The critical role of GRP78 in physiologic and pathologic stress

Current Opinion in Cell Biology

Volumn 23, Issue 2, 2011, Pages 150-156

  Pfaffenbach, Kyle T ^a   Lee, Amy S ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN 78; INSULIN; SOMATOMEDIN C;

AGING; CARCINOGENESIS; CELL PROLIFERATION; CELL STRESS; EMBRYO DEVELOPMENT; HUMAN; NEOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; REVIEW; SIGNAL TRANSDUCTION; TUMOR VASCULARIZATION;

AGING; ANIMALS; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; NEOPLASMS; SIGNAL TRANSDUCTION; STRESS, PHYSIOLOGICAL;

EID: 79952842932     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.09.007     Document Type: Review

References (53)

1. Ni M., Lee A.S. ER chaperones in mammalian development and human diseases. FEBS Lett 2007, 581:3641-3651.
2. Rutkowski D.T., Kaufman R.J. A trip to the ER: coping with stress. Trends Cell Biol 2004, 14:20-28.
3. Luo S., Mao C., Lee B., Lee A.S. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 2006, 26:5688-5697.
4. Mao C., Dong D., Little E., Luo S., Lee A.S. Transgenic mouse models for monitoring endoplasmic reticulum stress in vivo. Nat Med 2004, 10:1013-1014.
5. Wu J., Kaufman R.J. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 2006, 13:374-384.
6. Lee A.S. GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res 2007, 67:3496-3499.
7. Wang M., Wey S., Zhang Y., Ye R., Lee A.S. Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders. Antioxid Redox Signal 2009, 11:2307-2316.
8. Henis-Korenblit S., Zhang P., Hansen M., McCormick M., Lee S.J., Cary M., Kenyon C. Insulin/IGF-1 signaling mutants reprogram ER stress response regulators to promote longevity. Proc Natl Acad Sci USA 2010, 107:9730-9735.
9. Paz Gavilan M., Vela J., Castano A., Ramos B., del Rio J.C., Vitorica J., Ruano D. Cellular environment facilitates protein accumulation in aged rat hippocampus. Neurobiol Aging 2006, 27:973-982.
10. Naidoo N., Ferber M., Master M., Zhu Y., Pack A.I. Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling. J Neurosci 2008, 28:6539-6548.
11. Rabek J.P., Boylston W.H., Papaconstantinou J. Carbonylation of ER chaperone proteins in aged mouse liver. Biochem Biophys Res Commun 2003, 305:566-572.
12. Nuss J.E., Choksi K.B., DeFord J.H., Papaconstantinou J. Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers. Biochem Biophys Res Commun 2008, 365:355-361.
13. Erickson R.R., Dunning L.M., Holtzman J.L. The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age. J Gerontol A Biol Sci Med Sci 2006, 61:435-443.
14. Pfaffenbach K.T., Nivala A.M., Reese L., Ellis F., Wang D., Wei Y., Pagliassotti M.J. Rapamycin inhibits postprandial-mediated X-box-binding protein-1 splicing in rat liver. J Nutr 2010, 140:879-884.
15. Yang L., Xue Z., He Y., Sun S., Chen H., Qi L. A Phos-tag-based approach reveals the extent of physiological endoplasmic reticulum stress. PLoS One 2010, 5:e11621.
16. Inageda K. Insulin modulates induction of glucose-regulated protein 78 during endoplasmic reticulum stress via augmentation of ATF4 expression in human neuroblastoma cells. FEBS Lett 2010, 584:3649-3654.
17. Novosyadlyy R., Kurshan N., Lann D., Vijayakumar A., Yakar S., LeRoith D. Insulin-like growth factor-I protects cells from ER stress-induced apoptosis via enhancement of the adaptive capacity of endoplasmic reticulum. Cell Death Differ 2008, 15:1304-1317.
18. Winnay J.N., Boucher J., Mori M.A., Ueki K., Kahn C.R. A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response. Nat Med 2010, 16:438-445.
19. Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nat Med 2010, 16:429-437.
20. Eizirik D.L., Cardozo A.K., Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr Rev 2008, 29:42-61.
21. Flamment M., Kammoun H.L., Hainault I., Ferre P., Foufelle F. Endoplasmic reticulum stress: a new actor in the development of hepatic steatosis. Curr Opin Lipidol 2010, 21:239-246.
22. Ozcan U., Yilmaz E., Ozcan L., Furuhashi M., Vaillancourt E., Smith R.O., Gorgun C.Z., Hotamisligil G.S. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006, 313:1137-1140.
23. Kammoun H.L., Chabanon H., Hainault I., Luquet S., Magnan C., Koike T., Ferre P., Foufelle F. GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice. J Clin Invest 2009, 119:1201-1215. Overexpression of GRP78 in liver of ob/ob mice using an adenoviral vector reduces ER stress and leads to metabolic improvements.
24. Gregor M.F., Yang L., Fabbrini E., Mohammed B.S., Eagon J.C., Hotamisligil G.S., Klein S. Endoplasmic reticulum stress is reduced in tissues of obese subjects after weight loss. Diabetes 2009, 58:693-700.
25. Ye R., Jung D.Y., Jun J.Y., Li J., Luo S., Ko H.J., Kim J.K., Lee A.S. Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance. Diabetes 2010, 59:6-16.
26. Ye R, Mareninova OA, Barron E, Wang M, Hinton DR, Pandol SJ, Lee AS: Grp78 heterozygosity regulates chaperone balance in exocrine pancreas with differential response to cerulein-induced acute pancreatitis. Am J Pathol 2010, in press.
27. Li J., Lee A.S. Stress induction of GRP78/BiP and its role in cancer. Curr Mol Med 2006, 6:45-54.
28. Pootrakul L., Datar R.H., Shi S.R., Cai J., Hawes D., Groshen S.G., Lee A.S., Cote R.J. Expression of stress response protein Grp78 is associated with the development of castration-resistant prostate cancer. Clin Cancer Res 2006, 12:5987-5993.
29. Daneshmand S., Quek M.L., Lin E., Lee C., Cote R.J., Hawes D., Cai J., Groshen S., Lieskovsky G., Skinner D.G., et al. Glucose-regulated protein GRP78 is up-regulated in prostate cancer and correlates with recurrence and survival. Hum Pathol 2007, 38:1547-1552.
30. Zhuang L., Scolyer R.A., Lee C.S., McCarthy S.W., Cooper W.A., Zhang X.D., Thompson J.F., Hersey P. Expression of glucose-regulated stress protein GRP78 is related to progression of melanoma. Histopathology 2009, 54:462-470.
31. Lee E., Nichols P., Spicer D., Groshen S., Yu M.C., Lee A.S. GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res 2006, 66:7849-7853.
32. Lee E., Nichols P., Groshen S., Spicer D., Lee AS GRP78 as potential predictor for breast cancer response to adjuvant taxane therapy. Int J Cancer 2011, 128:726-731.
33. Pyrko P., Schonthal A.H., Hofman F.M., Chen T.C., Lee A.S. The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas. Cancer Res 2007, 67:9809-9816.
34. Martin S., Hill D.S., Paton J.C., Paton A.W., Birch-Machin M.A., Lovat P.E., Redfern CP Targeting GRP78 to enhance melanoma cell death. Pigment Cell Melanoma Res 2010, 23(5):675-682.
35. Virrey J.J., Dong D., Stiles C., Patterson J.B., Pen L., Ni M., Schonthal A.H., Chen T.C., Hofman F.M., Lee A.S. Stress chaperone GRP78/BiP confers chemoresistance to tumor-associated endothelial cells. Mol Cancer Res 2008, 6:1268-1275.
36. Kern J., Untergasser G., Zenzmaier C., Sarg B., Gastl G., Gunsilius E., Steurer M. GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib. Blood 2009, 114:3960-3967.
