The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control

Antioxidants and Redox Signaling

Volumn 8, Issue 9-10, 2006, Pages 1391-1418

  Görlach, Agnes ^a   Klappa, Peter ^b   Kietzmann, Thomas ^c  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF KENT   (United Kingdom)

^c Rheinland Pfälzische Technische Universität Kaiserslautern Landau   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; ACTIVATING TRANSCRIPTION FACTOR 6; ADENOSINE TRIPHOSPHATE; AMINO ACID OXIDASE; ANTIOXIDANT; ARACHIDONIC ACID; CALCIUM; CALCIUM BINDING PROTEIN; CALRETICULIN; CYTOCHROME P450; GLUCOSE OXIDASE; GLUCOSE REGULATED PROTEIN 78; INOSITOL 1,4,5 TRISPHOSPHATE; OXIDOREDUCTASE; PROTEIN BAK; PROTEIN BAX; PROTEIN BID; PROTEIN DISULFIDE ISOMERASE; PROTEIN IRE1; PROTEIN SERINE THREONINE KINASE; PYRROLIDINE DITHIOCARBAMATE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RYANODINE RECEPTOR; SUPEROXIDE DISMUTASE; THIOL; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF2; XANTHINE OXIDASE;

ANTIOXIDANT ACTIVITY; CALCIUM HOMEOSTASIS; CATALYST; CELL DEATH; CELL NUCLEUS; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ERO1 GENE; GENE; GENE MUTATION; HUMAN; ISOMERIZATION; MITOCHONDRION; NONHUMAN; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SYNTHESIS; REDUCTION; REGULATORY MECHANISM; REVIEW; SACCHAROMYCES CEREVISIAE; SECOND MESSENGER; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; SYSTEMATIC REVIEW; TRANSCRIPTION REGULATION;

ANIMALS; CALCIUM; ENDOPLASMIC RETICULUM; HOMEOSTASIS; HUMANS; MODELS, BIOLOGICAL; OXIDATION-REDUCTION; PROTEIN FOLDING; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION;

EID: 33750902737     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.1391     Document Type: Review

References (270)

1. Alam J, Stewart D, Touchard C, Boinapally S, Choi AM, and Cook JL. Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J Biol Chem 274: 26071-26078, 1999.
2. Alanen HI, Salo KE, Pekkala M, Siekkinen HM, Pirneskoski A, and Ruddock LW. Defining the domain boundaries of the human protein disulfide isomerases. Antioxid Redox Signal 5: 367-374, 2003.
3. Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, and Sitia R. Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J 22: 5015-5022, 2003.
4. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, and Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 21: 835-844, 2002.
5. Aridor M and Hannan LA. Traffic jam: a compendium of human diseases that affect intracellular transport processes. Traffic 1: 836-851, 2000.
6. Babior BM. The leukocyte NADPH oxidase. Isr Med Assoc J 4: 1023-1024, 2002.
7. Banhegyi G, Lusini L, Puskas F, Rossi R, Fulceri R, Braun L, Mile V, di Simplicio P, Mandl J, and Benedetti A. Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles. J Biol. Chem 274: 12213-12216, 1999.
8. Bass R, Ruddock LW, Klappa P, and Freedman RB. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 279: 5257-5262, 2004.
9. Bassani JW Yuan W, and Bers DM. Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am J Physiol 268: C1313-C1319, 1995.
10. Benayoun B, Esnard-Feve A, Castella S, Courty Y, and Esnard F. Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family. J Biol Chem 276: 13830-13837, 2001.
11. Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, and Braakman I. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. EMBO J 19: 4493-4502, 2000.
12. Bernardi P, Scorrano L, Colonna R, Petronilli V, and Di Lisa F. Mitochondria and cell death. Mechanistic aspects and methodological issues. Eur J Biochem 264: 687-701, 1999.
13. Berridge MJ. Calcium signalling and cell proliferation. Bioessays 17: 491-500, 1995.
14. Berridge MJ. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32: 235-249, 2002.
15. Berridge MJ, Bootman MD, and Roderick HL. Calcium signalling: dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol 4: 517-529, 2003.
16. Bertolotti A, Zhang Y, Hendershot LM, Harding HP, and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332, 2000.
17. Blais JD, Filipenko V, Bi M, Harding HP, Ron D, Koumenis C, Wouters BG, and Bell JC. Activating transcription factor 4 is translationally regulated by hypoxic stress. Mol Cell Biol 24: 7469-7482, 2004.
18. Boraso A and Williams AJ. Modification of the gating of the cardiac sarcoplasmic reticulum Ca(2+)-release channel by H2O2 and dithiothreitol. Am J Physiol 267: H1010-H1016, 1994.
19. Bowie AG and O'Neill LAJ. Vitamin C inhibits NF-kappa B activation by TNF via the activation of p38 mitogen-activated protein kinase. J Immunol 165: 7180-7188, 2000.
20. Brigelius-Flohe R, Banning A, and Schnurr K. Selenium-dependent enzymes in endothelial cell function. Antioxid Redox Signal 5: 205-215, 2003.
21. Brostrom CO and Brostrom MA. Regulation of translational initiation during cellular responses to stress. Prog Nucl Acid Res Mol Biol 58: 79-125, 1998.
22. Brostrom MA and Brostrom CO. Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium 34: 345-363, 2003.
23. Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, and Durham HD. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J Neurochem 72: 693-699, 1999.
24. Bulleid NJ and Freedman RB. Defective co-translational formation of disulfide bonds in protein disulfide-isomerase-deficient microsomes. Nature 335: 649-651, 1988.
25. Burdakov D, Petersen OH, and Verkhratsky A. Intraluminal calcium as a primary regulator of endoplasmic reticulum function. Cell Calcium 38: 303-310, 2005.
26. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, and Sitia R. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275: 4827-4833, 2000.
27. Cai H and Harrison DG. Endothelial dysfunction in cardiovascular diseases-The role of oxidant stress. Circ Res 87: 840-844, 2000.
28. Calfon M, Zeng H, Urano F, Till JH, Hubbard SR, Harding HP, Clark SG, and Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415: 92-96, 2002.
29. Camacho P and Lechleiter JD. Calreticulin inhibits repetitive intracellular Ca2+ waves. Cell 82: 765-771, 1995.
30. Caroppo R, Colella M, Colasuonno A, DeLuisi A, Debellis L, Curci S, and Hofer AM. A reassessment of the effects of luminal [Ca2+] on inositol 1,4,5-trisphosphate-induced Ca2+ release from internal stores. J Biol Chem 278: 39503-39508, 2003.
31. Chakravarthi S and Bulleid NJ. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J Biol Chem 279: 39872-39879, 2004.
32. Cheng H, Lederer MR, Xiao RP, Gomez AM, Zhou YY, Ziman B, Spurgeon H, Lakatta EG, and Lederer WJ. Excitation-contraction coupling in heart: new insights from Ca2+ sparks. Cell Calcium 20: 129-140, 1996.
33. Ching LL, Williams AJ, and Sitsapesan R. Evidence for Ca(2+) activation and inactivation sites on the luminal side of the cardiac ryanodine receptor complex. Circ Res 87: 201-206, 2000.
34. Clapham DE. Calcium signaling. Cell 80: 259-268, 1995.
35. Cooper GR, Brostrom CO, and Brostrom MA. Analysis of the endoplasmic reticular Ca2+ requirement for alpha1-antitrypsin processing and transport competence. Biochem J 325: 601-608, 1997.
36. Coppock DL, Cina-Poppe D, and Gilleran S. The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Genomics 54: 460-468, 1998.
37. Corbett EF and Michalak M. Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem Sci 25: 307-311, 2000.
38. Corbett EF, Oikawa K, Francois P, Tessier DC, Kay C, Bergeron JJ, Thomas DY, Krause KH, and Michalak M. Ca2+ regulation of interactions between endoplasmic reticulum chaperones. J Biol Chem 274: 6203-6211, 1999.
39. Crompton M, Virji S, Doyle V, Johnson N, and Ward JM. The mitochondrial permeability transition pore. Biochem Soc Symp 66: 167-179, 1999.
40. Cullinan SB and Diehl JA. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J Biol Chem 279: 20108-20117, 2004.
41. Cullinan SB, Zhang D, Hannink M, Arvisais E, Kaufman RJ, and Diehl JA. Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol Cell Biol 23: 7198-7209, 2003.
42. Cunnea PM, Miranda-Vizuete A, Bertoli G, Simmen T, Damdimopoulos AE, Hermann S, Leinonen S, Huikko MP, Gustafsson JA, Sitia R, and Spyrou G. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278: 1059-1066, 2003.
43. Cuozzo JW and Kaiser CA. Competition between glutathione and protein thiols for disulfide-bond formation. Nat Cell Biol 1: 130-135, 1999.
44. Darby NJ and Creighton TE. Catalytic mechanism of Dsba and Its comparison With that of protein disulfide-isomerase. Biochemistry 34: 3576-3587, 1995.
45. Darby NJ and Creighton TE. Characterization of the active-site cysteine residues of the thioredoxin-like domains of protein disulfide-isomerase. Biochemistry 34: 16770-16780, 1995.
46. Darby NJ and Creighton TE. Functional properties of the individual thioredoxin-like domains of protein disulfide-isomerase. Biochemistry 34: 11725-11735, 1995.
47. Demaurex N and Frieden M. Measurements of the free luminal ER Ca(2+) concentration with targeted "cameleon" fluorescent proteins. Cell Calcium 34: 109-119, 2003.
48. Dinkova-Kostova AT, Holtzclaw WD, and Wakabayashi N. Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein. Biochemistry 44: 6889-6899, 2005.
49. Donoso P, Prieto H, and Hidalgo C. Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle. Biophys J 68: 507-515, 1995.
50. Dorner AJ, Wasley LC, and Kaufman RJ. Increased synthesis of secreted proteins induces expression of glucose-regulated proteins in butyrate-treated Chinese hamster ovary cells. J Biol Chem 264: 20602-20607, 1989.
51. Dunn A, Luz JM, Natalia D, Gamble JA, Freedman RB, and Tuite MF. Protein disulfide-isomerase (Pdi) is required for the secretion of a native disulfide-bonded protein from Saccharomyces cerevisiae. Biochem Soc Trans 23: S78-S78, 1995.
52. Dykens JA. Isolated cerebral land cerebellar mitochondria produce free radicals when exposed to elevated CA2+ and Na+: implications for neurodegeneration. J Neurochem 63: 584-591, 1994.
53. Edman JC, Ellis L, Blacher RW, Roth RA, and Rutter WJ. Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin. Nature 317: 267-270, 1985.
54. Ellgaard L and Ruddock LW. The human protein disulfide isomerase family: substrate interactions and functional properties. EMBO Rep 6: 28-32, 2005.
55. Epstein CJ, Goldberger RF, and Anfinsen CB. The genetic control of tertiary protein structure: studies with model systems. Cold Spring Harbor Symp Quant Biol 28: 439-449, 1963.
56. Ermak G and Davies KJ. Calcium and oxidative stress: from cell signaling to cell death. Mol Immunol 38: 713-721, 2002.
57. Estes SD, Stoler DL, and Anderson GR. Normal fibroblasts induce the C/EBP beta and ATF-4 bZIP transcription factors in response to anoxia. Exp Cell Res 220: 47-54, 1995.
