особенности его развития при воздействии ингибиторов цепных реакций. Докл АН СССР. 1958, 121, 141-144.
8.Владимиров Ю.А. Свободно-радикальное окисление липидов
èфизические свойства биологических мембран. Биофизика. 1987, 32, 830-844.
9.MacGregor J.T. The future of regulatory toxicology: impact of the biotechnology revolution. Toxicol Sci. 2003, 75, 236-248.
10.Wright M.M., Howe A.G., Zaremberg V. Cell membranes and apoptosis: role of cardiolipin, phosphatidylcholine, and anticancer lipid analogues. Biochem Cell Biol. 2004, 82, 18-26.
11.Haque M.A., Russell N.J. Strains of Bacillus cereus vary in the phenotypic adaptation of their membrane lipid composition in response to low water activity, reduced temperature and growth in rice starch. Microbiology. 2004, 150, 1397-1404.
12.Brown M.S., Goldstein J.L. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell. 1997, 89, 331-340.
13.Worgall T.S., Johnson R.A., Seo T., Gierens H., Deckelbaum R.J. Unsaturated fatty acid-mediated decreases in sterol regulatory elementmediated gene transcription are linked to cellular sphingolipid metabolism. J Biol Chem. 2002, 277, 3878-3885.
14.Yakovlev A.G., Faden A.I. Mechanisms of neural cell death: implications for development of neuroprotective treatment strategies. J.Amer Soc Exper Neuro Therapeutics. 2004, 1, 5-16.
15.Thrall K.D., Vucelick M.E., Gies R.A., Zangar R.C., Weitz K.K., Poet T.S., Springer D.L., Grant D.M., Benson J.M. Comparative metabolism of carbon tetrachloride in rats, mice, and hamsters using gas uptake and PBPK modeling. J Toxicol Environ Health. 2000, 60, 531548.
16.Glucksmann A. Cell death in normal vertebrate ontogeny. Biol Rev. 1951, 26, 59-86.
17.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.
18.Yeh E.T.H. Life and death in the cardiovascular system. Circulation. 1997, 95, 782-786.
19.Bhatia M. Apoptosis versus necrosis in acute pancreatitis. Am J Physiol Gastrointest Liver Physiol. 2004, 286, 189-196.
20.Padanilam B.J. Cell death induced by acute renal injury: a perspective on the contributions of apoptosis and necrosis. Am J Physiol Renal Physiol. 2003, 284, 608-627.
21.Green D.R. Overview: apoptotic signaling pathways in the immune system. Immunol Rev. 2003, 193, 5-9.
151
22.Самуилов В.Ф. Биохимия программируемой клеточной смерти (апоптоза) у животных. Соросовский образовательный журнал. 2001, 7, 18-25.
23.Ranganath R.M., Nagashree N.R. Role of programmed cell death in development. Int Rev Cytol. 2001, 202, 159-242.
24.Скулачев В.П. Законы биоэнергетики. Соросовский образовательный журнал. 1997, 1, 9-14.
25.Israels L.G., Israels E.D. Apoptosis. Stem Cells. 1999, 17, 306-313.
26.Leist M., Single B., Castoldi A., Kuhnle S., Nicotera P. Intracellular Adenosine Triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J Exp Ved. 1997, 185, 1481-1486.
27.Afford S., Randhawa S. Apoptosis. Mol Pathol. 2000, 53, 55-63.
28.Gompel A., Chaouat M., Hugol D., Forgez P. Steroidal hormones and proliferation, differentiation and apoptosis in breast cells. Maturitas. 2004, 49, 16-24.
29.Ширшев С.В., Куклина Е.М., Ярилин А.А. Роль репродуктивных гормонов в контроле апоптоза Т-лимфоцитов. Биохимия. 2003, 68, 470-475.
30.Walker A., Ward C., Dransfield I., Haslett C., Rossi A.G. Regulation of granulocyte apoptosis by hemopoietic growth factors, cytokines and drugs: potential relevance to allergic inflammation. Curr Drug Targets Inflamm Allergy. 2003, 2, 339-347.
