GRP78: A multifunctional receptor on the cell surface

Antioxidants and Redox Signaling

Volumn 11, Issue 9, 2009, Pages 2299-2306

  Gonzalez Gronow, Mario ^a   Selim, Maria Angelica ^a   Papalas, John ^a   Pizzo, Salvatore V ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 MACROGLOBULIN; AUTOANTIBODY; AUTOANTIGEN; CALCIUM; DNA; GLUCOSE REGULATED PROTEIN 78; GROWTH FACTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PLASMA PROTEIN; PLASMINOGEN KRINGLE 5; PROTEIN DNAJ; TERATOCARCINOMA DERIVED GROWTH FACTOR 1; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR; VOLTAGE DEPENDENT ANION CHANNEL;

AUTOIMMUNITY; CALCIUM CELL LEVEL; CELL MEMBRANE; CELL PROLIFERATION; CELL STRESS; CELL SURFACE; COXSACKIE VIRUS B; CYTOSOL; DENGUE VIRUS; DNA SYNTHESIS; HUMAN; HYDROPHOBICITY; IMMUNOHISTOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; REVIEW; SIGNAL TRANSDUCTION;

AUTOANTIBODIES; HEAT-SHOCK PROTEINS; HUMANS; RECEPTORS, CELL SURFACE; SIGNAL TRANSDUCTION;

DENGUE VIRUS;

EID: 68949209302     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2009.2568     Document Type: Review

References (68)

