Proteins of the PDI family: Unpredicted non-ER locations and functions

Journal of Cellular Physiology

Volumn 193, Issue 2, 2002, Pages 154-163

  Turano, Carlo ^a   Coppari, Sabina ^a   Altieri, Fabio ^a   Ferraro, Anna ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEIN DISULFIDE ISOMERASE;

ARTICLE; CELL NUCLEUS; CELL SURFACE; CYTOSOL; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME MECHANISM; ISOMERISM; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN FAMILY; PROTEIN FOLDING; REDUCTION;

ANIMALS; CELL MEMBRANE; CELL NUCLEUS; CYTOSOL; ENDOPLASMIC RETICULUM; EXTRACELLULAR SPACE; HUMANS; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN STRUCTURE, TERTIARY;

VERTEBRATA;

EID: 0036836665     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.10172     Document Type: Article

References (110)

1. Abell BA, Brown DT. 1993. Sindbis virus membrane fusion is mediated by reduction of glycoprotein disulfide bridges at the cell surface. J Virol 67:5496-5501.
2. Altieri F, Maras B, Eufemi M, Ferraro A, Turano C. 1993. Purification of a 57 kDa nuclear matrix protein associated with thiol:protein disulfide oxidoreductase and phospholipase C activities. Biochem Biophys Res Commun 194:992-1000.
3. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R. 2002. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 21:835-844.
4. Belin D, Bost S, Vassalli J-D, Strub K. 1996. A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J 15:468-478.
5. Bennett CF, Balcarek JM, Varrichio A, Crooke ST. 1988. Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334:268-270.
6. Bennett TA, Edwards BS, Sklar LA, Rogelj S. 2000. Sulfhydryl regulation of L-selectin shedding: Phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes. J Immunol 164:4120-4129.
7. Berezney R. 1991. The nuclear matrix: A heuristic model for investigating genomic organization and function in the cell nucleus. J Cell Biochem 47:109-123.
8. Bohring C, Krause E, Habermann B, Krause W. 2001. Isolation and identification of sperm membrane antigens recognized by antisperm antibodies, and their possible role in immunological infertility disease. Mol Hum Reprod 7:113-118.
9. Burgess JK, Hotchkiss KA, Suter C, Dudman NP, Szollosi J, Chesterman CN, Chong BH, Hogg PJ. 2000. Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane. J Biol Chem 275:9758-9766.
10. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275:4827-4833.
11. Chen K, Lin Y, Detwiler TC. 1992. Protein disulfide isomerase activity is released by activated platelets. Blood 79:2226-2228.
12. Chen NQ, Davis AT, Canbulat EC, Liu YX, Goueli S, McKenzie BA, Eccleston ED, Jr., Ahmed K, Holtzman JL. 1996. Evidence that casein kinase 2 phosphorylates hepatic microsomal calcium-binding proteins 1 and 2 but not 3. Biochemistry 35:8299-8306.
13. Clive DR, Greene JJ. 1996. Cooperation of protein disulfide isomerase and redox environment in the regulation of NF-kappaB and AP1 binding to DNA. Cell Biochem Funct 14:49-55.
14. Coppari S, Altieri F, Ferraro A, Chichiarelli S, Eufemi M, Turano C. 2002. Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells. J Cell Biochem 85:325-333.
15. Couet J, de Bernard S, Loosfelt H, Saunier B, Milgrom E, Misrahi M. 1996. Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain. Biochemistry 35:14800-14805.
16. Danon A. 2002. Redox reactions of regulatory proteins: Do kinetics promote specificity? Trends Biochem Sci 27:197-203.
17. Delom F, Mallet B, Carayon P, Lejeune PJ. 2001. Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein. J Biol Chem 276:21337-21342.
18. Demmer J, Zhou C, Hubbard MJ. 1997. Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS Lett 402:145-150.
19. Dingwall C, Laskey RA. 1998. Nuclear import: A tale of two sites. Curr Biol 8:922-924.
20. Donella-Deana A, James P, Staudenmann W, Cesaro L, Marin O, Brunati AM, Ruzzene M, Pinna LA. 1996. Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites. Eur J Biochem 235:18-25.
21. Dorner AJ, Wasley LC, Raney P, Haugejorden S, Green M, Kaufman RJ. 1990. The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion. J Biol Chem 265:22029-22034.
22. Elliott JG, Oliver JD, High S. 1997. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J Biol Chem 272:13849-13855.
23. Essex DW, Li M. 1999a. Protein disulphide isomerase mediates platelet aggregation and secretion. Br J Haematol 104:448-454.