58. Fagioli C, Mezghrani A, and Sitia R. Reduction of interchain disulfide bonds precedes the dislocation of Ig-mu chains from the endoplasmic reticulum to the cytosol for proteasomal degradation. J Biol Chem 276: 40962-40967, 2001.
59. Farmery MR, Allen S, Allen AJ, and Bulleid NJ. The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system. J Biol Chem 275: 14933-14938, 2000.
60. Favre CJ, Schrenzel J, Jacquet J, Lew DP, and Krause KH. Highly supralinear feedback inhibition of Ca2+ uptake by the Ca2+ load of intracellular stores. J Biol Chem 271: 14925-14930, 1996.
61. Feng W, Liu G, Allen PD, and Pessah IN. Transmembrane redox sensor of ryanodine receptor complex. J Biol Chem 275: 35902-35907, 2000.
62. Ferrari DM, Nguyen Van P, Kratzin HD, and Soling HD. ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. Eur J Biochem 255: 570-579, 1998.
63. Ferrari DM and Soling HD. The protein disulfide-isomerase family: unravelling a string of folds. Biochem J 339: 1-10, 1999.
64. Fewell SW, Travers KJ, Weissman JS, and Brodsky JL. The action of molecular chaperones in the early secretory pathway. Annu Rev Genet 35: 149-191, 2001.
65. Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 52: 3-6, 2001.
66. Forman HJ, Torres M, and Fukuto J. Redox signaling. Mol Cell Biol 234: 49-62, 2002.
67. Forman MS, Lee VM, and Trojanowski JQ. 'Unfolding' pathways in neurodegenerative disease. Trends Neurosci 26: 407-410, 2003.
68. Frand AR and Kaiser CA. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1: 161-170, 1998.
69. Frand AR and Kaiser CA. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4: 469-477, 1999.
70. Frand AR and Kaiser CA. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol Biol Cell 11: 2833-2843, 2000.
71. Freedman RB, Gane PJ, Hawkins HC, Hlodan R, McLaughlin SH, and Parry JW. Experimental and theoretical analyses of the domain architecture of mammalian protein disulfide-isomerase. Biol Chem 379: 321-328, 1998.
72. Freedman RB and Klappa P. Protein disulfide isomerase: a catalyst of thiol:disulfide interchange and associated protein folding. In: Molecular Chaperones and Protein Folding, Bukau B, ed., Harwood Academic Press, London, 1999, pp. 437-459.
73. Freedman RB, Klappa P, and Ruddock LW. Model peptide substrates and ligands in analysis of action of mammalian protein disulfide isomerase. Methods Enzymol 348: 342-354, 2002.
74. Freedman RB, Klappa P, and Ruddock LW. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3: 136-140, 2002.
75. Freeman BA and Crapo JD. Free radicals and tissue injury. Lab Invest 47: 412-426, 1982.
76. Gelebart P, Opas M, and Michalak M. Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37: 260-266, 2005.
77. Gerber J, Muhlenhoff U, Hofhaus G, Lill R, and Lisowsky T. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/A1rp protein family. J Biol Chem 276: 23486-23491, 2001.
78. Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, and Kurtz A. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha, Eur J Biochem 270: 2228-2235, 2003.
79. Goldberger RF, Epstein CJ, and Anfinsen CB. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem 238: 628-635, 1963.
80. Goldstein JL, DeBose-Boyd RA, and Brown MS. Protein sensors for membrane sterols. Cell 124: 35-46, 2006.
81. Gorlach A. Redox regulation of the coagulation cascade. Antioxid Redox Signal 7: 1398-1404, 2005.
82. Gorlach A, Kietzmann T, and Hess J. Redox signaling through NADPH oxidases: involvement in vascular proliferation and coagulation. Ann NY Acad Sci 973: 505-507, 2002.
83. Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C, and Fass D. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci USA 103: 299304, 2006.
84. Gross E, Sevier CS, Vala A, Kaiser CA, and Fass D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol 9: 61-67, 2002.
85. Gunther R, Srinivasan M, Haugejorden S, Green M, Ehbrecht IM, and Kuntzel H. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem 268: 7728-7732, 1993.
86. Gyorke I and Gyorke S. Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites. Biophys J 75: 2801-2810, 1998.
87. Gyorke I, Hester N, Jones LR, and Gyorke S. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 86: 2121-2128, 2004.
88. Han S, Schiefer A, and Isenberg G. Ca2+ load of guinea-pig ventricular myocytes determines efficacy of brief Ca2+ currents as trigger for Ca2+ release. J Physiol 480: 411-421, 1994.
89. Harding HP, Zhang Y, and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271-274, 1999.
90. Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, Calfon M, Sadri N, Yun C, Popko B, Paules R, Stojdl DF, Bell JC, Hettmann T, Leiden JM, and Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633, 2003.
91. Hayakawa M, Miyashita H, Sakamoto I, Kitagawa M, Tanaka H, Yasuda H, Karin M, and Kikugawa K. Evidence that reactive oxygen species do not mediate NF-kappa B activation. EMBO J 22: 3356-3366, 2003.
92. Hayano T, Inaka K, Otsu M, Taniyama Y, Miki K, Matsushima M, and Kikuchi M. PDI and glutathione-mediated reduction of the glutathionylated variant of human lysozyme. FEBS Lett 328: 203-208, 1993.
93. Haze K, Okada T, Yoshida H, Yanagi H, Yura T, Negishi M, and Mori K. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response. Biochem J 355: 19-28, 2001.
94. Heacock CS and Sutherland RM. Induction characteristics of oxygen regulated proteins. Int J Radiat Oncol Biol Phys 12: 1287-1290, 1986.
95. Hebert DN, Garman SC, and Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol 15: 364-370, 2005.
96. Helenius A and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73: 1019-1049, 2004.
97. Henschke PN and Elliott SJ. Oxidized glutathione decreases luminal Ca2+ content of the endothelial cell ins(1,4,5)P3-sensitive Ca2+ store. Biochem J 312: 485-489, 1995.
98. Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, and Mikoshiba K. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 120: 85-98, 2005.
99. Hirose K and Iino M. Heterogeneity of channel density in inositol-1,4,5-trisphosphate-sensitive Ca2+ stores. Nature 372: 791-794, 1994.
100. Hirota K and Semenza GL. Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases. Biochem Biophys Res Commun 338: 610-616, 2005.
101. Holmberg SR and Williams AJ. The calcium-release channel from cardiac sarcoplasmic reticulum: function in the failing and acutely ischaemic heart. Basic Res Cardiol 87 Suppl 1: 255-268, 1992.
102. Holst B, Tachibana C, and Winther JR. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138: 1229-1238, 1997.
103. Hong M, Li M, Mao C, and Lee AS. Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6. J Cell Biochem 92: 723-732, 2004.
104. Hoober KL, Glynn NM, Burnside J, Coppock DL, and Thorpe C. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J Biol Chem 274: 31759-31762, 1999.
105. Hoober KL, Joneja B, White HB3, and Thorpe C. A sulfhydryl oxidase from chicken egg white. J Biol Chem 271: 30510-30516, 1996.
106. Hoober KL and Thorpe C. Egg white sulfhydryl oxidase: kinetic mechanism of the catalysis of disulfide bond formation. Biochemistry 38: 3211-3217, 1999.
107. Horton JD, Goldstein JL, and Brown MS. SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J Clin Invest 109: 1125-1131, 2002.
108. Houston NL, Fan C, Xiang JQ, Schulze JM, Jung R, and Boston RS. Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol 137: 762-778, 2005.
109. Hu Q, Yu ZX, Ferrans VJ, Takeda K, Irani K, and Ziegelstein RC. Critical role of NADPH oxidase-derived reactive oxygen species in generating Ca2+ oscillations in human aortic endothelial cells stimulated by histamine. J Biol Chem 277: 32546-32551, 2002.
110. Huber-Wunderlich M and Glockshuber R. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3: 161-171, 1998.
111. Hwang C, Lodish HF, and Sinskey AJ. Measurement of glutathione redox state in cytosol and secretory pathway of cultured cells. Methods Enzymol 251: 212-221, 1995.
112. Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
113. Ihara Y, Kageyama K, and Kondo T. Overexpression of calreticulin sensitizes SERCA2a to oxidative stress. Biochem Biophys Res Commun 329: 1343-1349, 2005.
114. Inesi G and de Meis L. Regulation of steady state filling in sarcoplasmic reticulum. Roles of back-inhibition, leakage, and slippage of the calcium pump. J Biol Chem 264: 5929-5936, 1989.
115. Jacobson J and Duchen MR. Mitochondrial oxidative stress and cell death in astrocytes-requirement for stored Ca2+ and sustained opening of the permeability transition pore. J Cell Sci 115: 1175-1188, 2002.
116. Janiszewski M, Lopes LR, Carmo AO, Pedro MA, Brandes RP, Santos CX, and Laurindo FR. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J Biol Chem 280: 40813-40819, 2005.
117. Jessop CE, Chakravarthi S, Watkins RH, and Bulleid NJ. Oxidative protein folding in the mammalian endoplasmic reticulum. Biochem Soc Trans 32: 655-658, 2004.
118. John LM, Lechleiter JD, and Camacho P. Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol 142: 963-973, 1998.
119. Kim PS and Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev 19: 173-202, 1998.
120. Kimata Y, Kimata YI, Shimizu Y, Abe H, Farcasanu IC, Takeuchi M, Rose MD, and Kohno K. Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14: 2559-2569, 2003.
121. Klappa P, Freedman RB, and Zimmermann R. Protein disulfide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation. Eur J Biochem 232: 755-764, 1995.
122. Klappa P, Hawkins HC, and Freedman RB. Interaction between protein disulfide isomerase and peptides. Eur J Biochem 248: 37-42, 1997.
123. Klappa P, Ruddock LW, Darby NJ, and Freedman RB. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 17: 927-935, 1998.
124. Knoblach B, Keller BO, Groenendyk J, Aldred S, Zheng J, Lemire BD, Li L, and Michalak M. ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins. Mol Cell Proteomics 2: 1104-1119, 2003.
125. Kondo S, Murakami T, Tatsumi K, Ogata M, Kanemoto S, Otori K, Iseki K, Wanaka A, and Imaizumi K. OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Nat Cell Biol 7: 186-194, 2005.
126. Koong AC, Auger EA, Chen EY, and Giaccia AJ. The regulation of GRP78 and messenger RNA levels by hypoxia is modulated by protein kinase C activators and inhibitors. Radiat Res 138: S60-S63, 1994.
127. Kourie JI. Interaction of reactive oxygen species with ion transport mechanisms. Am J Physiol 275: C1-C24, 1998.
128. Kowaltowski AJ, Netto LE, and Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J Biol Chem 273: 12766-12769, 1998.
129. Kozutsumi Y, Segal M, Normington K, Gething MJ, and Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464, 1988.
130. Kramer B, Ferrari DM, Klappa P, Pohlmann N, and Soling HD. Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding. Biochem J 357: 83-95, 2001.
131. Kroemer G. Cytochrome c. Curr Biol 9: R468, 1999.
132. Kulp MS, Frickel EM, Ellgaard L, and Weissman JS. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J Biol Chem 281: 876-884, 2006.
133. Kuwabara K, Matsumoto M, Ikeda J, Hori O, Ogawa S, Maeda Y, Kitagawa K, Imuta N, Kinoshita T, Stern DM, Yanagi H, and Kamada T. Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain. J Biol Chem 271: 5025-5032, 1996.