1. Bhattacharjee G, Ahamed J, Pedersen B, El-Sheikh A, Mackman N, Ruf W, Liu C, and Edgington TS. Regulation of tissue factor-mediated initiation of the coagulation cascade by cell surface grp78. Arterioscler Thromb Vasc Biol 25: 1737-1743, 2005.
2. Bodman-Smith MD, Corrigal VM, Berglin E, Cornell HR, Tzioufas AG, Mavragani CP, Chan C, Rantapää-Dahlqvist S, and Panayi G. Antibody response to the human stress protein BiP in rheumatoid arthritis. Rheumatology 43: 1283-1287, 2004.
3. Boon T, Old LJ. Cancer tumor antigens. Curr Opin Immunol 9: 681-683, 1997.
4. Chang CC, Campoli M, and Ferrone S. HLA class I antigen expression in malignant cells: Why does it not always correlate with CTL-mediated lysis? Curr Opin Immunol 16: 644-650, 2004.
5. Chen LY, Chiang AS, Hung JJ, Hung HI, and Lai YK. Thapsigargin-induced GRP78 expression is mediated by the increase of cytosolic free calcium in 9L rat brain tumor cells. J Cell Biochem 78: 404-416, 2000.
6. Chen X and Wolin SL. The Ro60 kDa autoantigen: Insights into cellular function and role in autoimmunity. J Mol Med 82: 232-239, 2004.
7. Chevalier M, Rhee H, Elguindi EC, and Blond S. Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1. J Biol Chem 275: 19620-19627, 2000.
8. Chignard N, Shang S, Wang H, Marrero J, Brechot C, Hanash S, and Beretta L. Cleavage of endoplasmic reticulum proteins in hepatocellular carcinoma: Detection of generated fragments in patient sera. Gastroenterology 130: 2010-2022, 2006.
9. Chinni SR, Falchetto R, Gercel-Taylor C, Chabanowitz J, Hunt DF, and Taylor DD. Humoral immune responses to cathepsin D and glucose-regulated protein 78 in ovarian cancer patients. Clin Cancer Res 3: 1557-1564, 1997.
10. Cianfrocca M and Goldstein LJ. Prognostic and predictive factors in early stage breast cancer. Oncologist 9: 606-616, 2004.
11. Davidson DJ, Haskell C, Majest S, Kherzai A, Egan DA, Walter KA, Schneider A, Gubbins EF, Solomon L, Chen Z, Lesniewski R, and Henkin J. Kringle 5 of human plasminogen induces apoptosis of endothelial and tumor cells through surface-expressed glucose-regulated protein 78. Cancer Res 65: 4663-4672, 2005.
12. Delpino A and Castelli M. The 78 kDa glucose-regulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation. Biosci Rep 22: 407-420, 2002.
13. Gonzalez-Gronow M, Cuchacovich M, Llanos C, Urzua C, Gawdi G, and Pizzo SV. Prostate cancer cell proliferation in vitro is modulated by antibodies against glucose-regulated protein 78 isolated from patient serum. Cancer Res 66, 11424-11431, 2006.
14. Gonzalez-Gronow M, Kaczowka SJ, Payne S, Wang F, Gawdi G, and Pizzo SV. Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel. J Biol Chem 282: 32811-32820, 2007.
15. Hakomori S. Tumor-associated carbohydrate antigens defining tumor malignancy: basis for development of anticancer vaccines. Adv Exp Med Biol 491: 369-402, 2001.
16. Hardy B, Raiter A, Weiss C, Kaplan B, Tenebaum A, and Battler A. Angiogenesis induced by novel peptides selected from a phage display library by screening human vacuolar endothelial cells under different physiological conditions. Peptides 3: 691-701, 2000.
17. Hardy B, Battler A, Weiss C, Kudasi O, and Raiter A. Therapeutic angiogenesis of mouse hind limb ischemia by novel peptide activating GRP78 receptor on endothelial cells. Biochem Pharmacol 75: 891-899, 2008.
18. Henderson LM. The ER chaperone BiP is a master regulator of ER function. Mt Sinai J Med 71: 289-297, 2004.
19. Jakobsen CG, Rasmussen N, Laenkholm AV, Ditzel HJ. Phage display-derived human monoclonal antibodies isolated by binding to the surface of the live primary breast cancer cells recognize GRP78. Cancer Res 67:9507-9517, 2007.
20. Jindadamrongwech S, Thepparit C, and Smith DR. Identifications of GRP78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch Virol 149: 915-927, 2004.
21. Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev 13: 1211-1233, 1999.
22. Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 110: 1389-1398, 2002.
23. Kiang JG and Tsokos GC. Heat shock protein 70kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 80: 183-201, 1998.
