СТРЕСС ЭНДОПЛАЗМАТИЧЕСКОГО РЕТИКУЛУМА ГЛАЗАМИ НЕФРОЛОГА (СООБЩЕНИЕ I)
https://doi.org/10.24884/1561-6274-2012-16-3/1-54-71
Аннотация
В обзоре приводятся данные, касающиеся стресса эндоплазматического ретикулума (ЭПР-стресса). Приводятся сведения относительно биологической роли ЭПР-стресса, причин его возникновения, внутриклеточных событий, обеспечивающих развитие адаптивного и проапоптозного биохимических каскадов, лежащих в основе UPR, реакции на ЭПР-стресс, и определяющих судьбу клетки, подвергшейся воздействию этого стресса. Обсуждаются физиологические и патофизиологические аспекты ЭПР-стресса, его связь с гипоксией, воспалением, оксидативным стрессом. Рассматривается роль ЭПР-стресса в патогенезе ряда заболеваний.
Об авторах
Я. Ф. Зверев
Алтайского государственного медицинского университета
Россия
Россия
кафедра фармакологии
656038, г. Барнаул, пр. Ленина, д. 40. Тел.: (3852)26-08-35
В. М. Брюханов
Алтайского государственного медицинского университета
Россия
Кафедра фармакологии
Россия
Кафедра фармакологии
Список литературы
1. Gaut JR, Hendershot LM. The modification and assembly of proteins in the endoplasmic reticulum. Curr Opin Cell Biol 1993; 5: 589-595
2. Ni M, Lee AS. ER chaperones in mammalian development and human diseases. FEBS Lett 2007; 581: 3641-3651
3. Cybulsky AV. Endoplasmic reticulum stress in proteinuric kidney disease. Kidney Int 2010; 77 (3): 187-193
4. Lee AS The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 2001; 26: 504-510
5. Szegezdi E, Logue SE, Gorman AM, Samali A. Mediatirs of endoplasmic reticulum stresss-induced apoptosis. EMBO Rep 2006; 7 (9): 880-885
6. Kitamura M. Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces. Am J Physiol Renal Physiol 2008; 295 (2): F323-F334
7. Zhang K, Kaufman DJ. Identification and characterization of endoplasmic reticulum stress-induced apoptosis in vivo. Methods Enzymol 2008; 442: 395-419
8. Inagi R. Endoplasmic reticulum stress in the kidney as a novel mediator of kidney injury. Nephron Exp Nephrol 2009; 112 (1): e1-e9
9. Kleizen B, Braakman I. Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 2004; 16: 343-349
10. Kitamura M. Endoplasmic reticulum stress in the kidney. Clin Exp Nephrol 2008; 12: 317-325
11. Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007; 9: 2277-2293
12. Kitamura M. Endoplasmic reticulum stress in glomerulonephritis: the bad guy turns good? J Am Soc Nephrol 2009; 20 (9): 1871-1873
13. Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8: 519-529
14. Dickhout JG, Krepinsky JC. Endoplasmic reticulum stress and renal disease. Antioxid Redox Signal 2009; 11 (9): 2341-2352
15. Yoshida H, Matsui T, Yamamoto A et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107: 881-891
16. Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 2003; 23: 7448-7459
17. Yamamoto K, Sato T, Matsui T et al. Transcriptional induction of mammalian ERquality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev Cell 2007; 13: 365-376
18. Voges D, Zwicki P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015-1068
19. Brodsky JL. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulumassociated degradation). Biochem J 2007; 404: 353-363
20. Cybulsky AV, Takano T, Papillon J et al. Glomerular epithelial cell injury associated with mutant α-actinin-4. Am J Physiol Renal Physiol 2009; 297 (4): F987-F995
21. Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397: 271-274
22. Harding HP, Zhang Y, Bertolotti A et al. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000; 5: 897-904
23. Zhang DD. Mechanistic studies of Nrf2-Keap1 signaling pathway. Drug Metab Rev 2006; 28: 769-789