37. Dong D., Ni M., Li J., Xiong S., Ye W., Virrey J.J., Mao C., Ye R., Wang M., Pen L., et al. Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival and tumor angiogenesis in transgene-induced mammary tumor development. Cancer Res 2008, 68:498-505.
38. Fu Y., Wey S., Wang M., Ye R., Liao C.P., Roy-Burman P., Lee A.S. Pten null prostate tumorigenesis and AKT activation are blocked by targeted knockout of ER chaperone GRP78/BiP in prostate epithelium. Proc Natl Acad Sci USA 2008, 105:19444-19449.
39. Dai R.Y., Chen Y., Fu J., Dong L.W., Ren Y.B., Yang G.Z., Qian Y.W., Cao J., Tang S.H., Yang S.L., et al. p28GANK inhibits endoplasmic reticulum stress-induced cell death via enhancement of the endoplasmic reticulum adaptive capacity. Cell Res 2009, 19:1243-1257.
40. Lin Y., Wang Z., Liu L., Chen L Akt is the downstream target of GRP78 in mediating cisplatin resistance in ER stress-tolerant human lung cancer cells. Lung Cancer 2011, 71:291-297.
41. Lee A.S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 2005, 35:373-381.
42. Arap M.A., Lahdenranta J., Mintz P.J., Hajitou A., Sarkis A.S., Arap W., Pasqualini R. Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands. Cancer Cell 2004, 6:275-284.
43. Zhang Y., Liu R., Ni M., Gill P., Lee A.S. Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP. J Biol Chem 2010, 285:15065-15075.
44. Misra U.K., Deedwania R., Pizzo S.V. Activation and cross-talk between Akt, NF-κB, and unfolded protein response signaling in 1-LN prostate cancer cells consequent to ligation of cell surface-associated GRP78. J Biol Chem 2006, 281:13694-13707.
45. Burikhanov R., Zhao Y., Goswami A., Qiu S., Schwarze S.R., Rangnekar V.M. The tumor suppressor Par-4 activates an extrinsic pathway for apoptosis. Cell 2009, 138:377-388.
46. Shani G., Fischer W.H., Justice N.J., Kelber J.A., Vale W., Gray P.C. GRP78 and Cripto form a complex at the cell surface and collaborate to inhibit transforming growth factor beta signaling and enhance cell growth. Mol Cell Biol 2008, 28:666-677.
47. Misra U.K., Pizzo S.V. Modulation of the unfolded protein response in prostate cancer cells by antibody-directed against the carboxyl-terminal domain of GRP78. Apoptosis 2010, 15:173-182.
48. Kelber J.A., Panopoulos A.D., Shani G., Booker E.C., Belmonte J.C., Vale W.W., Gray P.C. Blockade of Cripto binding to cell surface GRP78 inhibits oncogenic Cripto signaling via MAPK/PI3K and Smad2/3 pathways. Oncogene 2009, 28:2324-2336.
49. Misra U.K., Pizzo S.V. Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells. Cancer Biol Ther 2010, 9:142-152.
50. Liu Y., Steiniger S.C., Kim Y., Kaufmann G.F., Felding-Habermann B., Janda K.D. Mechanistic studies of a peptidic GRP78 ligand for cancer cell-specific drug delivery. Mol Pharm 2007, 4:435-447.
51. Gonzalez-Gronow M., Cuchacovich M., Llanos C., Urzua C., Gawdi G., Pizzo S.V. Prostate cancer cell proliferation in vitro is modulated by antibodies against glucose-regulated protein 78 isolated from patient serum. Cancer Res 2006, 66:11424-11431.
52. Misra U.K., Mowery Y., Kaczowka S., Pizzo S.V. Ligation of cancer cell surface GRP78 with antibodies directed against its COOH-terminal domain up-regulates p53 activity and promotes apoptosis. Mol Cancer Ther 2009, 8:1350-1362.
53. McFarland B.C., Stewart J., Hamza A., Nordal R., Davidson D.J., Henkin J., Gladson C.L. Plasminogen Kringle 5 induces apoptosis of brain microvessel endothelial cells: sensitization by radiation and requirement for GRP78 and LRP1. Cancer Res 2009, 69:5537-5545.