24. Kim Y, Lillo AM, Steiniger SC, Liu Y, Ballatore C, Anichini A, Mortarini R, Kaufmann GF, Zhou B, Felding-Habermann B, and Janda KD. Targeting heat shock proteins on cancer cells: Selection, characterization, and cell-penetrating properties of a peptidic GRP78 ligand. Biochemistry 45: 9434-9444, 2006.
25. Kinoshita G, Purcell AW, Keech CL, Farris AD, McCluskey J, and Gordon TP. Molecular chaperones are targets of autoimmunity in Ro(SS-A) immune mice. Clin Exp Immunol 115: 268-274, 1999.
26. Lee AS. Mammalian stress response: Induction of the glucose-regulated protein family. Curr Opin Cell Biol 4: 267-273, 1992.
27. Lee AS. The glucose-regulated proteins: Stress induction and clinical applications. Trends Biochem Sci 26: 504-510, 2001.
28. Lee AS. GRP78 induction in cancer: T andprognostic implications. Cancer Res 67: 3496-3499, 2007.
29. Liu Y, Steiniger SC, Kim Y, Kaufmann GF, Felding-Habermann B, and Janda KD. Mechanistic studies of a peptide GRP78 ligand for cancer cell-specific drug delivery. Mol Pharm 4: 435-447, 2007.
30. Ma Y and Henderson LM. The role of the unfolded protein response in tumor development: Friend or foe? Nat Rev Cancer 4: 966-977, 2004.
31. Marincola FM, Jafee EM, Hicklin DJ, and Ferrone S. Escape of human solid tumors from T-cell recognition: Molecular mechanisms and functional significance. Adv Immunol 74: 181-273, 2000.
32. Markoff LJ, Innis BL, Houghten R, and Henchal LS. Development of cross-reactive antibodies to plasminogen during the immune response to dengue virus infection. J Infect Dis 164: 294-307, 1991.
33. Mintz PJ, Kim J, Do KA, Wang X, Zinner RG, Cristofanilli M, Arap MA, Hong WK, Troncoso P, Logothetis CJ, Pasqualini R, and Arap W. Fingerprinting the circulating repertoire of antibodies from cancer patients. Nat Biotechnol 21: 57-63, 2003.
34. Misra UK, Chu CT, Gawdi G, and Pizzo SV. Evidence for a second a2-macroglobulin receptor. J Biol Chem 269: 12541-12547, 1994.
35. Misra UK, Gonzalez-Gronow M, Gawdi G, Hart JP, Johnson CE, and Pizzo SV. The role of GRP78 in alpha-2-macroglobulin induced signal transduction. Evidence from RNA interference that the low density lipoprotein receptor-related protein is associated with but not necessary for GRP78-mediatedsignal transduction. J Biol Chem 277: 42082-42087, 2002.
36. Misra UK, Gonzalez-Gronow M, Gawdi G, Wang F, and Pizzo SV. A novel receptor function for the heat shock protein GRP78: Silencing of GRP78 gene expression attenuates alpha-2M*-induced signaling. Cell Signal 16: 929-938, 2004.
37. Misra UK and Pizzo SV. Potentiation of signal transduction mitogenesis and cellular proliferation upon binding of receptor-recognized forms of a2-macroglobulin to 1-LN prostate cancer cells. Cell 16: 487-496, 2004.
38. Misra UK, Gonzalez-Gronow M, Gawdi G, and Pizzo SV. The role of MTJ-1 in cell surface translocation of GRP78, a receptor for a2-macroglobulin-dependent signaling. J Immunol 174; 2092-2097, 2005.
39. Misra UK, Deedwania R, and Pizzo SV. Activation and crosstalk between Akt, NF-kappB, and unfolded protein response signaling in 1-LN prostate cancer cells consequent to ligation of cell-surface GPR78. J Biol Chem 281: 13694-13707, 2006.
40. Misra UK and Pizzo SV. Heterotrimeric Galpha11 co-immunoprecipitates with surface-anchored GRP78 from plasma membranes of alpha-2M*-stimulated macrophages. J Cell Biochem 104: 96-104, 2008.
41. Miyake H, Hara I, Arakawa S, and Kamidono S. Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J Cell Biochem 77: 396-408, 2000.
42. Munro S and Pelham HRB. An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46: 291-300, 1986.
43. Paulsson KM, Wang P, Anderson PO, Chen S, Petterson RF, and Li S. Distinct differences in association of MHC Class I with endoplasmic reticulum proteins in wild-type, and beta-2-microglobulin- and TAP-deficient reticulum proteins in wild-type, and beta-2-microglobulin- and TAP-deficient cell lines. Int Immunol 13: 1063-1073, 2001.
44. 2M*. FASEB J 19: A253, 2005.
45. Purcell AW, Todd A, Kinoshita G, Lynch TA, Keech CL, Gething MJ, and Gordon TP. Association of stress proteins with autoantigens: A possible mechanism for triggering autoimmunity. Clin Exp Immunol 132: 193-200, 2003.
