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Volumn 26, Issue 15, 2006, Pages 5688-5697

GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development

Author keywords

[No Author keywords available]

Indexed keywords

CRE RECOMBINASE; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HEAT SHOCK PROTEIN; HYBRID PROTEIN; MESSENGER RNA; PROTEIN; PROTEIN DISULFIDE ISOMERASE; REGULATOR PROTEIN; TRANSCRIPTION FACTOR E2A; TROPHECTODERM; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 33746500168     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00779-06     Document Type: Article
Times cited : (394)

References (47)
  • 1
    • 4544255170 scopus 로고    scopus 로고
    • Cell surface expression of the stress response ehaperonc GRP78 enables tumor targeting by circulating ligands
    • Arap, M. A., J. Lahdenranta, P. J. Mintz, A. Hajitou, A. S. Sarkis, W. Arap, and R. Pasqualini. 2004. Cell surface expression of the stress response ehaperonc GRP78 enables tumor targeting by circulating ligands. Cancer Cell 6:275-284.
    • (2004) Cancer Cell , vol.6 , pp. 275-284
    • Arap, M.A.1    Lahdenranta, J.2    Mintz, P.J.3    Hajitou, A.4    Sarkis, A.S.5    Arap, W.6    Pasqualini, R.7
  • 2
    • 0002777920 scopus 로고    scopus 로고
    • Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress
    • Barnes, J. A., and I. W. Smoak. 2000. Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress. Anat. Embryol. 202:67-74.
    • (2000) Anat. Embryol. , vol.202 , pp. 67-74
    • Barnes, J.A.1    Smoak, I.W.2
  • 3
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Y. Zhang, L. M. Hendershot, H. P. Harding, and D. Ron. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:326-332.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 5
    • 0030998545 scopus 로고    scopus 로고
    • Apoptosis during mouse blastocyst formation: Evidence for a role for survival factors including transforming growth factor alpha
    • Brison, D. R., and R. M. Schultz. 1997. Apoptosis during mouse blastocyst formation: evidence for a role for survival factors including transforming growth factor alpha. Biol. Reprod. 56:1088-1096.
    • (1997) Biol. Reprod. , vol.56 , pp. 1088-1096
    • Brison, D.R.1    Schultz, R.M.2
  • 8
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner, A. J., L. C. Wasley, and R. J. Kaufman. 1992. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11:1563-1571.
    • (1992) EMBO J. , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 9
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality eontrol in the secretory pathway
    • Ellgaard, L., M. Molinari, and A. Helenius. 1999. Setting the standards: quality eontrol in the secretory pathway. Science 286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 10
    • 0037073712 scopus 로고    scopus 로고
    • Activation of an unfolded protein response during differentiation of antibody-secreting B cells
    • Gass, J. N., N. M. Gifford, and J. W. Brewer. 2002. Activation of an unfolded protein response during differentiation of antibody-secreting B cells. J. Biol. Chem. 277:49047-49054.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49047-49054
    • Gass, J.N.1    Gifford, N.M.2    Brewer, J.W.3
  • 11
    • 0033014498 scopus 로고    scopus 로고
    • De-regulation of GRP stress protein expression in human breast cancer cell lines
    • Gazit, G., J. Lu, and A. S. Lee. 1999. De-regulation of GRP stress protein expression in human breast cancer cell lines. Breast Cancer Res. Treat. 54:135-146.
    • (1999) Breast Cancer Res. Treat. , vol.54 , pp. 135-146
    • Gazit, G.1    Lu, J.2    Lee, A.S.3
  • 12
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot, L. M. 2004. The ER function BiP is a master regulator of ER function. Mt. Sinai J. Med. 71:289-297.
    • (2004) Mt. Sinai J. Med. , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 13
    • 0028965528 scopus 로고