31.Kharroubi I., Ladriere L., Cardozo A.K., Dogusan Z., Cnop M., Eizirik D.L. Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappaB and endoplasmic reticulum stress. Endocrinology. 2004, 145, 5087-5096.
32.Kaufmann S.H., Hengartner M.O. Programmed cell death: alive and well in the new millennium. Trends Cell Biol. 2001, 11, 526-534.
33.Roth W., Reed J.C. FLIP protein and TRAIL-induced apoptosis. Vitam Horm. 2004, 67, 189-206.
34.MacEwan D.J. TNF ligands and receptors - a matter of life and death. Brit J Pharmacol. 2002, 135, 855-875.
35.Rudner J., Jendrossek V., Lauber K., Daniel P.T., Wesselborg S., Belka C. Type I and type II reactions in TRAIL-induced apoptosis - results from dose-response studies. Oncogene. 2005, 24, 130-140.
36.Creagh E.M., Martin S.J. Caspases: cellular demolition experts. Biochem Soc Trans. 2001, 29, 696-702.
37.Earnshaw W.C., Martins L.M., Kaufmann S.H. Mammalian caspases: structure, activation, substrates and functions during apoptosis. Ann Rev Biochem. 1999, 68, 383-424.
38.Kruidering M., Schouten T., Evan G.I., Vreugdenhil E. Caspasemediated cleavage of the Ca2+ dependent protein kinase-like kinase
152
facilitates neuronal apoptosis. J Biol Chem. 2001, 276, 38417-38425.
39.Strasser A., O'Konnor L., Dixit V.M. Apoptosis signaling. Ann Rev Biochem. 2000, 69, 217-245.
40.Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 1998, 281, 1312-1316.
41.Tibbetts M.D., Zheng L., Lenardo M.J. The death effector domain protein family: regulators of cellular homeostasis. Nat Immun. 2003, 4, 404-409.
42.Gruenbaum Y., Goldman R.D., Meyuhaus R., Mills E., Margalit A., FridkinA., Dayani Y., Prokocimer M., Enosh A. The nuclear lamina and its functions in the nucleus. Int Rev Cytol. 2003, 226, 1-62.
43.Nagase H., Fukuyama H., Tanaka M., Kawane K., Nagata S. Mutually regulated expression of caspase-activated DNase and its inhibitor for apoptotic DNA fragmentation. Cell Death Differ. 2003, 10, 142-143.
44.Goping I.S., Barry M., Liston P., Sawchuk T., Constantinescu G., Michalak K.M., Shostak I., Roberts D.L., Hunter A.M., Korneluk R., Bleackley R.C. Granzyme B-induced apoptosis requires both direct caspase activation and relief of caspase inhibition. Immunity. 2003, 18, 355-365.
45.Bortner C.D., Cidlowski J.A. Caspase independent/dependent regulation of K(+), cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis. J Biol Chem. 1999, 274, 21953-21962.
46.Скулачев В.П. Явления запрограммированной смерти. Митохондрии, клетки и органы: роль активных форм кислорода. Соросовский образовательный журнал. 2001, 7, 4-10.
47.Desagher S., Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 2000, 10, 369-377.
48.Bellamy C.O., Makcomson R.D., Harrison D.J., Wyllie A.H. Cell death in health and disease: the biology and regulation of apoptosis. Semin Cancer Biol. 1995, 6, 3-16.
49.Hengartner M.G. The biochemistry of apoptosis. Nature. 2000, 407, 770-775.
50.Boonstra J., Post J.A. Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. Gene. 2004, 337, 1-13.
51.Villialba J.M., Navas P. Plasma membrane redox system in the control of stress-induced apoptosis. Antiox Redox Signal. 2000, 2, 213-230.
52.Willis S., Day C.L., Hinds M.G., Huang D.C.S. The Bcl-2-regulated apoptotic pathway. J Cell Science. 2003, 116, 4053-4056.
53.Zha H., Aime-Sempre C., Sato T., Reed J.C. Proapoptotic protein Bax heterodimerizes with Dcl2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem. 1996, 271, 7440-7444.
