Endoplasmic reticulum stress-induced transcriptional factor CHOP and cardiovascular diseases

Current Hypertension Reviews

Volumn 6, Issue 1, 2010, Pages 55-65

  Gotoh, Tomomi ^a   Endo, Motoyoshi ^a   Oike, Yuichi ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Atherosclerosis; CHOP; Diabetes; ER stress; Inflammation; Ischemia

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN; DNA; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HETERODIMER;

APOPTOSIS; ATHEROSCLEROSIS; BINDING SITE; CARDIOVASCULAR DISEASE; CELL COUNT; CELL DAMAGE; DIABETES MELLITUS; ENDOPLASMIC RETICULUM STRESS; HEART FAILURE; HEART PROTECTION; HUMAN; ISCHEMIA; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 77949752636     PISSN: 15734021     EISSN: None     Source Type: Journal    
DOI: 10.2174/157340210790231717     Document Type: Review

References (123)

1. Gotoh T, Mori, M. Nitric oxide and endoplasmic reticulum stress. (Review). Arterioscler Thromb Vasc Biol 2006; 7: 1439-46.
2. Yoshida H. ER stress and diseases. FEBS J 2007; 274: 630-58.
3. Schröder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74: 739-89.
4. Viner RI, Williams TD, Schoneich C. Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase. Biochemistry 1999; 38: 12408-15.
5. (a) Cardozo AK, Ortis F, Storling J, Feng YM, Rasschaert, J, Tonnesen M, Van Eylen F, Mandrup-Poulsen T, Herchuelz A, Eizirik D.L. 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: 452-61.
6. (b) Verkhratsky A, Toescu EC. Endoplasmic reticulum Ca2+ homeostasis and neuronal death. J Cell Mol Med 2003; 7: 351-61.
7. (c) Denmeade SR, Isaacs JT. The SERCA Pump as a Therapeutic Target. Cancer Biol Ther 2005; 4: 14-22.
8. (d) Zalk R, Lehnart SE, Marks AR. Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem 2007; 76: 367-85.
9. (e) Wuytack F, Raeymaekers L, Missiaen L. Molecular physiology of the SERCA and SPCA pumps. Cell Calcium 2002; 32: 279-305.
10. (f) Taylor CW, Laude AJ. IP3 receptors and their regulation by calmodulin and cytosolic Ca2+. Cell Calcium 2002; 32: 321-34.
11. (g) Rossi D, Sorrentino V. Molecular genetics of ryanodine receptors Ca2+ -release channels. Cell Calcium 2002; 32: 307-19.
12. Meusser B, Hirsch C, Jarosch E, Sommer T. ERAD: the long road to destruction. Nat Cell Biol 2005; 7: 766-72.
13. 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.
14. Takeda K, Matsuzawa A, Nishitoh H, Ichijo H. Roles of MAPKKK ASK1 in stress-induced cell death. Cell Struct Funct 2003; 28: 23-9.
15. Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 2004; 11: 381-89.
16. Marciniak SJ, Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 2006; 86: 1133-49.
17. Ron D, Habener JF. CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. Genes Dev 1992; 6: 439-53.
18. Wang XZ, Lawson B, Brewer JW, et al. Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153). Mol Cell Biol 1996; 16: 4273-80.
19. Endo M, Mori M, Akira S, Gotoh T. C/EBP homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation. J Immunol 2006; 176: 6245-53.
20. Takiguchi M. The C/EBP family of transcription factors in the liver and other organs. Int J Exp Pathol 1998; 79: 369-91.
21. Batchvarova N, Wang X-Z, Ron D. Inhibition of adipogenesis by the stress-induced protein CHOP (Gadd153). EMBO J 1995; 14: 4654-61.
22. Adelmant G, Gilbert JD, Freytag SO. Human translocation liposarcoma-CCAAT/enhancer binding protein (C/EBP) homologous protein (TLS-CHOP) oncoprotein prevents adipocyte differentiation by directly interfering with C/EBPbeta function. J Biol Chem 1998; 273: 15574-81.
23. Tang Q-Q, Lane MD. Role of C/EBP homologous protein (CHOP-10) in the programmed activation of CCAAT/enhancer-binding protein-beta during adipogenesis. Proc Natl Acad Sci USA 2000; 97: 12446-50.
24. Shirakawa K, Maeda S, Gotoh T, et al. CCAAT/enhancer-binding protein homologous protein (CHOP) regulates osteoblast differentiation. Mol Cell Biol 2006; 26: 6105-16.
25. Aman P, Ron D, Mandahl N, et al. Rearrangement of the transcription factor gene CHOP in myxoid liposarcomas with t(12;16)(q13;p11). Genes Chromosomes Cancer 1992; 5: 278-85.
26. Ariyama Y, Shimizu H, Satoh T, et al. Chop-deficient mice showed increased adiposity but no glucose intolerance. Obesity 2007; 15: 1647-56.