    • In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum
    • Hendershot, L. M., J. Y. Wei, J. R. Gaut, B. Lawson, P. J. Frelden, and K. G. Murti. 1995. In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell 6:283-296.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 283-296
    • Hendershot, L.M.1    Wei, J.Y.2    Gaut, J.R.3    Lawson, B.4    Frelden, P.J.5    Murti, K.G.6
  • 14
    • 3042588257 scopus 로고    scopus 로고
    • Differential expression of glucose-regulated protein 78 during spermatogenesis
    • Huo, R., Y. F. Zhu, X. Ma, M. Lin, Z. M. Zhou, and J. H. Sha. 2004. Differential expression of glucose-regulated protein 78 during spermatogenesis. Cell Tissue Res. 316:359-367.
    • (2004) Cell Tissue Res. , vol.316 , pp. 359-367
    • Huo, R.1    Zhu, Y.F.2    Ma, X.3    Lin, M.4    Zhou, Z.M.5    Sha, J.H.6
  • 15
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly, C., and R. I. Morimoto. 2000. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 92:1564-1572.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 16
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman, R. J. 2002. Orchestrating the unfolded protein response in health and disease. J. Clin. Investig. 110:1389-1398.
    • (2002) J. Clin. Investig. , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 17
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 18
    • 23844469871 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone 1 analog acts as an antiapoptotic factor in mouse blastocysts
    • Kawamura, K., J. Fukuda, J. Kumagai, Y. Shimizu, H. Kodama, A. Nakamura, and T. Tanaka. 2005. Gonadotropin-releasing hormone 1 analog acts as an antiapoptotic factor in mouse blastocysts. Endocrinology 146:4105-4116.
    • (2005) Endocrinology , vol.146 , pp. 4105-4116
    • Kawamura, K.1    Fukuda, J.2    Kumagai, J.3    Shimizu, Y.4    Kodama, H.5    Nakamura, A.6    Tanaka, T.7
  • 19
    • 18844396119 scopus 로고    scopus 로고
    • Embryonic stem cell differentiation: Emergence of a new era in biology and medicine
    • Keller, G. 2005. Embryonic stem cell differentiation: emergence of a new era in biology and medicine. Genes Dev. 19:1129-1155.
    • (2005) Genes Dev. , vol.19 , pp. 1129-1155
    • Keller, G.1
  • 20
    • 0025348378 scopus 로고
    • Expression of the glucose-regulated 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
    • Kim, S. K., Y. K. Kim, and A. S. Lee. 1990. Expression of the glucose-regulated 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 42:153-159.
    • (1990) Differentiation , vol.42 , pp. 153-159
    • Kim, S.K.1    Kim, Y.K.2    Lee, A.S.3
  • 21
    • 0034971343 scopus 로고    scopus 로고
    • Isolation, expression, and characterization of fully functional nontoxic BiP/GRP78 mutants
    • King, L. S., M. Berg, M. Chevalier, A. Carey, E. C. Elguindi, and S. Y. Blond. 2001. Isolation, expression, and characterization of fully functional nontoxic BiP/GRP78 mutants. Protein Expr. Purif. 22:148-158.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 148-158
    • King, L.S.1    Berg, M.2    Chevalier, M.3    Carey, A.4    Elguindi, E.C.5    Blond, S.Y.6
  • 22
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B., and I. Braakman. 2004. Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16:343-349.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 24
    • 0033644144 scopus 로고    scopus 로고
    • Conditional gene knockout using ere recombinase
    • Le, Y., and B. Sauer. 2000. Conditional gene knockout using ere recombinase. Methods Mol. Biol. 136:477-485.
    • (2000) Methods Mol. Biol. , vol.136 , pp. 477-485
    • Le, Y.1    Sauer, B.2
  • 25
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee, A. S. 2005. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35:373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 26
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S. 2001. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26:504-510.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 27