24. Essex DW, Li M. 1999b. A polyclonal antibody to protein disulfide isomerase induces platelet aggregation and secretion. Thromb Res 96:445-450.
25. Essex DW, Chen K, Swiatkowska M. 1995. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 6:2168-2173.
26. Essex DW, Li M, Miller A, Feinman RD. 2001. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 40:6070-6075.
27. Fenouillet E, Barbouche R, Courageot J, Miquelis R. 2001. The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding. J Infect Dis 183:744-752.
28. Ferrari DM, Söling HD. 1999. The protein disulphide-isomerase family: Unravelling a string of folds. Biochem J 339:1-10.
29. Ferrari DM, Nguyen Van P, Kratzin HD, Söling HD. 1998. 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.
30. Ferraro A, Altieri F, Coppari S, Eufemi M, Chichiarelli S, Turano C. 1999. Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA. J Cell Biochem 72:528-539.
31. Frand AR, Kaiser CA. 1999. Erolp oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4:469-477.
32. Freedman RB, Hirst TR, Tuite MF. 1994. Protein disulphide isomerase: Building bridges in protein folding. Trends Biochem Sci 19:331-336.
33. Gerner C, Holzmann K, Meissner M, Gotzmann J, Grimm R, Sauermann G. 1999. Reassembling proteins and chaperones in human nuclear matrix protein fractions. J Cell Biochem 74:145-151.
34. Grillo C, Coppari S, Turano C, Altieri F. 2002. The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a′ domain. Biochem Biophys Res Commun 295:67-73.
35. Hausman RE, Moscona AA. 1975. Purification and characterization of the retina-specific cell-aggregating factor. Proc Natl Acad Sci USA 72:916-920.
36. Hawkins HC, Blackburn EC, Freedman RB. 1991. Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate. Biochem J 275:349-353.
37. Hirano N, Shibasaki F, Sakai R, Tanaka T, Nishida J, Yazaki Y, Takenawa T, Hirai H. 1995. Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Eur J Biochem 234:336-342.
38. Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, Yodoi J. 1997. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 94:3633-3638.
39. Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM. 2001. Calreticulin is a receptor for nuclear export. J Cell Biol 152:127-140.
40. Holmgren A. 1989. Thioredoxin and glutaredoxin systems. J Biol Chem 264:13963-13966.
41. Hotchkiss KA, Matthias LJ, Hogg PJ. 1998. Exposure of the cryptic Arg-Gly-Asp sequence in thrombospondin-1 by protein disulfide isomerase. Biochim Biophys Acta 1388:478-488.
42. Huang EM, Detwiler TC, Milev Y, Essex DW. 1997. Thiol-disulfide isomerization in thrombospondin: Effects of conformation and protein disulfide isomerase. Blood 89:3205-3212.
43. Huber-Wunderlich M, Glockshuber R. 1998. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3:161-171.
44. Janson IM, Ek B, Ek P. 1997. Phosphorylation of CaBP1 and CaBP2 by protein kinase CK2. J Biochem 121:112-117.
45. Jiang XM, Fitzgerald M, Grant CM, Hogg PJ. 1999. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase. J Biol Chem 274:2416-2423.
46. Joelson T, Sjoberg BM, Eklund H. 1990. Modifications of the active center of T4 thioredoxin by site-directed mutagenesis. J Biol Chem 265:3183-3188.
47. Johnson AE, van Waes MA. 1999. The translocon: A dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15:799-842.
48. Johnson E, Henzel W, Deisseroth A. 1992. An isoform of protein disulfide isomerase isolated from chronic myelogenous leukemia cells alters complex formation between nuclear proteins and regulatory regions of interferon-inducible genes. J Biol Chem 267:14412-14417.
49. Johnson S, Michalak M, Opas M, Eggleton P. 2001. The ins and outs of calreticulin: From the ER lumen to the extracellular space. Trends Cell Biol 11:122-129.
50. Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE. 1997. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr Biol 7:239-245.
51. Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ. 1999. The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR 13:357-368.
52. Klappa P, Ruddock LW, Darby NJ, Freedman RB. 1998. 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.
53. Klein M, Gestmann I, Berndorfer U, Schmitz A, Herzog V. 2000. The thioredoxin boxes of thyroglobulin: Possible implications for intermolecular disulfide bond formation in the follicle lumen. Biol Chem 381:593-601.