27. Marciniak SJ, Yun CY, Oyadomari S, et al. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 2004; 18: 3066-77.
28. Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfoldedprotein response. Nat Cell Biol 2000; 2: 326-32.
29. Bukau B, Weissman J, Horwich, A. Molecular chaperones and protein quality control. Cell 2006; 125: 443-51.
30. Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999; 10: 3787-99.
31. Ye J, Rawson RB, Komuro R, et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 2000; 6: 1355-64.
32. Li M, Baumeister P, Roy B, et al. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stressinduced changes and synergistic interactions with NF-Y and YY1. Mol Cell Biol 2000; 20: 5096-106.
33. Kimata Y, Ishiwata-Kimata Y, Ito T, et al. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol 2007; 179: 75-86.
34. Nadanaka S, Okada T, Yoshida H, Mori K. Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol Cell Biol 2007; 27: 1027-1043.
35. Rutkowski DT, Kaufman RJ. All roads lead to ATF4. Dev Cell 2003; 4: 442-4.
36. Novoa I, Zeng H, Harding HP, Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 2001; 153: 1011-22.
37. Yoshida H, Okada T, Haze K, et al. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 2000; 20: 6755-67.
38. Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. 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: 881-91.
39. Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, Mori K. A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 2003; 4: 265-71.
40. Shen X, Ellis RE, Lee K, et al. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 2001; 107: 893-903.
41. Calfon M, Zeng H, Urano F, et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002; 415: 92-6.
42. Lee K, Tirasophon W, Shen X, et al. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 2002; 16: 452-66.
43. Yoshida H, Oku M, Suzuki M, Mori K. pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J Cell Biol 2006; 172: 565-75.
44. Hosokawa N, Wada I, Hasegawa K, et al. A novel ER alphamannosidase-like protein accelerates ER-associated degradation. EMBO Rep 2001; 2: 415-22.
45. Oda Y, Hosokawa N, Wada I, Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003; 299: 1394-7.
46. Oda Y, Okada T, Yoshida H, Kaufman RJ, Nagata K, Mori K. Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 2006; 172: 383-93.
47. Yamamoto K, Sato T, Matsui T, et al. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell 2007; 13: 365-76.
48. Lindholm D, Wootz H, Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ 2006; 13: 385-92.
49. 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: 982-95.
50. Takiguchi M, Mori M. Transcriptional regulation of genes for ornithine cycle enzymes. [Review] Biochem J 1995; 312: 649-59.
51. 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: 12343-50.
52. 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: 619-33.
53. Wang XZ, Ron D. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science 1996; 272: 1347-49.
54. Wang XZ, Kuroda M, Sok J, et al. Identification of novel stressinduced genes downstream of chop. EMBO J 1998; 17: 3619-30.
55. McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ. Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21: 1249-59.
56. Gotoh T, Terada K, Oyadomari S, Mori M. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 2004; 11: 390-402.
57. Puthalakath H, O'Reilly LA, Gunn P, et al. ER stress triggers apoptosis by activating BH3-only protein Bim. Cell 2007; 129: 1337-49.
58. Oyadomari S, Takeda K, Takiguchi M, et al. Nitric oxide-induced apoptosis in pancreatic beta cells is mediated by the endoplasmic reticulum stress pathway. Proc Natl Acad Sci USA 2001; 98: 10845-50.
59. Kawahara K, Oyadomari S, Gotoh T, Kohsaka S, Nakayama H, Mori M. Induction of CHOP and apoptosis by nitric oxide in p53-deficient microglial cells. FEBS Lett 2001; 506: 135-9.
60. Oyadomari S, Koizumi A, Takeda K, et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest 2002; 109: 525-32.
61. Tsutsumi S, Gotoh T, Tomisato W, et al. Endoplasmic reticulum stress response is involved in nonsteroidal anti-inflammatory druginduced apoptosis. Cell Death Differ 2004; 11: 1009-16.
62. 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: 403-15.