134. Laboissiere MCA, Sturley SL, and Raines RT. The essential function of protein-disulfide isomerase is to unscramble nonnative disulfide bonds. J Biol Chem 270: 28006-28009, 1995.
135. Lamantia ML and Lennarz WJ. The essential function of yeast protein disulfide-isomerase does not reside in its isomerase activity. Cell 74: 899-908, 1993.
136. Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4: 181-189, 2004.
137. Lappi AK, Lensink MF, Alanen HI, Salo KE, Lobell M, Juffer AH, and Ruddock LW. A conserved arginine plays a role in the catalytic cycle of the protein disulfide isomerases. J Mol Biol 335: 283-295, 2004.
138. Lechleiter J, Girard S, Peralta E, and Clapham D. Spiral calcium wave propagation and annihilation in Xenopus laevis oocytes. Science 252: 123-126, 1991.
139. Leonardi A, Vito P, Mauro C, Pacifico F, Ulianich L, Consiglio E, Formisano S, and Di Jeso B. Endoplasmic reticulum stress causes thyroglobulin retention in this organelle and triggers activation of nuclear factor-kappa B via tumor necrosis factor receptor-associated factor 2. Endocrinology 143: 2169-2177, 2002.
140. Li JM and Shah AM. Intracellular localization and pre-assembly of the NADPH oxidase complex in cultured endothelial cells. J Biol Chem 277: 19952-19960, 2002.
141. Li NX and Karin M. Is NF-kappa B the sensor of oxidative stress? FASEB J 13: 1137-1143, 1999.
142. Li SJ, Hong XG, Shi YY, Li H, and Wang CC. Annular arrangement and collaborative actions of four domains of protein disulfide isomerase. A small angle X-ray scattering study in solution. J Biol Chem 281: 6581-6588, 2006.
143. Li Y and Camacho P. Ca2+-dependent redox modulation of SERCA 2b by ERp57. J Cell Biol 164: 35-46, 2004.
144. Liu H, Miller E, van de WB, and Stevens JL. Endoplasmic reticulum stress proteins block oxidant-induced Ca2+ increases and cell death. J Biol Chem 273: 12858-12862, 1998.
145. Liu Q, Berchner-Pfannschmidt U, Moller U, Brecht M, Wotzlaw C, Acker H, Jungermann K, and Kietzmann T. A Fenton reaction at the endoplasmic reticulum is involved in the redox control of hypoxia-inducible gene expression. Proc Natl Acad Sci USA 101: 4302-4307, 2004.
146. Lomax RB, Camello C, Van Coppenolle F, Petersen OH, and Tepikin AV. Basal and physiological Ca(2+) leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons. J Biol Chem 277: 26479-26485, 2002.
147. Lukyanenko V, Gyorke I, and Gyorke S. Regulation of calcium release by calcium inside the sarcoplasmic reticulum in ventricular myocytes. Pflugers Arch 432: 1047-1054, 1996.
148. Lundstrom J and Holmgren A. Determination of the reduction oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32: 6649-6655, 1993.
149. Ma Y and Hendershot LM. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress. Chaperones 7: 222-229, 2002.
150. Matsuo Y, Akiyama N, Nakamura H, Yodoi J, Noda M, and Kizaka-Kondoh S. Identification of a novel thioredoxin-related transmembrane protein. J Biol Chem 276: 10032-10038, 2001.
151. Matsuzawa A, Nishitoh H, Tobiume K, Takeda K, and Ichijo H. Physiological roles of ASK1-mediated signal transduction in oxidative stress- and endoplasmic reticulum stress-induced apoptosis: advanced findings from ASK1 knockout mice. Antioxid Redox Signal 4: 415-425, 2002.
152. Meng X, Zhang C, Chen J, Peng S, Cao Y, Ying K, Xie Y, and Mao Y. Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2. Biochem Genet 41: 99-106, 2003.
153. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, and Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20: 6288-6296, 2001.
154. Michalak M, Robert Parker JM, and Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32: 269-278, 2002.
155. Missiaen L, De Smedt H, Parys JB, and Casteels R. Coactivation of inositol trisphosphate-induced Ca2+ release by cytosolic Ca2+ is loading-dependent. J Biol Chem 269: 7238-7242, 1994.
156. Mogami H, Tepikin AV, and Petersen OH. Termination of cytosolic Ca2+ signals: Ca2+ reuptake into intracellular stores is regulated by the free Ca2+ concentration in the store lumen. EMBO J 17: 435-442, 1998.
157. Molinari M and Helenius A. Glycoproteins form mixed disulfides with oxidoreductases during folding in living cells. Nature 402: 90-93, 1999.
158. Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, and Sitia R. Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. J Biol Chem. 279: 32667-32673, 2004.
159. Mourelatos Z, Gonatas NK, Stieber A, Gurney ME, and Dal Canto MC. The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, pre-clinical stages of the disease. Proc Natl Acad Sci USA 93: 5472-5477, 1996.
160. Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, and Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403: 98-103, 2000.
161. Nakaso K, Yano H, Fukuhara Y, Takeshima T, Wada-Isoe K, and Nakashima K. PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells. FEBS Lett 546: 181-184, 2003.
162. Nguyen T, Sherratt PJ, and Pickett CB. Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu Rev Pharmacol Toxicol 43: 233-260, 2003.
163. Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, Hori S, Kakizuka A, and Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16: 1345-1355, 2002.
164. Norgaard P, Tachibana C, Bruun AW, and Winther JR. Gene regulation in response to protein disulfide isomerase deficiency. Yeast 20: 645-652, 2003.
165. Norgaard P, Westphal V, Tachibana C, Alsoe L, Holst B, and Winther JR. Functional differences in yeast protein disulfide isomerases. J Cell Biol 152: 553-562, 2001.