153
54.van Loo G., Schotte P., van Gurp M., Demol H., Hoorelbeke B., Gevaert K., Rodriguez I., Ruiz-Carrillo A., Vandekerckhove J., Declercq W., Beyaert R., Vandenabeele P. Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation. Cell Death Differ. 2001, 8, 1136-1142.
55.Liang Y., Eid M.A., Lewis R.W., Kumar M.V. Mitochondria from TRAIL-resistant prostate cancer cells are capable of responding to apoptotic stimuli. Cell Signal. 2005, 17, 243-251.
56.Goonesinghe A., Mundy E.S., Smith M., Khosravi-Far R., Martinou J.C., Esposti M.D. Pro-apoptotic Bid induces membrane perturbation by inserting selected lysolipids into the bilayer. Biochem J. 2005, 387, 109-118.
57.Tsujimoto Y. Bcl-2 family of proteins: life-or-death switch in mitochondria. Biosci Rep. 2002, 22, 47-58.
58.Adams J.M., Cory S. Life or death decisions by the Bcl-2 protein family. Trends in Biochem Sci. 2001, 26, 61-66.
59.Bernardi P., Scorrano L., Colonna R., Petronilli V., Di Lisa F. Mitochondria and cell death. Mechanistic aspects and methodological issues. Eur J Biochem. 1999, 264, 687-701.
60.Szewczyk A., Wojtczak L. Mitochondria as a pharmacological target. Pharmacol Rev. 2002, 54, 101-127.
61.Kim J.S., Qian T., Lemasters J.J. Mitochondrial permeability transition in the switch from necrotic to apoptotic cell death in ischemic rat hepatocytes. Gastroenterology. 2003, 124, 494-503.
62.Lemasters J.J., Qian T., He L., Kim J.S., Elmore S.P., Cascio W.E., Brenner D.A. Role of mitochondrial inner membrane permeabilization in necrotic cell death, apoptosis, and autophagy. Antioxid Redox Signal. 2002, 4, 769-781.
63.Petrolini V., Penzo D., Scorrano L., Bernardi P., Di Lisa F. The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore opening in situ. J Biol Chem. 2001, 276, 12030-12034.
64.Henry-Mowatt J., Dive C., Martinou J.C., James D. Role of mitochondrial membrane permeabilization in apoptosis and cancer. Oncogene. 2004, 23, 2850-2860.
65.Sakahira H., Takemura Y., Nagata S. Enzymatic active site of cas- pase-activated DNase (CAD) and its inhibition. Arch Biochem Biophys. 2001, 388, 91-99.
66.Li L.Y., Luo X., Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature. 2001, 412, 95-97.
67.Seluanov A., Gorbunova V., Falcovitz A., Sigal A., Milyavsky M., Zurer I., Shohat G., Goldfinger N., Rotter V. Change of the death pathway in senescent human fibroblasts in response to DNA damage is
154
caused by an inability to stabilize p53. Mol Cellular Biol. 2001, 21, 1552-1564.
68.Scoggins C.R., Meszoely I.M., Wada M., Means A.I., Yang L., Leach SD. p53-dependent acinar cells apoptosis triggers epithelial proliferation in duct-ligated murine pancrease. Am J Physiol Gastrointest Liver Physiol. 2000, 279, 827-836.
69.Lain S., Xirodimas D., Lane D.P. Accumulating active p53 in the nucleus by inhibition of nuclear export: a novel strategy to promote the p53 tumor suppressor function. Exp Cell Res. 1999, 253, 315-324.
70.Gil J., Esteban M. Induction of apoptosis by the dsRNA-depend- ent proteinkinase R (PKR): mechanism of action. Apoptosis. 2000, 5, 107-114.
71.Iordanov M.S., Ryabinina O.P., Schneider P., Magun B.E. Two mechanisms of caspase 9 processing in double-stranded RNAand virus-triggered apoptosis. Apoptosis. 2005, 10, 153-166.
72.Brookes P.S., Yoon Y., Robotham J.L., Anders M.W., Sheu S.S. Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am J Physiol Cell Physiol. 2004, 287, 817-833.
73.Davies A.M., Hershman S., Stabley G.J., Hoek J.B., Peterson J., Cahil A. A Ca2+ induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within the mitochondrial matrix. Nucleic Acids Res. 2003, 31, 1364-1373.
