Role of glucose-regulated protein 78 in embryonic development and neurological disorders

Journal of the Formosan Medical Association

Volumn 110, Issue 7, 2011, Pages 428-437

  Weng, Wen Chin ^a,b   Lee, Wang Tso ^a   Hsu, Wen Ming ^a   Chang, Bei En ^a   Lee, Hsinyu ^b  

^a Departments of Medicine   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Embryonic development; Endoplasmic reticulum stress; Glucose regulated protein 78; Neurological disorders; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; BIOLOGICAL MARKER; CALNEXIN; CALRETICULIN; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 34; NERVE GROWTH FACTOR; PROTEIN IRE1; SMALL INTERFERING RNA; TEMOZOLOMIDE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; VALPROIC ACID; X BOX BINDING PROTEIN 1;

5' UNTRANSLATED REGION; ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; APOPTOSIS; AUTOPHAGOSOME; BIPOLAR DISORDER; BLASTOCYST; BRAIN ISCHEMIA; BREAST CANCER; CALCIUM BINDING; CANCER GROWTH; CANCER INVASION; CELL PROLIFERATION; CELL PROTECTION; CELL SURFACE; CEREBELLUM ATROPHY; EMBRYO DEVELOPMENT; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; GLIOBLASTOMA; GOLGI COMPLEX; GROWTH RETARDATION; HUMAN; LIVER CELL CARCINOMA; LUNG CANCER; METASTASIS; MYOCLONUS EPILEPSY; NERVE DEGENERATION; NERVE FIBER GROWTH; NEUROBLASTOMA; NEUROLOGIC DISEASE; NEUROPROTECTION; NONHUMAN; PARKINSON DISEASE; PATHOGENESIS; PROGNOSIS; PROSTATE CANCER; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PSYCHOMOTOR RETARDATION; REVIEW; SCHIZOPHRENIA; SIGNAL TRANSDUCTION; SPINOCEREBELLAR DEGENERATION; STOMACH CARCINOMA; UBIQUITINATION; UNFOLDED PROTEIN RESPONSE; UPREGULATION;

EID: 79960803788     PISSN: None     EISSN: 09296646     Source Type: Journal    
DOI: 10.1016/S0929-6646(11)60064-8     Document Type: Review

References (88)