24. Schroder M, Kaufman RJ. The mammalian unfolded protein response. Ann Rev Biochem 2005; 74: 739-789
25. Adachi Y, Yamamoto K, Okada T et al. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct 2008; 33: 75-89
26. Wu J, Rutkowski DT, Dubois M et al. ATF6alpha optimizes longterm endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 2007; 13: 351-364
27. Fonesca SG, Urano F, Burcin M, Gromada J. Stress hypERactivation in the β-cell. Islets 2010; 2 (1): 1-9
28. Pallet N, Beuvier N, Legendre C et al. Autophagy protects renal tubular cells against cyclosporine toxicity. Autophagy 2008; 4: 783-791
29. Pallet N, Anglicheau D, Thervet E. Autophagy is an adaptive mechanism against endoplasmic reticulum stress. Nephrol Dial Transplant 2009; 24: 3891
30. Kawakami T, Inagi R, Takano H et al. Endoplasmic reticulum stress induces autophagy in renal proximal tubular cells. Nephrol Dial Transplant 2009; 24: 2665-2672
31. Ogata M, Hino S, Saito A et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006; 26: 9220-9231
32. Yorimitsu T, Nair U, Yang Z, Klionsky DJ. Endoplasmic reticulum stress triggers autophagy. J Biol Chem 2006; 281: 30299-30304
33. Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451 (7182): 1069-1075
34. Periyasamy-Thandavan S, Jiang M, Wei Q et al. Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells. Kidney Int 2008; 74 (5): 631-640
35. Hartleben D, Gödel M, Meyer-Schwesinger C et al. Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest 2010; 120 (4): 1084-1096
36. Ding WX, Ni HM, Gao W et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171: 513-524
37. Høyer-Hansen M, Jäättelä M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007; 14: 1576-1582
38. Harding HP, Zhang Y, Zeng H et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 2003; 11 (3): 619-633
39. McCullough KD, Martindale JL, Klotz LO et al. Gadd 153 sensitizes cells by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21: 1249-1259
40. Anding AL, Chapman JS, Barnett DW et al. The unhydrolyzable fenretinide analogue 4-hydroxybenylretinone induces the proaptotic genes GADD 153 (CHOP) and Bcl-2-binding component 3 (PUMA) and apoptosis that is caspase-dependent and independent of the retinoic acid receptor. Cancer Res 2007; 67: 6270-6277
41. Bhatt K, Feng L, Pabla N et al. Effects of targeted Bcl-2 expression in mitochondria or endoplasmic reticulum on renal tubular cell apoptosis. Am J Physiol Renal Physiol 2008; 94: F499-F507
42. Zinszner H, Kuroda M, Wang X et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 1998; 12: 982-995
43. Urano F, Wang X, Bertolotti A et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666
44. Nishitoh H, Matsuzawa A, Tobiume K et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002; 16: 1345-1355
45. Kim R, Emi M, Tanabe K, Murakami S. Role of the unfolded protein response in cell death. Apoptosis 2006; 11: 5-13
46. Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000; 103: 239-252
47. Князькин ИВ, Цыган ВН. Апоптоз в урологии. Наука, СПб., 2007; 25-26
48. Yoneda T, Imaizumi K, Oono K et al. Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276: 13935-13940
49. Nakagawa T, Zhu H, Morishima N et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103
50. Rao RV, Hermel E, Castro-Obregon S et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J Biol Chem 2001; 276: 33869-33874
51. Morishima N, Nakanishi K, Takenouchi H et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 2002; 277: 34287-34294
52. Hitomi J, Katayama T, Eguchi Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165: 347-356