46. Rauschert N, Brändlein S, Holzinger E, Hensel F, Muller-Hermelink HK, and Vollmers HP. A new tumor-specific variant of GRP78 as target for antibody-based therapy. Lab Invest 88: 375-386, 2008.
47. Reddy R, Mao C, Baumeister P, Austin R, Kaufman RJ, and Lee AS. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors. J Biol Chem 278: 20915-20924, 2003.
48. Rosenberg SA. Progress in human tumor immunology and immunotherapy. Nature 411: 380-384, 2001.
49. Rutkowski DT, Kang SW, Goodman AG, Garrison JL, Taunton J, Katze MG, Kaufman RJ, and Hedge RS. The role of p58IPK in protecting the stressed endoplasmic reticulum. Mol Biol Cell 18: 3681-3691, 2007.
50. Sasaya H, Utsumi T, Shimoke K, Nakayama H, Matsumura Y, Fukunaga K, and Ikeuchi T. Nicotine suppresses tunicamycin-induced, but not thapsigargin-induced expression of GRP78 during ER stress-mediated apoptosis in PC12 cells. J Biochem 144: 251-257, 2008.
51. Scanlan MJ, Gure AO, Jungbluth AA, Old J, and Chen YT. Cancer/testis antigens: an expanding family of targets for cancer immunotherapy. Immunol Rev 188: 22-32, 2002.
52. Seliger B, Maeurer MJ, and Ferrone S. Antigen-processing machinery breakdown and tumor growth. Immunol Today 21: 455-464, 2000.
53. Seliger B, Atkins D, Bock M, Ritz U, Ferrone S, Huber C, and Storkel S. Characterization of human lymphocyte antigen class I antigen-processing machinery defects in renal cell carcinoma lesions with special emphasis on transporter-associated with antigen-processing down-regulation. Clin Cancer Res 9: 1721-1727, 2003.
54. Shani G, Fischer WH, Justice NJ, Kelber JA, Vale W and Gray PC. GRP78 and Cripto form a complex at the cell surface and collaborate to inhibit transforming growth factor β signaling and enhance cell growth. Mol Cell Biol 28: 666-677, 2008.
55. Shen X, Zhangh K, and Kaufman RJ. The unfolded protein response: stress signaling pathway of the endoplasmic reticulum. J Chem Neuoroanat 28: 79-92, 2004.
56. Tamura Y, Peng P, Liu K, Daou M, and Srivastava PK. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 278; 117-120, 1997.
57. Thastrup O, Dawson AP, Scharff O, Foder B, Cullen PJ, Drobak BK, Bjerrum RJ, Christensen SB, and Hanley MR. Thapsigargin, a novel molecular probe for studying intracellular calcium release and storage. Agents Actions 43: 187-193, 1994.
58. 2+-ATPases. Trends Pharmacol Sci 19: 131-135, 1998.
59. Triantafilou M, Fradelizi D, and Triantafilou K. Major histocompatibility class one molecule associates with glucose related protein (GRP)78 on the cell surface. Hum Immunol 62: 764-770, 2001.
60. Triantafilou K, Fradelizi D, Wilson K, and Triantafilou K. GRP78, a co-receptor for Coxsackie virus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization. J Virol 76: 633-643, 2002.
61. Watson LM, Chan AK, Berry LR, Li J, Sood SK, Dickhout JG, Werstuck GH, Gajzar L, Klamut HJ, and Austin RC. Overexpression of the 78-kDa glucose-regulated protein/immunoglobulin-binding protein (GRP78/BiP) inhibits tissue factor procoagulant activity. J Biol Chem 278: 17438-17447, 2003.
62. Xiao G, Chung TF, Pyun HY, Fine RE, and Johnson RJ. KDEL proteins are found on the surface of NG108-15 cells. Brain Res Mol Brain Res 72: 121-128, 1999.
63. Xie P, Browning DD, Hay N, Mackman N, and Ye RD. Activation of NF-kappa B by bradykinin through a Galpha(q)- and Gbeta gamma-dependent pathway that involves phosphoinositide 3-kianse and Akt. J Biol Chem 275: 24907-24914, 2000.
64. 2+ storage. Eur J Cell Biol 81: 469-483, 2002.
65. Young JD, Tsuchiya D, Sandlin DE, and Holroyde MJ. Enzymatic O-glycosylation of synthetic peptides from sequences in basic protein myelin protein. Biochemistry 18: 4444-4448, 1979.
66. Yoshida H, Haze K, Yanagi H, Yura T, and Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for the transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273: 33741-33749, 1998.
67. 2+ store itself may be a major factor in thapsigargin-induced ER stress and apoptosis in PC12 cells. Neurochem Int 48: 696-702, 2006.
68. Zhang K, and Kaufman RJ. The unfolded protein response: A stress signaling pathway critical for health and disease. Neurology 66: S102-S109, 2006.