1. Dorner AJ, Bole DG, Kaufman RJ. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J Cell Biol 1987;105:2665-74.
2. Wiertz EJ, Tortorella D, Bogyo M, et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996;384: 432-8.
3. Rutkowski DT, Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol 2004;14:20-8.
4. Ruddon RW, Bedows E. Assisted protein folding. J Biol Chem 1997;272:3125-8.
5. Wu J, Kaufman RJ. From acute ER stress to physiological roles of the unfolded protein responses. Cell Death Differ 2006;13:374-84.
6. Ni M, Lee AS. ER chaperones in mammalian development and human disease. FEBS Lett 2007;581:3641-51.
7. Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005;4:739-89.
8. Schroder M, Kaufman RJ. Divergent roles of IRE1alpha and PERK in the unfolded protein response. Curr Mol Med 2006;6:5-36.
9. Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 2004;167:27-33.
10. Ye J, Rawson RB, Komuro R, et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 2000;6:1355-64.
11. Yoshida H, Matsui T, Yamamoto A, et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001;107:881-91.
12. Faitova J, Krekac D, Hrstka R, et al. Endoplasmic reticulum stress and apoptosis. Cell Mol Biol Lett 2006;11: 488-505.
13. Yoshida H, Haze K, Yanagi H, et al. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 1998;23:33741-9.
14. Meunier L, Usherwood YK, Chung KT, et al. A subset of chaperones and folding enzymes form multiproteins complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 2002;13:4456-69.
15. Lee AS. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 2005;35:373-81.
16. King LS, Berg M, Chevalier M, et al. Isolation, expression, and characterization of fully functional nontoxic BiP/GRP78 mutants. Protein Expr Purif 2001;22:148-58.
17. Bertolotti A, Zhang Y, Hendershot LM, et al. Dynamic interaction of BiP and ER stress transducers in the unfoldedprotein response. Nature Cell Biol 2000;2:326-32.
18. Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 1999;10:465-72.
19. Cunnea PM, Miranda-Vizuete A, Bertoli G, et al. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 2002;278:1059-66.
20. Shen Y, Hendershot LM. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interaction with unfolded substrates. Mol Biol Cell 2005;16:40-50.
21. Shen Y, Meunier L, Hendershot LM. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J Biol Chem 2002;277: 15947-56.
22. Chung KT, Shen Y, Hendershot LM. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 2002; 277:47557-63.
23. 2+. J Biol Chem 1997;272: 30873-9.
24. Aoki M, Tamatani M, Taniguchi M, et al. Hypothermic treatment restores glucose regulated protein 78 (GRP78) expression in ischemic brain. Brain Res Mol Brain Res 2001;95:117-28.
25. Yu Z, Luo H, Fu W, et al. The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp Neurol 1999; 155:302-14.
26. 2+ disturbances, and cell death in renal epithelial cells. J Biol Chem 1997;272:21751-9.
27. Reddy RK, Mao C, Baumeister P, et al. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J Biol Chem 2003;278:20915-24.
28. Rao RV, Peel A, Logvinova A, et al. Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett 2002;514:122-8.
29. Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007;9:2277-93.
30. Ogata M, Hino S, Saito A, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006;26:9220-31.
31. Yorimitsu T, Klionsky DJ. Endoplasmic reticulum stress: a new pathway to induce autophagy. Autophagy 2007;3: 160-2.
32. Høyer-Hansen M, Jäättelä M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007;14: 1576-82.
33. Li J, Ni M, Lee B, et al. The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells. Cell Death Differ 2008;15:1460-71.
34. Zhang LH, Zhang X. Roles of GRP78 in physiology and cancer. J Cell Biochem 2010;110:1299-305.
35. Gonzalez-Gronow M, Selim MA, Papalas J, et al. GRP78: a multifunctional receptor on the cell surface. Antioxid Redox Signal 2009;11:2299-306.
36. Ting J, Lee AS. Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 1998;7:275-86.
37. Kim SK, Kim YK, Lee AS. Expression of the glucoseregulated proteins (GRP94 and GRP78) in differentiated and undifferentiated mouse embryonic cells and the use of the GRP78 promoter as an expression system in embryonic cells. Differentiation 1990;42:153-9.
38. Barnes JA, Smoak IW. Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress. Anat Embryol (Berl) 2000;202:67-74.
39. Luo S, Mao C, Lee B, et al. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 2006;26:5688-97.
40. Nijhawan D, Honarpour N, Wang X. Apoptosis in neural development and disease Annu Rev Neurosci 2000;23:73-87.
41. Breckenridge DG, Germain M, Mathai JP, et al. Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene 2003;22:8608-18.
42. Zhang X, Szabo E, Michalak M, et al. Endoplasmic reticulum stress during the embryonic development of the central nervous system in the mouse. Int J Dev Neurosci 2007;25: 455-63.
43. Wang M, Ye R, Barron E, et al. Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ 2010;17:488-98.
44. Lin W, Popko B. Endoplasmic reticulum stress in disorders of myelinating cells. Nat Neurosci 2009;12:379-85.
45. Dickhout JG, Krpinsky JC. Endoplasmic reticulum stress and renal disease. Antioxid Redox Signal 2009;11:2341-52.
46. Khan MJ, Pichna BA, Shi Y, et al. Evidence supporting a role for endoplasmic reticulum stress in the development of atherosclerosis in a hyperglycaemic mouse model. Antioxid Redox Signal 2009;11:2289-98.
47. Austin RC. The unfolded protein response in health and disease. Antioxid Redox Signal 2009;11:2279-87.
48. Koumenis C. ER stress, hypoxia tolerance and tumor progression. Curr Mol Med 2006;6:55-69.
49. Lee E, Nichols P, Spicer D, et al. GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res 2006;66:7849-53.