53. Scorrano L, Oakes SA, Opferman JT et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science 2003; 300: 135-139
54. Zong WX, Li C, Hatzivassiliou G et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol 2003; 162: 59-69
55. Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150: 887-894
56. Orrenius S, Zhivotovsky B, Nicotera P. Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 2003; 4: 552-565
57. Ryan PM, Bedard K, Breining T, Cribb AE. Disruption of the endoplasmic reticulum by cytotoxins in LLC-PK1 cells. Toxicol Lett 2005; 159: 154-163
58. Muruganandan S, Cribb AE. Calpain-induced endoplasmic reticulum stress and cell death following cytotoxic damage to renal cells. Toxicol Sci 2006; 94 (1): 118-128
59. Tan Y, Dourdin N, Wu C et al. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2006; 281: 16016-16024
60. Gallego-Sandin S, Alonso MT, Garcia-Sancho J. Calcium homeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem J 2011; 437 (3): 469-475
61. Lin JH, Li H, Yasumura D et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 2007; 318: 944-949
62. Rurkowski DT, Arnold SM, Miller CN et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and proapoptotic mRNAs and proteins. PLoS Biol 2006; 4: e374
63. Nakanishi K, Sudo T, Morishima N. Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development. J Cell Biol 2005; 169: 555-560
64. Wu J, Kaufman RJ. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 2006; 13: 374-384
65. Rush JS, Sweitzer T, Kent C et al. Biogenesis of the endoplasmic reticulum in activated B lymphocytes: temporal relationships between the induction of protein N-glycosylation activity and the biosynthesis of membrane protein and phospholipid. Arch Biochem Biophys 1991; 84: 63-70
66. Reimold AM, Iwakoshi NN, Manis J et al. Plasma cell differentiation requires the transcription factor XBP1. Nature 2001; 412: 300-307
67. Zhang K, Wong HN, Song B et al. The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 2005; 115: 268-281
68. Iwakoshi NN, Lee AH, Vallabhajosyula P et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP1. Nat Immun 2003; 4: 321-329
69. Drori A, Tirosh B. Regulation of immunoglobulin synthesis, modification, and trafficking by unfolded protein response a quantitative approach. Methods Enzymol 2011; 491: 309-325
70. Delepine M, Nicolino M, Barrett T et al. EIFAK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 2000; 25: 406-409
71. Harding HP, Zeng H, Zhang Y et al. Diabetes mellitus and exocrine pancreatic dysfunction in perk -/- mice reveals a role for translational control in secretory cell survival. Mol Cell 2001; 7: 1153-1163
72. Reimold AM, Etkin A, Clauss I et al. An essential role in liver development for transcription factor XBP-1. Genes Dev 2000; 14: 152-157
73. Yang X, Matsuda K, Bialek P et al. ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry syndrome. Cell 2004; 117: 387-398
74. Zhang P, McGrath B, Li S et al. The PERK eukaryotic initiation factor 2α kinase is required for the development of skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 2002; 22: 3864-3874
75. Nakanishi K, Dohmae N, Morishima N. Endoplasmic reticulum stress increases myofiber formation in vitro. FASEB J 2007; 21: 2994-3003
76. Ostergaard L, Simonsen U, Eskildsen-Helmond Y et al. Proteomics reveals lowering oxygen alters cytoskeletal and endoplasmic stress proteins in human endothelial cells. Proteomics 2009; 19: 4457-4467
77. Werno C, Zhou J, Brüne B. A 23187 ionomycin and thapsigargin upregulate mRNA of HIF-1 alpha via endoplasmic reticulum stress rather than a rise in intracellular calcium. J Cell Physiol 2008; 215: 798-714