74.Luchen S., Ussat S., Kronke M., Adam-Klages S. Cleavage of human cytosolic phospholiase A2 by caspase-1 (ICE) and caspase-8
(FLICE). Biochem Biophys Res Commun. 1998, 253, 92-98.
75.Cumming D.S., Mchowat J., Schnellmann R.G. Phospholipase À2s in cell injury and death. J Pharmacol Experim Therapeutic. 2000, 294, 793-799.
76.Wissing D., Mouritzen H., Egeblad M., Poirer G.G, Jattela M. Involvement of caspase-dependent activation of cytosolic phospholipase À2 in tumor necrosis factor-induced apoptosis. Pros Natl Acad Sci USA. 1997, 94, 5073-5077.
77.Zhao M., Antunes F., Eaton J.W., Brunk U.T. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome ñ release sand apoptosis. Eur J Biochem. 2003, 270, 3778-3786.
78.Brunk U.T., Neuzil J., Eaton J.W. Lysosomal involvement in apoptosis. Redox Report. 2001, 6, 91-97.
79.Salvesen G.S. A lysosomal protease enters the death scene. J Clin Invest. 2001, 107, 21-22.
80.Ono K., Kim S.O., Han J. Susceptibility of lysosomes to rupture is a determinant for plasma membrane disruption in tumor necrosis fac-
155
tor alpha-induced cell death. Mol Cell Biol. 2003, 23, 665-676.
81.Fabisiak J.P., Borisenko G.G., Kagan V.E. Quantitative method of measuring phosphatidylserine externalization during apoptosis using electron paramagnetic resonance spectroscopy and annexin-conjugated iron. Methods Mol Biol. 2005, 291, 457-464.
82.Fadeel B. Plasma membrane alterations during apoptosis: role in corpse clearance. Antiox Redox Signal. 2004, 6, 269-275.
83.Kagan V.E., Borisenko G.G., Serinkan B.F., Tyurina Y.Y., Tyurin V.A., Jiang J., Liu S.X., Shvedova A.A., Fablsiak J.P., Uthaisang W., Fadeel B. Appetizing rancidity of apoptotic cells for macrophages: oxidation, externalization, and recognition of phosphatidylserine. Am J Physiol Lunp Cell Mol Physiol. 2003, 285, l-17.
84.Henson P.M., Bratton D.L., Fadok V.A. The phosphatidylserine receptor: a crucial molecular switch? Nature Rev Mol Cell Biol. 2001, 2, 627-633.
85.Kagan V.E., Borisenko G.G., Tyurina Y.Y., Tyurin V.A., Jiang J., Potapovich A., Kini V., Amoscato A.A., Fuji Y. Oxidative lipidomics of apoptosis: rådox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine. Free Rad Biol Med. 2004, 37, 1963-1985.
86.Szabo I., Adams C., Gulbins E. Ion channels and membrane rafts in apoptosis. Pflugers Arch. 2004, 448, 304-312.
87.Eramo A., Vitani L.R., Sargiacomo M., Peschle, De Maria R. CD95 signaling is initiated in lipid rafts. The Third European Workshop on cell death. Salobreca (Spain). 2002, abstr. 8.
88.Gomez-Munoz A., Kong J.Y., Salh B., Steinbrecher U.P. Ceramide-1-phosphate blocks apoptosis through inhibition of acid sohingomyelinase in macrophages. J Lipid Res. 2004, 45, 99-105.
89.Hannun Y.A., Obeid L.M. Mechanisms of ceramide-mediated apoptosis. Adv Exp Med Biol. 1997, 407, 145-149.
90.Cremesti A., Paris F., Grassme H., Holler N., Tschopp J., Fuks Z., Gulbins E., Kolesnick R Ceramide enables fas to cap and kill. J Biol Chem. 2001, 276, 23954-23961.
91.Novgorodov S.A., Szulc Z.M., Luberto C., Jones J.A., Bielawski J., Bielawska A., Hannun Y.A., Obeid L.M. Positively charged ceramide is a potent inducer of mitochondrial permeablization. J Biol Chem. 2005, 280, 16096-16105.