63. Tajiri S, Yano S, Morioka M, Kuratsu J, Mori M, Gotoh T. CHOP is involved in neuronal apoptosis induced by neurotrophic factor deprivation. FEBS Lett 2006; 580: 3462-8.
64. Awai M, Koga T, Inomata Y, et al. NMDA-induced retinal injury is mediated by an endoplasmic reticulum stress-related protein, CHOP/GADD153. J Neurochem 2006; 96: 43-52.
65. Suyama K, Ohmuraya M, Hirota M, et al. C/EBP homologous protein is crucial for the acceleration of experimental pancreatitis. Biochem Biophys Res Commun 2008; 367: 176-82.
66. Endo M, Oyadomari S, Suga S, Mori M, Gotoh T. The Endoplasmic reticulum stress pathway involving CHOP is activated in the lung of the septic shock model mouse. J Biochem (Tokyo) 2005; 138: 501-7.
67. Lamkanfi M, Festjens N, Declercq W, Vanden-Berghe T, Vandenabeele P. Caspases in cell survival, proliferation and differentiation. Cell Death Differ 2007; 14: 44-55.
68. Scott AM, Saleh M. The inflammatory caspases: guardians against infections and sepsis. Cell Death Differ 2007; 14: 23-31.
69. Park S, Cheon S, Cho D. The dual effects of interleukin-18 in tumor progression. Cell Mol Immunol 2007; 4: 329-35.
70. Noguchi T, Ishii K, Fukutomi H, Naguro I, Matsuzawa A, Takeda K, Ichijo H. Requirement of reactive oxygen species-dependent ac tivation of ASK1-p38 MAPK pathway for extracellular ATPinduced apoptosis in macrophage. J Biol Chem 2008; 283: 7657-65.
71. Takeda K, Noguchi T, Naguro I, Ichijo H. Apoptosis signalregulating kinase 1 in stress and immune response. Annu Rev Pharmacol Toxicol 2008; 48: 199-225.
72. Tobiume K, Matsuzawa A, Takahashi T, et al. ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep 2001; 2: 222-8.
73. 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: 1345-55.
74. Oyadomari S, Araki E, Mori M. Endoplasmic reticulum stressmediated apoptosis in pancreatic beta-cells. Apoptosis 2002; 7: 335-45.
75. Ho P-K, Hawkins CJ. Mammalian initiator apoptotic caspases. FEBS J 2005; 272: 5436-53.
76. Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150: 887-94.
77. Yoneda T, Imaizumi K, Oono K, et al. Activation of caspase-12, an endoplastic 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: 13935-40.
78. 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: 33869-74.
79. Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005; 280: 29578-87.
80. Martinon F, Tschopp J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ 2007; 14: 10-22.
81. Reimertz C, Kögel D, Rami A, Chittenden T, Prehn JH. Gene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway. J Cell Biol 2003; 162: 587-97.
82. Li J, Lee B, Lee AS. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J Biol Chem 2006; 281: 7260-70.
83. Kieran D, Woods I, Villunger A, Strasser A, Prehn JH. Deletion of the BH3-only protein puma protects motoneurons from ER stressinduced apoptosis and delays motoneuron loss in ALS mice. Proc Natl Acad Sci USA 2007; 104: 20606-11.
84. Muoio DM, Newgard CB. Mechanisms of disease: molecular and metabolic mechanisms of insulin resistance and beta-cell failure in type 2 diabetes. Nat Rev Mol Cell Biol 2008; 9: 193-205.
85. Danne T, Becker D. Paediatric diabetes: achieving practical, effective insulin therapy in type 1 and type 2 diabetes. Acta Paediatr 2007; 96: 1560-70.
86. Ichinose K, Kawasaki E, Eguchi K. Recent advancement of understanding pathogenesis of type 1 diabetes and potential relevance to diabetic nephropathy. Am J Nephrol 2007; 27: 554-64.
87. Ignarro LJ. Nitric Oxide; biology and Pathology; London: Academic Press 2000.
88. Wang J, Takeuchi T, Tanaka S, et al. A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. J Clin Invest 1999; 103: 27-37.
89. 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 beta cells. Genes Cells 2004; 9: 261-70.
90. Wellen KE, Hotamisligil GS. Inflammation, stress, and diabetes. J Clin Invest 2005; 115: 1111-9.
91. Hotamisligil GS. Inflammation and metabolic disorders. Nature 2006; 444: 860-7.
92. Kaneto H, Matsuoka T-A, Nakatani Y, et al. Oxidative stress, ER stress, and the JNK pathway in type 2 diabetes. J Mol Med 2005; 83: 429-39.
93. Chung J, Nguyen A-K, Henstridge D-C, et al. HSP72 protects against obesity-induced insulin resistance. Proc Natl Acad Sci USA 2008; 105: 1739-44.