78. Gotoh T, Mori M. Nitric oxide and endoplasmic reticulum stress. Arterioscler Thromb Vasc Biol 2006; 26 (7): 1439-1446
79. Gotoh T, Oyadomari S, Mori K, Mori M. Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP. J Biol Chem 2002; 277 (14): 12343-12350
80. De Gracia DJ, Montie HL. Cerebral ischemia and the unfolded protein response. J Neurochem 2004; 91: 1-8
81. Kohno K., Higuchi T, Ohta S et al. Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil. Neurosci Lett 1997; 224: 17-20
82. Xu KY, Huso DL, Dawson TM et al. Nitric oxide synthase in cardiac sarcoplasmic reticulum. Proc Sci USA 1999; 96: 657-662
83. Oyadomari S, Takeda K, Takiguchi M et al. Nitric oxideinduced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway. Proc Natl Acad Sci USA 2001; 98 (19): 10845-10850
84. Inagi R. Endoplasmic reticulum stress as a progression factor for kidney injury. Curr Opin Pharmacol 2010; 10 (2): 156-165
85. Dickhout JG, Hossain GS, Pozza LM et al. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis. Arterioscler Thromb Vasc Biol 2005; 25: 2623-2629
86. Malhotra JD, Miao H, Zhang K et al. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. Proc Natl Sci USA 2008; 105 (47): 18525-18530
87. Hayashi T, Saito A, Okuno S et al. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal death. J Cereb Blood Flow Metabol 2003; 23: 1117-1128
88. Yokouchi M, Hiramatsu N, Hayakawa K et al. Involvement of selective reactive oxygen species upstream of proapoptotic branches of unfolded protein response. J Biol Chem 2008; 283 (7): 4252-4260
89. Cullinan SB, Diehl JA. Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway. Int J Biochem Cell Biol 2006; 38 (3): 317-332
90. Back SH, Scheuner D, Han J et al. Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells. Cell Metab 2009; 10: 13-26
91. Viner RI, Hühmer AF, Bigelow DJ, Schöneich C. The oxidative inactivation of sarcoplasmic reticulum Ca2+-ATPase by peroxinitrite. Free Radic Res 1996; 24: 243-259
92. Moreau VH, Castilho RF, Ferreira ST, Carvalho-Alves PC. Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase at submicromolar iron concentrations: evidence for metal-catalyzed oxidation. Free Radic Biol Med 1998; 25: 554-560
93. Kaplan P, Babusikova E, Lehotsky J, Dobrota D. Free radicalinduced protein modification and inhibition of Ca2+-ATPase of cardiac sarcoplasmic reticulum. Mol Cell Biochem 2003; 248: 41-47
94. Brunet S, Thibault L, Lepage G et al. Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ ascorbate-mediated lipid peroxidation. Free Radic Biol Med 2000; 28: 46-54
95. Hung CC, Ichimura T, Stevens JL, Bonventre JV. Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK ½ activation. J Biol Chem 2003; 278 (31): 29317-29326
96. Zhang K, Kaufman RJ. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008; 454: 455-462
97. Lin W, Harding HP, Ron D, Popko B. Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-γ. J Cell Biol 2005; 169: 603-612
98. Endo M, Mori M, Akira S, Gotoh T. C/EBR homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation. J Immunol 2006; 176: 6245-6253
99. Hiramatsu N, Kasai A, Hayakawa K et al. Real-time detection and continuous monitoring of ER stress in vitro and in vivo by ES-TRAP: evidence for systemic transient ER stress during endotoxemia. Nucleic Acids Res 2006; 34: e93
100. Nagaraju K, Casciola-Rosen L, Lundberg I et al. Activation of the endoplasmic reticulum stress response in autoimmune myositis: potential role in muscle fiber damage and dysfunction. Arthritis Rheum 2005; 52: 1824-1835