    • 0026843954 scopus 로고
    • Mammalian stress response: Induction of the glucose-regulated protein family
    • Lee, A. S. 1992. Mammalian stress response: induction of the glucose-regulated protein family. Curr. Opin. Cell Biol. 4:267-273.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 267-273
    • Lee, A.S.1
  • 28
    • 33646171070 scopus 로고    scopus 로고
    • Stress induction of GRP78/BiP and its role in cancer
    • Li, J., and A. S. Lee. 2006. Stress induction of GRP78/BiP and its role in cancer. Curr. Mol. Med. 6:45-54.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 45-54
    • Li, J.1    Lee, A.S.2
  • 29
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li, J., B. Lee, and A. S. Lee. 2006. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J. Biol. Chem. 281:7260-7270.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 30
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: Thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • Li, M., P. Baumeister, B. Roy, T. Phan, D. Foti, S. Luo, and A. S. Lee. 2000. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20:5096-5106.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 31
    • 0037106329 scopus 로고    scopus 로고
    • Requirement of the p38 MAPK signaling pathway for the induction of Grp78/BiP by azetidine stress: ATF6 as a target for stress-induced phosphorylation
    • Luo, S., and A. S. Lee. 2002. Requirement of the p38 MAPK signaling pathway for the induction of Grp78/BiP by azetidine stress: ATF6 as a target for stress-induced phosphorylation. Biochem. J. 366:787-795.
    • (2002) Biochem. J. , vol.366 , pp. 787-795
    • Luo, S.1    Lee, A.S.2
  • 32
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma, Y., and L. M. Hendershot. 2004. ER chaperone functions during normal and stress conditions. J. Chem. Neuroanat. 28:51-65.
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 33
    • 7044220129 scopus 로고    scopus 로고
    • Transgenic mouse models for monitoring endoplasmic reticulum stress in vivo
    • Mao, C., D. Dong, E. Little, S. Luo, and A. S. Lee. 2004. Transgenic mouse models for monitoring endoplasmic reticulum stress in vivo. Nat. Med. 10:1013-1014.
    • (2004) Nat. Med. , vol.10 , pp. 1013-1014
    • Mao, C.1    Dong, D.2    Little, E.3    Luo, S.4    Lee, A.S.5
  • 34
    • 33646828938 scopus 로고    scopus 로고
    • In vivo regulation of Grp78/BiP transcription in the embryonic heart: Role of the endoplasmic reticulum stress response element and GATA-4
    • Mao, C., W. C. Tai, Y. Bai, C. Poizat, and A. S. Lee. 2006. In vivo regulation of Grp78/BiP transcription in the embryonic heart: role of the endoplasmic reticulum stress response element and GATA-4. J. Biol. Chem. 281:8877-8887.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8877-8887
    • Mao, C.1    Tai, W.C.2    Bai, Y.3    Poizat, C.4    Lee, A.S.5
  • 35
    • 0034660877 scopus 로고    scopus 로고
    • Histone H3 and heat shock protein GRP78 are selectively cross-linked to DNA by photoactivated gilvocarcin V in human fibroblasts
    • Matsumoto, A., and P. C. Hanawalt. 2000. Histone H3 and heat shock protein GRP78 are selectively cross-linked to DNA by photoactivated gilvocarcin V in human fibroblasts. Cancer Res. 60:3921-3026.
    • (2000) Cancer Res. , vol.60 , pp. 3921-13026
    • Matsumoto, A.1    Hanawalt, P.C.2
  • 36
    • 23444437501 scopus 로고    scopus 로고
    • Ligation of cell surface-associated glucose-regulated protein 78 by receptor-recognized forms of alpha2-macroglobulin: Activation of p21-activated protein kinase-2-dependent signaling in murine peritoneal macrophages
    • Misra, U. K., T. Sharma, and S. V. Pizzo. 2005. Ligation of cell surface-associated glucose-regulated protein 78 by receptor-recognized forms of alpha2-macroglobulin: activation of p21-activated protein kinase-2-dependent signaling in murine peritoneal macrophages. J. Immunol. 175:2525-2533.