166. Okabe E, Tsujimoto Y, and Kobayashi Y. Calmodulin and cyclic ADP-ribose interaction in Ca2+ signaling related to cardiac sarcoplasmic reticulum: superoxide anion radical-triggered Ca2+ release. Antioxid Redox Signal 2: 47-54, 2000.
167. Oldershaw KA and Taylor CW. Luminal Ca2+ increases the affinity of inositol 1,4,5-trisphosphate for its receptor. Biochem J 292: 631-633, 1993.
168. Oliver JD, van der Wal FJ, Bulleid NJ, and High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275: 86-88, 1997.
169. Oono K, Yoneda T, Manabe T, Yamagishi S, Matsuda S, Hitomi J, Miyata S, Mizuno T, Imaizumi K, Katayama T, and Tohyama M. JAB1 participates in unfolded protein responses by association and dissociation with IRE1. Neurochem Int 45: 765-772, 2004.
170. Ou WJ, Bergeron JJ, Li Y, Kang CY, and Thomas DY. Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+. J Biol Chem 270: 18051-18059, 1995.
171. Ozawa K, Kondo T, Hori O, Kitao Y, Stern DM, Eisenmenger W, Ogawa S, and Ohshima T. Expression of the oxygen-regulated protein ORP150 accelerates wound healing by modulating intracellular VEGF transport. J Clin Invest 108: 41-50, 2001.
172. Ozawa K, Kuwabara K, Tamatani M, Takatsuji K, Tsukamoto Y, Kaneda S, Yanagi H, Stern DM, Eguchi Y, Tsujimoto Y, Ogawa S, and Tohyama M. 150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death. J Biol Chem 274: 6397-6404, 1999.
173. Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, and Sitia R. Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275: 23685-23692, 2000.
174. Pagani M, Pilati S, Bertoli G, Valsasina B, and Sitia R. The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. FEBS Lett 508: 117-120, 2001.
175. Pahl HL. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol Rev 79: 683-701, 1999.
176. Papaiahgari S, Zhang Q, Kleeberger SR, Cho HY, and Reddy SP. Hyperoxia stimulates an Nrf2-ARE transcriptional response via ROS-EGFR-PI3K-Akt/ERK MAP kinase signaling in pulmonary epithelial cells. Antioxid Redox Signal 8: 43-52, 2006.
177. Parodi AJ. Protein glucosylation and its role in protein folding. Annu Rev Biochem 69: 69-93, 2000.
178. Parys JB, Missiaen L, De Smedt H, and Casteels R. Loading dependence of inositol 1,4,5-trisphosphate-induced Ca2+ release in the clonal cell line A7r5. Implications for the mechanism of quantal Ca2+ release. J Biol Chem 268: 25206-25212, 1993.
179. Patil C and Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13: 349-355, 2001.
180. Patterson RL, Boehning D, and Snyder SH. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annu Rev Biochem 73: 437-465, 2004.
181. Pedruzzi E, Guichard C, Ollivier V, Driss F, Fay M, Prunet C, Marie JC, Pouzet C, Samadi M, Elbim C, O Dowd Y, Bens M, Vandewalle A, Gougerot-Pocidalo MA, Lizard G, and Ogier-Denis E. NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells. Mol Cell Biol 24: 10703-10717, 2004.
182. 181a. Petry A, Djordjevic T, Weitnauer M, Kietzmann T, Hess J, and Görlach A. NOX2 and NOX4 mediate proliferative response in endothelial cells. Antiox Redox Signal 8: 1473-1484, 2006.
183. Pollard MG, Travers KJ, and Weissman JS. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1: 171-182, 1998.
184. Pollock S, Kozlov G, Pelletier MF, Trempe JF, Jansen G, Sitnikov D, Bergeron JJ, Gehring K, Ekiel I, and Thomas DY. Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. EMBO J 23: 1020-1029, 2004.
185. Pottorf WJ, Duckles SP, and Buchholz JN. SERCA function declines with age in adrenergic nerves from the superior cervical ganglion. J Auton Pharmacol 20: 281-290, 2000.
186. Putney JW Jr., Broad LM, Braun FJ, Lievremont JP, and Bird GS. Mechanisms of capacitative calcium entry. J Cell Sci 114: 2223-2229, 2001.
187. Qian T, Herman B, and Lemasters JJ. The mitochondrial permeability transition mediates both necrotic and apoptotic death of hepatocytes exposed to Br-A23187. Toxicol Appl Pharmacol 154: 117-125, 1999.
188. Rao RV, Hermel E, Castro-Obregon S, del Rio G, Ellerby LM, Ellerby HM, and Bredesen DE. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J Biol Chem 276: 33869-33874, 2001.
189. Rizzuto R and Pozzan T. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev 86: 369-408, 2006.
190. Roderick HL, Lechleiter JD, and Camacho P. Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b. J Cell Biol 149: 1235-1248, 2000.
191. Ron D. Translational control in the endoplasmic reticulum stress response. J Clin Invest 110: 1383-1388, 2002.
192. Roth RA and Pierce SB. In vivo cross-linking of protein disulfide isomerase to immunoglobulins. Biochemistry 26: 4179-4182, 1987.
193. Ruoppolo M, Freedman RB, Pucci P, and Marino G. Glutathione-dependent pathways of refolding of RNase T-1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase. Biochemistry 35: 13636-13646, 1996.
194. Russell SJ, Ruddock LW, Salo KE, Oliver JD, Roebuck QP, Llewellyn DH, Roderick HL, Koivunen P, Myllyharju J, and High S. The primary substrate binding site in the b′ domain of ERp57 is adapted for endoplasmic reticulum lectin association. J Biol Chem 279: 18861-18869, 2004.