101. Yamasaki S, Yagishita N, Tsuchimochi K et al. Rheumatoid arthritis as a hyperendoplasmic-reticulum-associated degradation disease. Arthritis Res Ther 2005; 7: 181-186
102. Pahl HL, Baeuerle PA. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB. EMBO J 1995; 14: 2580-2588
103. Jiang HY, Wek SA, McGrath BC et al. Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses. Mol Cell Biol 2003; 23: 5651-5663
104. Deng J, Lu PD, Zhang Y et al. Translational repression mediates activation of nuclear factor-κB by phosphorylated translation initiation factor 2. Mol Cell Biol 2004; 24: 10161-10168
105. Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 2005; 115: 2656- 2664
106. Kaneko M, Niinuma Y, Nomura Y. Activation signal of nuclear factor-κB in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2. Biol Pharm Bull 2003; 26: 931-935
107. Hu P, Han Z, Couvillon AD et al. Autocrine tumor necrosis factor-α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and downregulation of TRAF2 expression. Mol Cell Biol 2006; 26: 3071-3084
108. Shkoda A, Ruiz PA, Daniel H et al. Interleukin-10 blocked endoplasmic reticulum stress in intestinal epithelial cells: impact on chronic inflammation. Gastroenterology 2007; 132: 190-207
109. Maguire JA, Mulugeta S, Beers MF. Endoplasmic reticulum stress induced by surfactant protein C BRICHOS mutants promotes proinflammatory signaling by epithelial cells. Am J Respir Cell Mol Biol 2011; 44 (3): 404-414
110. Fougeray S, Bouvier N, Beaune P et al. Metabolic stress promotes renal tubular inflammation by triggering the unfolded protein response. Cell Death Dis 2011; 2: e143
111. Takano Y, Hiramatsu N, Okamura M et al. Suppression of cytokine response by GATA inhibitor K-7174 via unfolded protein response. Biochem Biophys Res Commun 2007; 360: 470-475
112. Hayakawa K, Hiramatsu N, Okamura M et al. Blunted activation of NF-κB and NF-κB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response. Biochem Biophys Res Commun 2008; 365: 47-53
113. Hayakawa K, Hiramatsu N, Okamura M et al. Acquisition of energy to proinflammatory cytokines in nonimmune cells through endoplasmic reticulum stress response: a mechanism for subsidence of inflammation. J Immunol 2009; 182 (2): 1182-1191
114. Forman MS, Lee VM, Trojanowski JQ. “Unfolding” pathways is neurodegenerative disease. Trends Neurosci 2003; 26: 407-410
115. Onuki R, Bando Y, Suyama E et al. An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer’s disease. EMBO J 2004; 23: 959-968
116. Hoozemans JJ, Veerhuis R, Van Haastert ES et al. The unfolded protein response is activated in Alzheimer’s disease. Acta Neuropathol (Berl) 2005; 110: 165-172
117. Conn KJ, Gao W, McKee A et al. Identification of the protein disulfide isomerase family member PDlp in experimental Parkinson’s disease and Lewy body pathology. Brain Res 2004; 1022 (1-2): 164-172
118. Holtz WA, O’Malley KL. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 2003; 278 (21): 19367-19377
119. Yoshida H. ER stress and diseases. FEBS J 2007; 274: 630-658
120. Kharroubi I, Ladrière L, Cardozo AK et al. Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappa B and endoplasmic reticulum stress. Endocrinology 2004; 145: 5087-5096
121. Karaskov E, Scott C, Zhang L et al. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Endocrinology 2006; 147: 3398-3407
122. Cnop M, Ladrière L, Hekerman P et al. Selective inhibition of eukaryotic translation initiation factor 2alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem 2007; 282: 3989-3997