    • (2005) J. Immunol. , vol.175 , pp. 2525-2533
    • Misra, U.K.1    Sharma, T.2    Pizzo, S.V.3
  • 37
    • 0031054643 scopus 로고    scopus 로고
    • Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins
    • Morris, J. A., A. J. Dorner, C. A. Edwards, L. M. Hendershot, and R. J. Kaufman. 1997. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J. Biol. Chem. 272:4327-4134.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4327-14134
    • Morris, J.A.1    Dorner, A.J.2    Edwards, C.A.3    Hendershot, L.M.4    Kaufman, R.J.5
  • 39
    • 0034923117 scopus 로고    scopus 로고
    • A novel murine tryptase involved in blastocyst hatching and outgrowth
    • O'Sullivan, C. M., S. L. Rancourt, S. Y. Liu, and D. E. Rancourt. 2001. A novel murine tryptase involved in blastocyst hatching and outgrowth. Reproduction 122:61-71.
    • (2001) Reproduction , vol.122 , pp. 61-71
    • O'Sullivan, C.M.1    Rancourt, S.L.2    Liu, S.Y.3    Rancourt, D.E.4
  • 41
    • 0037115528 scopus 로고    scopus 로고
    • Cancer-inducible transgene expression by the Grp94 promoter: Spontaneous activation in tumors of various origins and cancer-associated macrophages
    • Reddy, R. K., L. Dubeau, H. Kleiner, T. Parr, P. Nichols, B. Ko, D. Dong, H. Ko, C. Mao, J. DiGiovanni, and A. S. Lee. 2002. Cancer-inducible transgene expression by the Grp94 promoter: spontaneous activation in tumors of various origins and cancer-associated macrophages. Cancer Res. 62:7207-7212.
    • (2002) Cancer Res. , vol.62 , pp. 7207-7212
    • Reddy, R.K.1    Dubeau, L.2    Kleiner, H.3    Parr, T.4    Nichols, P.5    Ko, B.6    Dong, D.7    Ko, H.8    Mao, C.9    DiGiovanni, J.10    Lee, A.S.11
  • 42
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation
    • Reddy, R. K., C. Mao, P. Baumeister, R. C. Austin, R. J. Kaufman, and A. S. Lee. 2003. 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. 278:20915-20924.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 43
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., X. Chen, L. Hendershot, and R. Prywes. 2002. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3:99-111.
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 44
    • 0034103657 scopus 로고    scopus 로고
    • Conditional inactivation of Fgf4 reveals complexity of signalling during limb bud development
    • Sun, X., M. Lewandoski, E. N. Meyers, Y. H. Liu, R. E. Maxson, Jr., and G. R. Martin. 2000. Conditional inactivation of Fgf4 reveals complexity of signalling during limb bud development. Nat. Genet. 25:83-86.
    • (2000) Nat. Genet. , vol.25 , pp. 83-86
    • Sun, X.1    Lewandoski, M.2    Meyers, E.N.3    Liu, Y.H.4    Maxson Jr., R.E.5    Martin, G.R.6
  • 45
    • 0023890443 scopus 로고
    • Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: Structure, conservation, and regulation
    • Ting, J., and A. S. Lee. 1988. Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7:275-286.
    • (1988) DNA , vol.7 , pp. 275-286
    • Ting, J.1    Lee, A.S.2
  • 46
    • 0035018190 scopus 로고    scopus 로고
    • Direct removal in the mouse of a floxed neo gene from a three-loxP conditional knockout allele by two novel approaches
    • Xu, X., C. Li, L. Garrett-Beal, D. Larson, A. Wynshaw-Boris, and C. X. Deng. 2001. Direct removal in the mouse of a floxed neo gene from a three-loxP conditional knockout allele by two novel approaches. Genesis 30:1-6.
    • (2001) Genesis , vol.30 , pp. 1-6
    • Xu, X.1    Li, C.2    Garrett-Beal, L.3    Larson, D.4    Wynshaw-Boris, A.5    Deng, C.X.6
  • 47
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L., C. Longo-Guess, B. S. Harris, J. W. Lee, and S. L. Ackerman. 2005. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37:974-979.
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5


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