54. Krishna Rao ASM, Hausman RE. 1993. cDNA for R-cognin: Homology with a multifunctional protein. Proc Natl Acad Sci USA 90:2950-2954.
55. Lahav J, Gofer-Dadosh N, Luboshitz J, Hess O, Shaklai M. 2000. Protein disulfide isomerase mediates integrin-dependent adhesion. FEBS Lett 475:89-92.
56. Landel CC, Kushner PJ, Greene GL. 1995. Estrogen receptor accessory proteins: Effects on receptor-DNA interactions. Environ Health Perspect 103(Suppl 7):23-28.
57. Langenbach KJ, Sottile J. 1999. Identification of protein-disulfide isomerase activity in fibronectin. J Biol Chem 274:7032-7038.
58. Lawrence DA, Song R, Weber P. 1996. Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation. J Leukoc Biol 60:611-618.
59. Lewis MJ, Mazzarella RA, Green M. 1986. Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum. Arch Biochem Biophys 245:389-403.
60. Lindquist JA, Jensen ON, Mann M, Hämmerling GJ. 1998. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J 17:2186-2195.
61. Lundstrom J, Holmgren A. 1990. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J Biol Chem 265:9114-9120.
62. Lundstrom-Ljung J, Birnbach U, Rupp K, Söling HD, Holmgren A. 1995. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase. FEBS Lett 357:305-308.
63. Lyles MM, Gilbert HF. 1991. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer. Biochemistry 30:613-619.
64. Macer DR, Koch GL. 1988. Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J Cell Sci 91:61-70.
65. Mandel R, Ryser HJ, Ghani F, Wu M, Peak D. 1993. Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase. Proc Natl Acad Sci USA 90:4112-4116.
66. Markus M, Benezra R. 1999. Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism. J Biol Chem 274:1040-1049.
67. Mazzarella RA, Marcus N, Haugejorden SM, Balcarek JM, Baldassare JJ, Roy B, Li LJ, Lee AS, Green M. 1994. Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. Arch Biochem Biophys 308:454-460.
68. Megidish T, Takio K, Titani K, Iwabuchi K, Hamaguchi A, Igarashi Y, Hakomori S. 1999. Endogenous substrates of sphingosine-dependent kinases (SDKs) are chaperone proteins: Heat shock proteins, glucose-regulated proteins, protein disulfide isomerase, and calreticulin. Biochemistry 38:3369-3378.
69. Mou Y, Ni H, Wilkins JA. 1998. The selective inhibition of beta 1 and beta 7 integrin-mediated lymphocyte adhesion by bacitracin. J Immunol 161:6323-6329.
70. Murthy MSR, Pande SV. 1994. A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme. Biochem J 304:31-34.
71. Ndubuisi MI, Guo GG, Fried VA, Etlinger JD, Sehgal PB. 1999. Cellular physiology of STAT3: Where is the cytoplasmic monomer? J Biol Chem 274:25499-25509.
72. Nigam SK, Goldberg AL, Ho S, Rohde MF, Bush KT, Sherman MYu. 1994. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. J Biol Chem 269:1744-1749.
73. Noiva R, Freedman RB, Lennarz WJ. 1993. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J Biol Chem 268:19210-19217.
74. O'Neill S, Robinson A, Deering A, Ryan M, Fitzgerald DJ, Moran N. 2000. The platelet integrin αIIβ 3 has an endogenous thiol isomerase activity. J Biol Chem 275:36984-36990.
75. Ohtani H, Wakui H, Ishino T, Komatsuda A, Miura AB. 1993. An isoform of protein disulfide isomerase is expressed in the developing acrosome of spermatids during rat spermiogenesis and is transported into the nucleus of mature spermatids and epididymal spermatozoa. Histochemistry 100:423-429.
76. Oliver JD, Roderick HL, Llewellyn DH, High S. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10:2573-2582.
77. Pariser HP, Zhang J, Hausman RE. 2000. The cell adhesion molecule retina cognin is a cell surface protein disulfide isomerase that uses disulfide exchange activity to modulate cell adhesion. Exp Cell Res 258:42-52.
78. Pihlajaniemi T, Helaakoski T, Tasanen K, Myllyla R, Huhtala MD, Koivu J, Kivirikko KI. 1987. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J 6:643-649.
79. Primm TP, Gilbert HF. 2001. Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum. J Biol Chem 276:281-286.
80. Puig A, Gilbert HF. 1994. Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme. J Biol Chem 269:25889-25896.
81. Quemeneur E, Guthapfel R, Gueguen P. 1994. A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase. J Biol Chem 269:5485-5488.
82. Ramachandran N, Root P, Jiang XM, Hogg PJ, Mutus B. 2001. Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proc Natl Acad Sci USA 98:9539-9544.
83. Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R. 1999. Identification, characterization, and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kDa protein. J Mol Biol 294:515-525.
84. Richarme G. 1998. Protein-disulfide isomerase activity of elongation factor EF-Tu. Biochem Biophys Res Commun 252:156-161.
85. Rigobello MP, Donella-Deana A, Cesaro L, Bindoli A. 2000. Isolation, purification, and characterization of a rat liver mitochondrial protein disulfide isomerase. Free Radic Biol Med 28:266-272.
86. Roderick HL, Campbell AK, Llewllyn DH. 1997. Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors. FEBS Lett 405:181-185.
87. Rogelj S, Reiter KJ, Kesner L, Li M, Essex D. 2000. Enzyme destruction by a protease contaminant in bacitracin. Biochem Biophys Res Commun 273:829-832.
88. Roti Roti JL, Kampinga HH, Malyapa RS, Wright WD, vanderWaal RP, Xu M. 1998. Nuclear matrix as a target for hyperthermic killing of cancer cells. Cell Stress Chaperones 3:245-255.
89. Rozell B, Holmgren A, Hansson HA. 1988. Ultrastructural demonstration of thioredoxin and thioredoxin reductase in rat hepatocytes. Eur J Cell Biol 46:470-477.
90. Ryser HJ, Levy EM, Mandel R, DiSciullo GJ. 1994. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction. Proc Natl Acad Sci USA 91:4559-4563.
91. Sehgal PB, Guo GG, Shah M, Kumar V, Patel K. 2002. Cytokine signaling: STATS in plasma membrane rafts. J Biol Chem 277:12067-12074.
92. Speziale MV, Detwiler TC. 1990. Free thiols of platelet thrombospondin. Evidence for disulfide isomerization. J Biol Chem 265:17859-17867.
93. Stein GS, van Wijnen AJ, Stein J, Lian JB, Montecino M. 1995. Contributions of nuclear architecture to transcriptional control. Int Rev Cytol 162A:251-278.
94. Tager M, Kroning H, Thiel U, Ansorge S. 1997. Membrane-bound proteindisulfide isomerase (PDI) is involved in regulation of surface expression of thiols and drug sensitivity of B-CLL cells. Exp Hematol 25:601-607.
95. Terada K, Manchikalapudi P, Noiva R, Jauregui HO, Stockert RJ, Schilsky ML. 1995. Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes. J Biol Chem 270:20410-20416.
96. Tsibris JC, Hunt LT, Ballejo G, Barker WC, Toney LJ, Spellacy WN. 1989. Selective inhibition of protein disulfide isomerase by estrogens. J Biol Chem 264:13967-13970.
97. Urade R, Nasu M, Moriyama T, Wada K, Kito M. 1992. Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J Biol Chem 267:15152-15159.
98. Urade R, Takenaka Y, Kito M. 1993. Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum. J Biol Chem 268:22004-22009.
99. Urade R, Oda T, Ito H, Moriyama T, Utsumi S, Kito M. 1997. Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. J Biochem 122:834-842.
100. Urade R, Yasunishi A, Okudo H, Moriyama T, Kito M. 1999. Autodegradation of protein disulfide isomerase. Biosci Biotechnol Biochem 63:610-613.
101. Van Nguyen P, Peter F, Söling HD. 1989. Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. J Biol Chem 264:17494-17501.
102. VanderWaal RP, Spitz DR, Griffith CL, Higashikubo R, Roti JL. 2002. Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring. J Cell Biochem 85:689-702.
103. Weisbart RH. 1992. An antibody that binds a neutrophil membrane protein, ERp72, primes human neutrophils for enhanced oxidative metabolism in response to formyl-methionyl-leucyl-phenylalanine. Implications for ERp72 in the signal transduction pathway for neutrophil priming. J Immunol 148:3958-3963.
104. Wetterau JR, Combs KA, Spinner SN, Joiner BJ. 1990. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 265:9801-9807.
105. Wroblewski VJ, Masnyk M, Khambatta SS, Becker GW. 1992. Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver. Diabetes 41:539-547.
106. Wyse B, Ali N, Ellison DH. 2002. Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter. Am J Physiol Renal Physiol 282:F424-F430.
107. Yamauchi K, Yamamoto T, Hayashi H, Koya S, Takikawa H, Toyoshima K, Horiuchi R. 1987. Sequence of membrane-associated thyroid hormone binding protein from bovine liver: Its identity with protein disulphide isomerase. Biochem Biophys Res Commun 146:1485-1492.
108. Yoshimori T, Semba T, Takemoto H, Akagi S, Yamamoto A, Tashiro Y. 1990. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem 265:15984-15990.
109. Zai A, Rudd MA, Scribner AW, Loscalzo J. 1999. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J Clin Invest 103:393-399.
110. Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273:6009-6012.