50. Zheng HC, Takahashi H, Li XH, et al. Overexpression of GRP78 and GRP94 are markers for aggressive behavior and poor prognosis in gastric carcinomas. Hum Pathol 2008; 39:1042-9.
51. Su R, Li Z, Li H, et al. Grp78 promotes the invasion of hepatocellular carcinoma. BMC Cancer 2010;10:20.
52. Pyrko P, Schönthal AH, Hofman FM, et al. The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas. Cancer Res 2007;67:9809-16.
53. Virrey JJ, Dong D, Stiles C, et al. Stress chaperone GRP78/BiP confers chemoresistance to tumor-associated endothelial cells. Mol Cancer Res 2008;6:1268-75.
54. Hsu WM, Hsieh FJ, Jeng YM, et al. GRP78 expression correlates with histologic differentiation and favorable prognosis in neuroblastic tumors. Int J Cancer 2005;113:920-7.
55. Maris JM, Matthay KK. Molecular biology of neuroblastoma. J Clin Oncol 1999;17:2264-79.
56. Tonini GP. Neuroblastoma: the result of multistep transformation? Stem Cells 1993;11:276-82.
57. Ijiri R, Tanaka Y, Kato K, et al. Clinicopathologic study of mass-screened neuroblastoma with special emphasis on untreated observed cases: a possible histologic clue to tumor regression. Am J Surg Pathol 2000;24:807-15.
58. Weinreb I, Goldstein D, Irish J, et al. Expression patterns of Trk-A, Trk-B, GRP78, and p75NRT in olfactory neuroblastoma. Hum Pathol 2009;40:1330-5.
59. Satoh T, Furuta K, Tomokiyo K, et al. Facilitatory roles of novel compounds designed from cyclopentenone prostaglandins on neurite outgrowth-promoting activities of nerve growth factor. J Neurochem 2000;75:1092-102.
60. Cho YM, Jang YS, Jang YM, et al. Induction of unfolded protein response during neuronal induction of rat bone marrow stromal cells and mouse embryonic stem cells. Exp Mol Med 2009;41:440-52.
61. Rao RV, Bredesen DE. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol 2004;16:653-62.
62. Paschen W, Mengesdorf T. Endoplasmic reticulum stress response and neurodegeneration. Cell Calcium 2005;38: 409-15.
63. Lin W, Harding HP, Ron D, et al. Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-gamma. J Cell Biol 2005;169:603-12.
64. Lindholm D, Wootz H, Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ 2006;13:385-92.
65. Yoshida H. ER stress and diseases. FEBS J 2007;274: 630-58.
66. Scheper W, Hoozemans JJ. Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy. Curr Med Chem 2009;16: 615-26.
67. Vernia S, Rubio T, Heredia M, et al. Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS One 2009;4:e5907.
68. Lee LC, Chen CM, Chen FL, et al. Altered expression of HSPA5, HSPA8 and PARK7 in spinocerebellar ataxia type 17 identified by 2-dimensional fluorescence difference in gel electrophoresis. Clin Chim Acta 2009;400:56-62.
69. Sasaki S. Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2010;69:346-55.
70. Jayanthi S, McCoy MT, Beauvais G, et al. Methamphetamine induces dopamine D1 receptor-dependent endoplasmic reticulum stress-related molecular events in the rat striatum. PLoS One 2009;4:e6092
71. Naidoo N. Cellular stress/the unfolded protein response: relevance to sleep and sleep disorders. Sleep Med Rev 2009;13:195-204.
72. Nakka VP, Gusain A, Raghubir R. Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats. Neurotox Res 2010;17: 189-202.
73. Zhao L, Longo-Guess C, Harris BS, et al. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat Genet 2005;37:974-9.
74. Anttonen AK, Mahjneh I, Hämäläinen RH, et al. The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone. Nat Genet 2005;37:1309-11.
75. Senderek J, Krieger M, Stendel C, et al. Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy. Nat Genet 2005;37:1312-4.
76. Mimura N, Yuasa S, Soma M, et al. Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP. Mol Cell Biol 2008; 28:293-301.
77. Impagnatiello F, Guidotti AR, Pesold C, et al. A decrease of reelin expression as a putative vulnerability factor in schizophrenia. Proc Natl Acad Sci USA 1998;95: 15718-23.
78. Hoozemans JJ, Veerhuis R, Van Haastert ES, et al. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol 2005;110:165-72.
79. Hoozemans JJ, van Haastert ES, Nijholt DA, et al. The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus. Am J Pathol 2009; 174:1241-51.
80. Naidoo N. ER and aging-protein folding and the ER stress response. Ageing Res Rev 2009;8:150-9.
81. Aoki T, Koike T, Nakano T, et al. Induction of Bip mRNA upon programmed cell death of differentiated PC12 cells as well as rat sympathetic neurons. J Biochem 1997;121:122-7.
82. Martinez JA, Zhang Z, Svetlov SI, et al. Calpain and caspase processing of caspase-12 contribute to the ER stressinduced cell death pathway in differentiated PC12 cells. Apoptosis 2010;15:1480-93.
83. Hayashi T, Saito A, Okuno S, et al. Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death. J Cereb Blood Flow Metab 2003;23:949-61.
84. Aoki M, Tamatani M, Taniguchi M, et al. Hypothermic treatment restores glucose regulated protein 78 (GRP78) expression in ischemic brain. Brain Res Mol Brain Res 2001;95:117-28.
85. Kudo T, Kanemoto S, Hara H, et al. A molecular chaperone inducer protects neurons from ER stress. Cell Death Differ 2008;15:364-75.
86. Lehotský J, Urban P, Pavlíková M, et al. Molecular mechanisms leading to neuroprotection/ischemic tolerance: effect of preconditioning on the stress reaction of endoplasmic reticulum. Cell Mol Neurobiol 2009;29:917-25.
87. Um HS, Kang EB, Leem YH, et al. Exercise training acts as a therapeutic strategy for reduction of the pathogenic phenotypes for Alzheimer's disease in an NSE/APPswtransgenic model. Int J Mol Med 2008;22:529-39.
88. Venkataramani V, Rossner C, Iffland L, et al. Histone deacetylase inhibitor valproic acid inhibits cancer cell proliferation via down-regulation of the alzheimer amyloid precursor protein. J Biol Chem 2010;285:10678-89.