123. Bach JF. Insulin-dependent diabetes mellitus as an autoimmune disease. Endocr Rev 1994; 15: 516-542
124. Delovitch TL, Singh B. The nonobese diabetic mouse as a model of autoimmune diabetes: immune dysregulation gets the NOD. Immunity 1997; 7: 727-738
125. Nozaki J, Kubota H, Yoshida H et al. The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic β cells. Genes Cells 2004; 9: 261-270
126. Scheuner D, Mierde DV, Song B et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nat Med 2005; 11: 757-764
127. Oyadomari S, Koizumi A, Takeda K et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-induced diabetes. J Clin Invest 2002; 109: 525-532
128. Cnop M, Welsh N, Jonas JC et al. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: many differences, few similarities. Diabetes 2005; 54: 97-107
129. Bradshaw E, Raddassi K, Elyaman W et al. Monocytes from patients with type 1 diabetes spontaneously secrete pro-inflammatory cytokines inducing Th17. J immunol 2009; 183 (7): 4432-4439
130. Araki E, Oyadomari S, Mori M. Impact of endoplasmic reticulum stress pathway on pancreatic beta-cells and diabetes mellitus. Exp Biol Med 2003; 228: 1213-1217
131. Cardozo AK, Ortis F, Storling J et al. Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+-ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells. Diabetes 2005; 54: 452-461
132. Eizirik DL, Flodström M, Karlsen AE, Welsh N. The harmony of spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells. Diabetologia 1996; 39: 875-890
133. Cardozo AK, Heimberg H, Heremans Y et al. A comprehensive analysis of cytokine-induced and nuclear factor-kappa Bdependent genes in primary rat pancreatic beta-cells. J Biol Chem 2001; 276: 48879-48886
134. Casciola-Rosen LA, Anhalt GJ, Rosen A. DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J Exp Med 1995; 182: 1625-1634
135. Butler AE, Janson J, Bonner-Weir S et al. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes 2003; 52: 102-110
136. Marchetti P, Bulgiani M, Lupi R et al. The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients. Diabetologia 2007; 50 (12): 2486-2494
137. Nakatani Y, Kaneto H, Kawamori D et al. Involvement of endoplasmic reticulum stress in insulin resistance and diabetes. J Biol Chem 2005; 280 (1): 847-851
138. Ozcan U, Cao Q, Yilmaz E et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004; 206: 457-461
139. Ozcan U, Yilmaz E, Ozcan L et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006; 313: 1137-1140
140. Toth A, Nickson P, Mandl A et al. Endoplasmic reticulum stress as a novel therapeutic target in heart diseases. Cardiovasc Hematol Disord Drug Targets 2007; 7 (3): 205-218
141. Groenendyk J, Sreenivasaiah PK, Kim do H et al. Biology of endoplasmic reticulum stress in the heart. Cir Res 2010; 107 (10): 1185-1197
142. Minamino T, Kitakaze M. ER stress in cardiovascular disease. J Mol Cell Cardiol 2010; 48 (6): 1105-1110
143. Aleshin AN, Sawa Y, Kitagawa-Sakakida S et al. 150-kDa oxygen-regulated protein attenuates myocardial ischemia-reperfusion injury in rat heart. J Mol Cell Cardiol 2005; 38: 517-525
144. Azfer A, Niu J, Rogers LM et al. Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am J Physiol Heart Circ Physiol 2006; 291: H1411-H1420
145. Thuerauf DJ, Marcinko M, Gude N et al. Activation of the unfolded protein response in infracted mouse heart and hypoxic cultured cardiac myocytes. Circ Res 2006; 99 (3): 275-282
146. Martindale JJ, Fernandez R, Thuerauf D et al. Endoplasmic reticulum stress gene induction and protection from ischemia/ reperfusion injury in the hearts of transgenic mice with a tamoxifenregulated form of ATF6. Circ Res 2006; 98 (9): 1186-1193
