang H. Y., Yang X. Proteases for cell suicide: functions and regulation of caspases // Microbiol. Mol. Biol. Rev. 2000. Vol. 64. P. 821-846.
- Ferreira C. G., Tolis C., Giaccone G. p53 and chemosensitivity // Ann. Oncol. 1999. Vol. 10. P. 1011-1021.
- Gougeon M. L. Apoptosis in AIDS. Genetic control and relevance for AIDS pathogenesis // Biochem. Soc. Trans. 1996. Vol. 24. P. 1055-1058.
- Gougeon M. L., Montagnier L. Programmed cell death as a mechanism of CD4 and CD8 T cell deletion in AIDS. Molecular control and effect of highly active anti-retroviral therapy // Ann. N. Y. Acad. Sci. 1999. Vol. 887. P. 199-212.
- Glucksmann A. Cell death in normal vertebrate ontogeny // Biol. Rev. 1951. Vol. 26. P. 59.
- Grigoriev M. Y., Pozharissky K. M., Hanson K. P. et al. Expression of caspase-3 and -7 does not correlate with the extent of apoptosis in primary breast carcinomas // Cell Cycle. 2002. Vol. 1. P. 337-342.
- Hanahan D., Weinberg R. A. The hallmarks of cancer// Cell. 2000. Vol. 100. P. 5 7-70.
- Harmon B. K, Corder A. M., Collins R. J. et al. Cell death induced in a murine mastocytoma by 42-47°C in vitro: Evidence that the form of death changes from apoptosis to necrosis above a critical heat load // Intern. Radiat. Biol. 1990. Vol. 58. P. 845-858.
- Horvitz H. R. Genetic control of programmed cell death in the nematode Caenorhabditis elegans // Cancer Res. 1999. Vol. 59: 1701s-1706s.
- Janicke R. U., Sprengart M. L., Wati M. R. et al. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis // J. Biol. Chem. 1998. Vol. 273. P. 93 57-93 60.
- Johnson D. E. Noncaspase proteases in apoptosis //Leukemia. 2000. Vol. 14. P. 1695-1703.
- Kerr J. F. R., Wyllie A. H., Currie A. R. Apoptosis: a basic biological phenomenon with wide ranging implications in tissue kinetics // Br. J. Cancer. 1972. Vol. 26. P. 239-257.
- Kerr J. F. R., Winterford C. M., Harmon B. V. Apoptosis. Its significance in cancer and cancer therapy // Cancer. 1994. Vol. 73. P. 2013-2026.
- Kluck R. M., Bossy-Wetzel E., Green D. R. et al. The release of cytochrome c from mitochondria: a primary site for bcl-2 regulation of apoptosis // Science. 1997. Vol. 275. P. 1132-1136.
- Korsmeyer S. J. Chromosomal translocations in lymphoid malignancies reveal novel proto-oncogenes // Annu. Rev. Immunol. 1992. Vol. 10. P. 785-807.
- Krammer P H. CD95’s deadly mission in the immune system // Nature. 2000. Vol. 407. P. 789-795.
- Kubasova T. A., Chukhlovin A. B., Somosy Z. et al. Detection of early membrane and nuclear alterations of thymocytes upon in vitro ionizing radiation // Acta Physiol. Hung. 1993. Vol. 81. P. 277-288.
- Li H., Zhu H., Xu C. J. et al. Cleavage of BID by caspase-8 mediates the mitochondrial damage in the Fas pathway of apoptosis // Cell. 1998. Vol. 94. P. 491-501.
- Mannick J. B., Hausladen A., Liu L. et al. Fasinduced caspase denitrosylation // Science. 1999. Vol. 284. P. 651-654.
- Muzio M., Chinnaiyan A. M., Kischkel E. C. et al. FLICE, a novel FADD-homologous ICE/CED3- like protease is recruited to the CD95 (Fas/ APO-1) death-inducing signaling complex // Cell. 1996. Vol. 85. P. 817-827.
- Nijhawan L. P., Budihardjo L., Srinivasula S. M. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade // Cell. 1997. Vol. 91. P. 479-489.
- Piacentini M., Colizzi V. Tissue transglutaminase: apoptosis versus autoimmunity // Immunol. Today. 1999. Vol. 20. P. 130-134.
- Savill J., Fadok V. Corpse clearance defines the meaning of cell death // Nature. 2000. Vol. 407. P. 784-788.
- Schuler M., Green D. R. Mechanisms of p53- dependent apoptosis // Biochem. Soc. Trans. 2001. Vol. 29. P. 684-688.
- Skalka M., Matyasova J., Cejkova M. DNA in chromatin of irradiated lymphoid tissues degrades in vivo into regular fragments // FEBS Lett. 1976. Vol. 72. P. 271-274.
- Stennicke H. R., Ryan C. A., Salvesen G. S. Reprieval from execution: the molecular basis of caspase inhibition // Trends Biochem. Sci. 2002. Vol. 27. P. 94-101.
- Thome M., Schneider P., Hofmann K. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors // Nature. 1997. Vol. 386. P. 517-521.
- Thornberry N. A., Lazebnik Y. Caspases: enemies within // Science. 1998. Vol. 281. P. 1312-1316.
- Yamada T., Ohyama H., Kinio Y. et al. Evidence for the internucleosomal breakage of chromatin in rat thymocytes irradiated in vitro // Radiat. Res. 1981. Vol. 85. P. 544-553.
- Yang E., Korsmeyer S. K. Molecular thanatopsis: A discourse on the bcl-2 family and cell death // Blood. 1996. Vol. 88. P. 386-401.
- Yang J., Liu X., Bhalla K. et al. Prevention of apoptosis by bcl-2: release of cytochrome c from mitochondria blocked // Science. 1997. Vol. 275. P. 1129-1132.
- Yuan J., Yankner B. A. Apoptosis in the nervous system // Nature. 2000. Vol. 407. P. 802-809.
- Zherbin E. A., Chukhlovin A. B., Koteles G. J. et al. Effect in vitro of cadmium ions on some membrane and nuclear parameters of normal and irradiated thymic lymphoid cells // Arch. Toxicol. 1986. Vol. 59. P. 21-25.
- Zhivotovsky B. D., Zvonareva N. B., Hanson K. P. Characteristics of rat thymus chromatin degradation products after whole body X-irradiation // Int. J. Radiat. Biol. 1981. Vol. 39. P. 437-440.
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