94. Harding HP, Ron D. Endoplasmic reticulum stress and the development of diabetes: a review. Diabetes 2002; 51: S455-61.
95. Özcan U, Cao Q, Yilmaz E, et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004; 306: 457-61.
96. Gregor MG, Hotamisligil GS. Adipocyte stress: The endoplasmic reticulum and metabolic disease. J Lipid Res 2007; 48: 1905-14.
97. Zhao L, Ackerman SL. Endoplasmic reticulum stress in health and disease. Curr Opin Cell Biol 2006; 18: 444-52.
98. Yoshiuchi K, Kaneto H, Matsuoka T, et al. Direct monitoring of in vivo ER stress during the development of insulin resistance with ER stress-activated indicator transgenic mice. Biochem Biophys Res Commun 2008; 366: 545-50.
99. Kim D, Jeong S, Kim H, Kim D, Chae S, Chae H. Effects of triglyceride on ER stress and insulin resistance. Biochem Biophys Res Commun 2007; 363: 140-5.
100. Gao L, Laude K, Cai H. Mitochondrial pathophysiology, reactive oxygen species, and cardiovascular diseases. Vet Clin North Am Small Anim Pract 2008; 38: 137-55.
101. Miller RS, Diaczok D, Cooke DW. Repression of GLUT4 expression by the endoplasmic reticulum stress response in 3T3-L1 adipocytes. Biochem Biophys Res Commun 2007; 362: 188-92.
102. Ota T, Gayet C, Ginsberg HN. Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents. J Clin Invest 2008; 118: 316-32.
103. Ozawa K, Miyazaki M, Matsuhisa M, et al. The endoplasmic reticulum chaperone improves insulin resistance in type 2 diabetes. Diabetes 2005; 54: 657-63.
104. Meier JJ. β cell mass in diabetes: a realistic therapeutic target? Diabetologia 2008; 51: 703-13.
105. 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: 1153-63.
106. Hayden MR, Tyagi SC, Kerklo MM, Nicolls MR. Type 2 diabetes mellitus as a conformational disease. J Pancreas 2005; 6: 287-302.
107. Ross R. Atherosclerosis-an inflammatory disease. N Engl J Med 1999; 340: 115-26.
108. Hansson GK. Inflammation, atherosclerosis, and coronary artery disease. N Engl J Med 2005; 352: 1685-95.
109. Maxfield FR, Tabas I. Role of cholesterol and lipid organization in disease. Nature 2005; 438: 612-21.
110. Bonomini F, Tengattini S, Fabiano A, Bianchi R, Rezzani R. Atherosclerosis and oxidative stress. Histol Histopathol 2008; 23: 381-90.
111. Feng B, Yao PM, Li Y, et al. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nat Cell Biol 2003; 5: 781-92.
112. Devries-Seimon T, Li Y, Yao PM, et al. Cholesterol-induced macrophage apoptosis requires ER stress pathways and engagement of the type A scavenger receptor. J Cell Biol 2005; 171: 61-73.
113. Zhou J, Lhotak S, Hilditch BA, Austin RC. Activation of the unfolded protein response occurs at all stages of atherosclerotic lesion development in apolipoprotein E-deficient mice. Circulation 2005; 111: 1814-21.
114. Goldin A, Beckman JA, Schmidt AM, Creager MA. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 2006; 114: 597-605.
115. Nagao K, Yanagita T. Bioactive lipids in metabolic syndrome. Prog Lipid Res 2008; 47: 127-46.
116. Li Y, Ge M, Ciani L, et al. Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: implications for depletion of endoplasmic reticulum calcium stores and apoptosis in cholesterol-loaded macrophages. J Biol Chem 2005; 279: 37030-9.
117. Ferdinandy P, Schulz R, Baxter GF. Interaction of cardiovascular risk factors with myocardial ischemia/reperfusion injury, preconditioning, and postconditioning. Pharmacol Rev 2007; 59: 418-58.
118. Vajdovich P. Free radicals and antioxidants in inflammatory processes and ischemia-reperfusion injury. Vet Clin North Am Small Anim Pract 2008; 38: 31-123.
119. Azfer A, Niu J, Rogers LM, Adamski FM, Kolattukudy PE. Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am J Physiol Heart Circ Physiol 2006; 291: 1411-20.
120. Szegezdi E, Duffy A, O'Mahoney ME, et al. ER stress contributes to ischemia-induced cardiomyocyte apoptosis. Biochem Biophys Res Commun 2006; 349: 1406-11.
121. Myoishi M, Hao H, Minamino T, et al. Increased endoplasmic reticulum stress in atherosclerotic plaques associated with acute coronary syndrome. Circulation 2007; 116: 1226-1233.
122. 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: 705-12.
123. 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: 8007-17.