147. Miyazaki Y, Kaikita K, Endo M et al. C/EBP homologous protein deficiency attenuates myocardial reperfusion injury by inhibiting myocardial apoptosis and inflammation. Arterioscler Thromb Vasc Biol 2011; 31 (5): 1124-1132
148. Xin W, Lu X, Li X et al. Attenuation of endoplasmic reticulum stress-related myocardial apoptosis by SERCA2a gene delivery in ischemic heart disease. Mol Med 2011; 17 (3-4): 201-210
149. Lu F, Tian Z, Zhang W et al. Calcium-sensing receptors induce apoptosis in rat cardiomyocytes via the endo(sarco)plasmic reticulum pathway during hypoxia/reoxygenation. Basic Clin Pharmacol Toxicol 2010; 106 (5): 396-405
150. Yeh C-H, Chen T-P, Wang Y-C et al. AMP-activated protein kinase activation during cardioplegia-induced hypoxia/reoxygenation injury attenuates cardiomyocytic apoptosis via regulation of endoplasmic reticulum stress. Mediators Inflamm 2010; 2010: 130636
151. Belmont PJ, Chen WJ, San Pedro MN et al. Roles for endoplasmic reticulum-associated degradation and the novel endoplasmic reticulum stress response gene derlin-3 in the ischemic heart. Circ Res 2010; 106: 307-316
152. Toko H, Takahashi H, Kayama Y et al. ANF6 is important under both pathological and physiological states in the heart. J Mol Cell Cardiol 2010; 49 (1): 113-120
153. Toldo S, Severino A, Abbate A, Baldi A. The role of PDI as a survival factor in cardiomyocyte ischemia. Methods Enzymol 2011; 489: 47-65
154. Karki P, Fliegel L. Overexpression of the NHE1 isoform of the Na(+)/H(+) exchanger causes elevated apoptosis in isolated cardiomyocytes after hypoxia/reoxygenation challenge. Mol Cell Biochem 2010; 338 (1-2): 47-57
155. Зверев ЯФ, Брюханов ВМ. Ингибирование Na+/H+ обмена как новый подход к защите миокарда от ишемического и реперфузионного повреждения. Обзоры клин фармакол и лек терап 2003; 2 (3): 16-34
156. Zhang Z-Y, Liu X-H, Hu W-C et al. The calcineurin-myocyte enhancer factor 2c pathway mediates cardiac hypertrophy induced by endoplasmic reticulum stress in neonatal cardiomyocytes. Am J Physiol Heart Circulat Physiol 2010; 298 (5): H1499-H1509
157. Dickhout JG, Carlisle RE, Austin RC. Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease. Endoplasmic reticulum stress as a mediator of pathogenesis. Circ Res 2011; 108: 629-642
158. Okada K, Minamino T, Tsukamoto Y et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004; 110 (6): 705-712
159. Wu T, Dong Z, Geng J et al. Valsartan protects against ER stress-induced myocardial apoptosis via CHOP/Puma signaling pathway in streptozotocin-induced diabetic rats. Eur J Pharm Sci 2011; 42 (5): 496-502
160. Hamid T, Guo SZ, Kingery JR et al. Cardiomyocyte NF- B p65 promotes adverse remodeling, apoptosis, and endoplasmic reticulum stress in heart failure. Cardiovasc Res 2011; 89 (1): 129-138
161. Sun Y, Liu G, Song T et al. Upregulation of GRP78 and caspase-12 in diastolic failing heart. Acta Biochim Pol 2008; 55 (3): 511-516
162. Avery J, Etzion S, DeBosch BJ et al. TRB3 function in cardiac endoplasmic reticulum stress. Cir Res 2010;106 (9): 1516-1523
163. Isodono K, Takahashi T, Imoto H et al. PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes. PLoS One 2010; 5 (3): e9746
164. Hamada H, Suzuki M, Yuasa S et al. Dilated cardiomyopathy caused by aberrant endoplasmic reticulum quality control in mutant KDEL receptor transgenic mice. Mol Cell Biol 2004; 24 (18): 8007-8017
165. Mao W, Fukuoka S, Iwai C et al. Cardiomyocyte apoptosis in autoimmune cardiomiopathy: mediated via endoplasmic reticulum stress and exaggerated by norepinephrine. Am J Physiol Heart Circ Physiol 2007; 293 (3): H1636-H1645