92.Cuvillier O., Nava V.E., Murthy S.K., Edsall L.C., Levade T., Milstien S., Spiegel S. Sphingosine generation, cytochrome c release, and activation of caspase-7 in doxorubicin-induced apoptosis of MCF7 breast adenocarcinoma cells.Cell Death Differ. 2001, 8, 162-171.
93.Payne S.G., Milstein S., Spiegel S. Sphingosine-1-phosphate: dual messenger functions. FEBS Lett. 2002, 531, 54-57.
94.Spiegel S., Milstein S. Sphingosine-1-phosphate, a key signaling
156
molecule. J Biol Chem. 2002, 277, 25851-25854.
95.Laio K.U., Shelburne J.D., Trump B.F. Observation on cell volume, ultrastructure, mitochondrial conformation and vital-dye uptake in Ehrlich ascites tumor cells. Effects of inhibiting energy production and function of the plasma membrane. Am J Pathol. 1971, 65, 203-230.
96.Trump B.F., Goldblatt P.J., Stowell R.E. Studies of necrosis in vitro of mouse hepatic parenchimal cells. Ultrastructural alterations in endoplasmatic reticulum, Golgi apparatus, plasma membrane and lipid droplets. Lab Invest. 1965, 14, 2000-2028.
97.Syntichaki P., Tavernakis N. Death by necrosis. Uncontrollable catastrophe, or is there order behind the haos? EMBO Reports. 2002, 3, 604-609.
98.Данченко Е.О. Влияние препаратов желчных кислот на биосинтез ДНК, апоптоз и некроз гепатоцитов in vitro. Вопр. мед. химии. 2001, 47, 236-242.
99.Ray S.D., Lam T.S., Rotollo J.A., Phadke S., Patel C., Dontabhaktuni A., Mohammad S., Lee H., Strika S., Dobrogowska A., Bruculeri C., Chou A., Patel S., Patel R., Manolas T., Stohs S. Oxidative stress is the master operator of drug and chemically-induced programmed and unprogrammed cell death: Implications of natural antioxidants in vivo. Biofactors. 2004, 21, 223-232.
100.Zeiss Ñ.J. The apoptosis-necrosis continuum: insights from genetically altered mice. Vet Pathol. 2003, 40, 481-495.
101.Владимиров Ю.А. Кальциевые насосы живой клетки. Соросовский образовательный журнал. 1998, 3, 20-27.
102.Barros L.F., Hermosilla T., Castro J. Necrotic volume increase and the early physiology of necrosis. Comp Biochem Physiol A Mol Integr Physiol. 2001, 130, 401-409.
103.Carini R., Bellomo G., Dianzani M.U., Albano E. The operation of Na+/Ca2+ exchanger prevents intracellular Ca2+ overload and hepatocytes killing following iron-induced lipid peroxidation. Biochem Biophys Res Commun. 1995, 208, 813-818.
104.Levitsky J., Gurell D., Frishman W.H. Sodium ion/hydrogen ion exchange inhibition: a new pharmacological approach to myocardial ishemia and reperfusion injury. J. Clin Pharmacol. 1998, 38, 887898.
105.Владимиров Ю.А. Нарушение барьерных свойств внутренней и наружной мембран митохондрий, некроз и апоптоз. Биологические мембраны. 2002, 19, 356-377.
106.Droge W. Free radicals in the physiological control of cell function. Physiol Rev. 2001, 82, 47-95.
107.Ermak G., Davies K.J. Calcium and oxidative stress: from cell signaling to cell death. Mol Immunol. 2002, 38, 713-721.
157
108.Wang K.K. Calpain and caspases: can you tell the difference? Trends Neurosci. 2000, 23, 20-26.
109.Kim J.S., He L., Qian T., Lemasters J.J. Role of the mitochondrial permeability transition in apoptotic and necrotic death after ischemia/reperfusion injury to hepatocytes. Curr Mol Med. 2003, 3, 527-535.
110.Ly J.D., Grubb D.R., Lawen A. The mitochondrial membrane potential (deltapsi(m)) in apoptosis; an update. Apoptosis. 2003, 8, 115128.