195. Rutkowski DT and Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol 14: 20-28, 2004.
196. Saitoh M, Nishitoh H, Fujii M, Takeda K, Tobiume K, Sawada Y, Kawabata M, Miyazono K, and Ichijo H. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17: 2596-2606, 1998.
197. Sanchez G, Pedrozo Z, Domenech RJ, Hidalgo C, and Donoso P. Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle. J Mol Cell Cardiol 39: 982-991, 2005.
198. Saran M and Bors W. Radical reactions in vivo-an overview. Radiat Environ Biophys 29: 249-262, 1990.
199. Sarti P, Avigliano L, Gorlach A, and Brune B. Superoxide and nitric oxide-participation in cell communication. Cell Death Differ 9: 1160-1162, 2002.
200. Satoh H, Blatter LA, and Bers DM. Effects of [Ca2+]i, SR Ca2+ load, and rest on Ca2+ spark frequency in ventricular myocytes. Am J Physiol 272: H657-H668, 1997.
201. Scherer NM and Deamer DW. Oxidative stress impairs the function of sarcoplasmic reticulum by oxidation of sulfhydryl groups in the Ca2+-ATPase. Arch Biochem Biophys 246: 589-601, 1986.
202. Schneider MF and Chandler WK. Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature 242: 244-246, 1973.
203. Schroder M and Kaufman RJ. ER stress and the unfolded protein response. Mutat Res 569: 29-63, 2005.
204. Schroder M and Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789, 2005.
205. Schwaller M, Wilkinson B, and Gilbert HF. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. J Biol Chem 278: 7154-7159, 2003.
206. Semenza GL. Hypoxia, clonal selection, and the role of HIF-1 in tumor progression. Crit Rev Biochem Mol Biol 35: 71-103, 2000.
207. Senkevich TG, White CL, Koonin EV, and Moss B. Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc Natl Acad Sci USA 99: 6667-6672, 2002.
208. Sevier CS, Cuozzo JW, Vala A, Aslund F, and Kaiser CA. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulfide bond formation. Nat Cell Biol 3: 874-882, 2001.
209. Shamu CE and Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J 15: 3028-3039, 1996.
210. Shen J, Chen X, Hendershot L, and Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 3: 99-111, 2002.
211. Shen X, Ellis RE, Lee K, Liu CY, Yang K, Solomon A, Yoshida H, Morimoto R, Kurnit DM, Mori K, and Kaufman RJ. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107: 893-903, 2001.
212. Shibata N. Transgenic mouse model for familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Neuropathology 21: 82-92, 2001.
213. Shiu RP, Pouyssegur J, and Pastan I. Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc Natl Acad Sci USA 74: 3840-3844, 1977.
214. Shuttleworth TJ. A re-evaluation of the apparent effects of luminal Ca2+ on inositol 1,4,5-trisphosphate-induced Ca2+ release. Cell Calcium 17: 393-398, 1995.
215. Sidrauski C, Chapman R, and Walter P. The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol 8: 245-249, 1998.
216. Silvennoinen L, Myllyharju J, Ruoppolo M, Orru S, Caterino M, Kivirikko KI, and Koivunen P. Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains. J Biol Chem 279: 13607-13615, 2004.
217. Sitsapesan R and Williams AJ. The gating of the sheep skeletal sarcoplasmic reticulum Ca(2+)-release channel is regulated by luminal Ca2+. J Memb Biol 146: 133-144, 1995.
218. Sitsapesan R and Williams AJ. Regulation of current flow through ryanodine receptors by luminal Ca2+. J Memb Biol 159: 179-185, 1997.
219. Solovyov A, Xiao R, and Gilbert HF. Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem 279: 34095-35100, 2004.
220. Solovyova N, Fernyhough P, Glazner G, and Verkhratsky A. Xestospongin C empties the ER calcium store but does not inhibit InsP3-induced Ca2+ release in cultured dorsal root ganglia neurones. Cell Calcium 32: 49-52, 2002.
221. Solovyova N, Veselovsky N, Toescu EC, and Verkhratsky A. Ca(2+) dynamics in the lumen of the endoplasmic reticulum in sensory neurons: direct visualization of Ca(2+)-induced Ca(2+) release triggered by physiological Ca(2+) entry. EMBO J 21: 622-630, 2002.
222. Squier TC. Oxidative stress and protein aggregation during biological aging. Exp Gerontol 36: 1539-1550, 2001.
223. Squier TC and Bigelow DJ. Protein oxidation and age-dependent alterations in calcium homeostasis. Front Biosci 5: D504-D526, 2000.
224. Srivastava SP, Davies MV, and Kaufman RJ. Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J Biol Chem 270: 16619-16624, 1995.
225. Suh JK and Robertus JD. Yeast flavin-containing monooxygenase is induced by the unfolded protein response. Proc Natl Acad Sci USA 97: 121-126, 2000.
226. Suh J-K, Poulsen LL, Ziegler DM, and Robertus JD. Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum. PNAS 96: 2687-2691, 1999.
227. Suzuki CK, Bonifacino JS, Lin AY, Davis MM, and Klausner RD. Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP. J Cell Biol 114: 189-205, 1991.
228. Suzuki YJ and Ford GD. Superoxide stimulates IP3-induced Ca2+ release from vascular smooth muscle sarcoplasmic reticulum. Am J Physiol 262: H114-H116, 1992.
229. Suzuki YJ, Forman HJ, and Sevanian A. Oxidants as stimulators of signal transduction. Free Radic Biol Med 22: 269-285, 1997.
230. Thorpe C, Hoober KL, Raje S, Glynn NM, Burnside J, Turi GK, and Coppock DL. Sulfliydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys 405: 1-12, 2002.
231. Tian G, Xiang S, Noiva R, Lennarz WJ, and Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124: 61-73, 2006.
232. Tirasophon W, Welihinda AA, and Kaufman RJ. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev 12: 1812-1824, 1998.