166. Mao W, Iwai C, Liu J et al. Darbepoetin alpha exerts cardioprotective effect in autoimmune cardiomyopathy via reduction of ER stress and activation of the PI3K/Akt and STAT3 pathways. J Mol Cell Cardiol 2008; 45 (2): 250-260
167. Shimazaki H, Watanabe K, Veeraveedu PT et al. The antioxidant edaravone attenuates ER-stress-mediated cardiac apoptosis and dysfunction in rats with autoimmune myocarditis. Free Radic Res 2010; 44 (9): 1082-1090
168. Sukumaran V, Watanabe K, Veeraveedu PT et al. Olmesartan, an AT1 antagonist, attenuates oxidative stress, endoplasmic reticulum stress and cardiac inflammatory mediators in rats with heart failure induced by experimental autoimmune myocarditis. Int J Biol Sci 2011; 7 (2): 154-167
169. Werstuck GH, Lentz SR, Dayal S et al. Homocysteineinduced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 2001; 107: 1263-1273
170. Myoishi M, Hao H, Minamino T et al. Increased endoplasmic reticulum stress in atherosclerotic plaques associated with acute coronary syndrome. Circulation 2007; 116 (11): 1226-1233
171. Tsukano H, Gotoh T, Endo M et al. The endoplasmic reticulum stress-C/EBP homologous protein pathway-mediated apoptosis in macrophages contributes to the instability of atherosclerotic plaques. Arterioscler Thromb Vasc Biol 2010; 30 (10): 1925-1932
172. Feldman DE, Chauhan V, Koong AC. The unfolded protein response: a novel component of the hypoxic stress response in tumors. Mol Cancer Res 2005; 3: 597-605
173. Ledoux S, Yang R, Friedlander G, Laouari D. Glucose depletion enhances P-glycoprotein expression in hepatoma cells: role of endoplasmic reticulum stress response. Cancer Res 2003; 63: 7284-7290
174. Ozawa K, Tsukamoto Y, Hori O et al. Regulation of tumor angiogenesis by oxygen-regulated protein 150, an inducible endoplasmic reticulum chaperone. Cancer Res 2001; 61: 4206-4213
175. Abcouwer SF, Marjon PL, Loper RK, Vander Jagt DL. Response of VEGF expression to amino acid deprivation and inducers of endoplasmic reticulum stress. Invest Ophthalmol Vis Sci 2002; 43: 2791-2798
176. Ozawa K, Kuwabara K, Tamatani M et al. 150-kDa oxygenregulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death. J Biol Chem 1999; 274: 6397-6404
177. Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110: 1389-1398
178. Kakiuchi C, Iwamoto K, Ishiwata M et al. Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder. Nat Genet 2003; 35: 171-175
179. Kakiuchi C, Ishiwata M, Nanko S et al. Functional polymorphisms of HSPA5: possible association with bipolar disorder. Biochem Biophys Res Commun 2005; 336: 1136-1143
180. Shao L, Sun X, Xu L et al. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci 2006; 78: 1317-1323
181. Tamtani M, Matsuyama T, Yamaguchi A. ORP 150 protects against hypoxia/ischemia-induced neuronal death. Nat Med 2001; 7: 317-323
182. Tajiri S, Oyadomari S, Yano S et al. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ 2004; 11: 403-415
183. Rissanen A, Sivenius J, Jolkkonen J. Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke. Brain Res 2006; 1087: 60-66
Рецензия
Для цитирования:
Зверев Я.Ф., Брюханов В.М. СТРЕСС ЭНДОПЛАЗМАТИЧЕСКОГО РЕТИКУЛУМА ГЛАЗАМИ НЕФРОЛОГА (СООБЩЕНИЕ I). Нефрология. 2012;16(3/1):54-71. https://doi.org/10.24884/1561-6274-2012-16-3/1-54-71
For citation:
Zverev Ya.F., Bruhanov V.M. NEPHROLOGIST’S IMPRESSION OF ENDOPLASMATIC RETICULUM STRESS (TEXT 1). Nephrology (Saint-Petersburg). 2012;16(3/1):54-71. (In Russ.) https://doi.org/10.24884/1561-6274-2012-16-3/1-54-71
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