111.Dussmann H., Rehm M., Kogel D., Prehn J.H. Outer mitochondrial membrane permeabilization during apoptosis triggers caspase-independ- ent mitochondrial and caspase-dependent plasma membrane potential depolarization: a single-cell analysis. J Cell Sci. 2003, 116, 525-536.
112.Guo K., Searfoss G., Krolikowski D., Pagnoni M., Franks C., Clark K., Yu K.T., Jaye M., Ivashenko Y. Hypoxia induces the expression of the proapoptotic gene BNIP3. Cell Death Differ. 2001, 8, 367376.
113.Yu S.W., Wang H., Poitras M.F., Coombs C., Bowers W.J., Fedoroff H.J., Poirier G.G., Dawson T.M., Dawson V.L. Mediation of poly(ADP-ribose) polymerase-1-dependent cell eath by apoptosis inducing factor. Science. 2002, 297, 259-263.
114.Pessayre D., Mansouri A., Haouzi D., Fromenty B. Hepatotoxicity due to mitochondrial dysfunction. Cell Biol Toxicol. 1999, 15, 367-373.
115.Hatano E., Bradham C.A., Stark A., Iimuro Y., Lemasters J.J., Brenner D.A. The mitochondrial permeability transition augments Fasinduced apoptosis in mouse hepatocytes. J Biol Chem. 2000, 275, 1181411823.
116.Fosslien Å. Mitochondrial medicine-molecular pathology of defective oxidative phosphorylation. Ann Clin Lab Sci. 2001, 31, 25-67.
117.Somosy Z. Radiation response of cell organelles. Micron. 2000, 31, 165-181.
118.Rodriguez-Enriquez S., He L., Lemasters J.J. Role of mitochondrial permeability transition pores in mitochondrial autophagy. Int J Biochem Cell Biol. 2004, 36, 2463-2472.
119.Copp J., Wiley S., Ward M.W., van der Geer P. Hypertonic shock inhibits growth factor receptor signaling, induces caspase-3 activation, and causes reversible fragmentation of the mitochondrial network. Am J Physiol Cell Physiol. 2005, 288, 403-415.
120.Davi G., Falco A., Patrono C. Lipid peroxidation in diabetes mellitus. Antioxid Redox Signal. 2005, 7, 256-268.
121.Asano G., Takashi E., Ishiwata T., Onda M., Yokoyama M., Naito Z., Ashraf M., Sugisaki Y. Pathogenesis and protection of
158
ischemia and reperfusion injury in myocardium. J Nippon Med Sch. 2003, 70, 384-392.
122.Lieberthal W., Menza S.A., Levine J.S. Graded ATP depletion can cause necrosis or apoptosis of cultured mouse proximal tubular cells. Am J Physiol. 1998, 274, 315-327.
123.Bruemmer-Smith S., Stuber F., Schroeder S. Protective functions of intracellular heat-shock protein (HSP) 70-expression in patients with severe sepsis. Intensive Care Med. 2001, 27, 1835-1841.
124.De Broe M.E. Apoptosis in acute renal failure. Nephrol Dial Transplant. 2001, 16, 23-26.
125.Lieberthal W., Levine J.S. Mechanism s of apoptosis and its potåntial rolå in renal tubular epithelial cell injury. Am J Physiol Renal Fluid Electrolyte Physiol. 1996, 271, 477-488.
126.Edelstein C.L., Shi Y., Schrier R.W. Role of caspases in hypox- ia-induced necrosis of rat renal proximal tubules. J Am Soc Nephrol. 1999, 10, 1940-1949.
127.Vanden Berghe T., van Loo G., Saelens X., Van Gurp M., Brouckaert G., Kalai M., Declercq W., Vandenabeele P. Differential signaling to apoptotic and necrotic cell death by Fas-associated death domain protein FADD. J Biol Chem. 2004, 279, 7925-7933.
128.Wang Y., Li X., Wang L., Ding P., Zhang Y., Han W., Ma D. An alternative form of paraptosis-like cell death, triggered by TAJ/TROY and enhanced by PDCD5 overexpression. J Cell Sci. 2004, 117, 15251532.