233. Tobisawa S, Hozumi Y, Arawaka S, Koyama S, Wada M, Nagai M, Aoki M, Itoyama Y, Goto K, and Kato T. Mutant SOD1 linked to familial amyotrophic lateral sclerosis, but not wild-type SOD1, induces ER stress in COS7 cells and transgenic mice. Biochem Biophys Res Commun 303: 496-503, 2003.
234. Tobiume K, Saitoh M, and Ichijo H. Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer. J Cell Physiol 191: 95-104, 2002.
235. Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, and Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258, 2000.
236. Tsai B, Ye Y, and Rapoport TA. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3: 246-255, 2002.
237. Tu BP, Ho-Schleyer SC, Travers KJ, and Weissman JS. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290: 1571-1574, 2000.
238. Tu BP and Weissman JS. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell 10: 983-994, 2002.
239. Tu BP and Weissman JS. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164: 341-346, 2004.
240. Tu PH, Gurney ME, Julien JP, Lee VM, and Trojanowski JQ. Oxidative stress, mutant SOD1, and neurofilament pathology in transgenic mouse models of human motor neuron disease. Lab Invest 76: 441-456, 1997.
241. Urade R, Okudo H, Kato H, Moriyama T, and Arakaki Y ER-60 domains responsible for interaction with calnexin and calreticulin. Biochemistry 43: 8858-8868, 2004.
242. Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, and Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666, 2000.
243. van Anken E and Braakman I. Endoplasmic reticulum stress and the making of a professional secretory cell. Crit Rev Biochem Mol Biol 40: 269-283, 2005.
244. Van Buul JD, Fernandez-Borja M, Anthony EC, and Hordijk PL. Expression and localization of NOX2 and NOX4 in primary human endothelial cells. Antioxid Redox Signal 7: 308-317, 2005.
245. van Lith M, Hartigan N, Hatch J, and Benham AM. PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. J Biol Chem 280: 1376-1383, 2005.
246. van d, V, Makkinje M, Jansens A, Braakman I, Verkleij AJ, Wirtz KW, and Post JA. Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxid Redox Signal 5: 381-387, 2003.
247. Verkhratsky A. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol Rev 85: 201-279, 2005.
248. Verkhratsky A and Petersen OH. The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death. Eur J Pharmacol 447: 141-154, 2002.
249. Viner RI, Ferrington DA, Williams TD, Bigelow DJ, and Schoneich C. Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle. Biochem J 340: 657-669, 1999.
250. Viner RI, Williams TD, and 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 38: 12408-12415, 1999.
251. Wakabayashi N, Dinkova-Kostova AT, Holtzclaw WD, Kang MI, Kobayashi A, Yamamoto M, Kensler TW, and Talalay P. Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducers. Proc Natl Acad Sci USA 101: 2040-2045, 2004.
252. Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, and Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J 17: 5708-5717, 1998.
253. Wesson DE and Elliott SJ. The H2O2-generating enzyme, xanthine oxidase, decreases luminal Ca2+ content of the IP3-sensitive Ca2+ store in vascular endothelial cells. Microcirculation 2: 195-203, 1995.
254. Wetmore DR and Hardman KD. Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3). Biochemistry 35: 6549-6558, 1996.
255. Williams CH Jr., Chemistry and Biochemistry of Flavoenzymes. CRC Press, Inc., Boca Raton, FL, 1992.
256. Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, and Price DL. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14: 1105-1116, 1995.
257. Xia R, Stangler T, and Abramson JJ. Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators. J Biol Chem 275: 36556-36561, 2000.
258. Xia R, Webb JA, Gnall LL, Cutler K, and Abramson JJ. Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide. Am J Physiol Cell Physiol 285: C215-C221, 2003.
259. Xiao R, Wilkinson B, Solovyov A, Winther JR, Holmgren A, Lundstrom-Ljung J, and Gilbert HF. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279: 49780-49786, 2004.
260. Xu KY, Zweier JL, and Becker LC. Oxygen-free radicals directly attack the ATP binding site of the cardiac Na+,K(+)-ATPase. Ann NY Acad Sci 834: 680-683, 1997.
261. Xue X, Piao JH, Nakajima A, Sakon-Komazawa S, Kojima Y, Mori K, Yagita H, Okumura K, Harding H, and Nakano H. Tumor necrosis factor alpha (TNFalpha) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFalpha. J Biol Chem 280: 33917-33925, 2005.
262. Yano K, Petersen OH, and Tepikin AV. Dual sensitivity of sarcoplasmic/endoplasmic Ca2+-ATPase to cytosolic and endoplasmic reticulum Ca2+ as a mechanism of modulating cytosolic Ca2+ oscillations. Biochem J 383: 353-360, 2004.
263. Ye J, Rawson RB, Komuro R, Chen X, Dave UP, Prywes R, Brown MS, and Goldstein JL. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6: 1355-1364, 2000.
264. Yoneda T, Imaizumi K, Oono K, Yui D, Gomi F, Katayama T, and Tohyama M. 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 276: 13935-13940, 2001.
265. Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M, and Mori K. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response. Mol Cell Biol 21: 1239-1248, 2001.
266. Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJM, and Thomas DY. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273: 6009-6012, 1998.
267. Zeng L, Lu M, Mori K, Luo S, Lee AS, Zhu Y, and Shyy JY. ATF6 modulates SREBP2-mediated lipogenesis. EMBO J 23: 950-958, 2004.
268. Zhang DD and Hannink M. Distinct cysteine residues in Keapl are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 23: 8137-8151, 2003.
269. Zhang DD, Lo SC, Cross JV, Templeton DJ, and Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cu13-dependent ubiquitin ligase complex. Mol Cell Biol 24: 10941-10953, 2004.
270. Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT, Back SH, and Kaufman RJ. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124: 587-599, 2006.