129.Skulachev V.P. How proapoptotic proteins can escape from mitochondria? Free Radic Biol Med. 2000, 29, 1056-1059.
130.Владимиров Ю.А., Арчаков А.И. Перекисное окисление липидов в биологических мембранах. Наука, М. 1972.
131.Archakov A.I., Bachmanova G.I. Cytochrome P-450 and active oxygen. Taylor & Francis, London, New York, Philadelphia. 1990.
132.Осипов А.Н., Азизова О.А., Владимиров Ю.А. Активные формы кислорода и их роль в организме. Успехи.биол.химии. 1990, 31, 180-208.
133.Girotti A.W. Lipid hydroperoxide generation, turnover, and effector action in biological systems. J Lipid Res. 1998, 39, 1529-1542.
134.Зенков Н.К., Ланкин В.З., Меньщикова Е.Б. Окислительный стресс. Биохимический и патофизиологический аспекты. МАИК, Наука/Интерпериодика, М. 2001.
135.Montine T.J., Neely M.D., Quinn J.F., Beal M.F., Markesbery W.R., Roberts L.J., Morrow J.D. Lipid peroxidation in aging brain and Alzheimer's disease. Free Radic Biol Med. 2002, 33, 620-626.
136.Spiteller G. Are lipid peroxidation processes induced by changes in the cell wall structure and how are these processes connected with dis-
159
eases? Med Hypotheses. 2003, 60, 69-83.
137.Владимиров Ю.А. Свободные радикалы в биологических системах. Соросовский образовательный журнал. Биология. 2000,
12, 13-19.
138.Davies M.J. Singlet oxygen-mediated damage to proteins and its consequences. Biochem Biophys Res Commun. 2003, 305, 761-770.
139.Davies M.J. Reactive species formed on proteins exposed to singlet oxygen. Photochem Photobiol Sci. 2004, 3, 17-25.
140.Kim S.Y, Kim E.J., Park J.W. Control of singlet oxygen-induced oxidative damage in Escherichia coli. J Biochem Mol Biol. 2002, 35, 353-357.
141.Klotz L.O., Kroncke K.D., Sies H. Singlet oxygen-induced signaling effects in mammalian cells. Photochem Photobiol Sci. 2003, 2, 88-94.
142.Kehrer J.P. Free radicals as mediators of tissue injury and disease. Crit Rev Toxicol. 1993, 23, 21-48.
143.Forman H.J., Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med. 2002, 166, 4-8.
144.Stamler J.S., Single D., Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science. 1992, 258, 1898-1902.
145.Gu X., Sun M., Gugiu B., Hazen S., Crabb J.W., Salomon R.G. Oxidatively truncated docosahexaenoate phospholipids: total synthesis, generation, and Peptide adduction chemistry. J Org Chem. 2003, 68, 3749-3761.
146.Daleke D.L. Regulation of transbilayer plasma membrane phospholipid asymmetry. J Lipid Res. 2003, 44, 233-242.
147.Korytowski W., Zareba M., Girotti A.W. Inhibition of free rad- ical-mediated cholesterol peroxidation by diazeniumdiolate-derived nitric oxide: effect of release rate on mechanism of action in a membrane system. Chem Res Toxicol. 2000, 13, 1265-1274.
148.Kunsch C., Medford R. Oxidative stress as a regulator of gene expression in vasculature. Circ Res. 1999, 85, 753-766.
149.Bowie A., O'Neill L.A. Oxidative stress and nuclear factorkappaB activation: a reassessment of the evidence in the light of recent discoveries. Biochem Pharmacol. 2000, 59, 13-23.
150.Eligini S., Brambilla M., Banfi C., Camera M., Sironi L., Barbieri S.S., Auwerx J., Tremoli E., Colli S. Oxidized phospholipids inhibit cyclooxygenase-2 in human macrophages via nuclear factorkappaB/IkappaBand ERK2-dependent mechanisms. Cardiovasc Res. 2002, 55, 406-415.
151.Sakoda T., Hirata K., Kuroda R. Myristoylation of endothelial cells nitric oxide synthase is important for extracellular release of nitric
160