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Volumn 16, Issue 4, 2011, Pages 539-563

ERp57/GRP58: A protein with multiple functions

Author keywords

Calcitriol; Cellular stress; DNA repair; Protein disulfide isomerases; Signal transduction; STAT3

Indexed keywords

CALCITRIOL; CALPAIN; GLUCOSE REGULATED PROTEIN 58; HEAT SHOCK PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; PROTEIN DISULFIDE ISOMERASE; STAT3 PROTEIN; UNCLASSIFIED DRUG; CHAPERONE; DNA; HLA ANTIGEN CLASS 1; PDIA3 PROTEIN, HUMAN; PDIA3 PROTEIN, MOUSE;

EID: 84855728063     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-011-0022-z     Document Type: Review
Times cited : (107)

References (90)
  • 1
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano, C., Coppari, S., Altieri, F. and Ferraro, A. Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell. Physiol. 193 (2002) 154-163.
    • (2002) J. Cell. Physiol. , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 2
    • 34247555889 scopus 로고    scopus 로고
    • The ERp57/GRp58/1,25D3-MARRS receptor: Multiple functional roles in diverse cell systems
    • Khanal, R. C. and Nemere, I. The ERp57/GRp58/1, 25D3-MARRS receptor: multiple functional roles in diverse cell systems. Curr. Med. Chem. 14 (2007) 1087-1093.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1087-1093
    • Khanal, R.C.1    Nemere, I.2
  • 3
    • 77953809347 scopus 로고    scopus 로고
    • ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe, H. and Michalak, M. ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase. Int. J. Biochem. Cell Biol. 42 (2010) 796-799.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 4
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositidespecific phospholipase C
    • Bennett, C. F., Balcarek, J. M., Varrichio, A. and Crooke, S. T. Molecular cloning and complete amino-acid sequence of form-I phosphoinositidespecific phospholipase C. Nature334 (1988) 268-270.
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.T.4
  • 5
    • 0019833479 scopus 로고
    • The accumulation of three specific proteins related to glucoseregulated proteins in a temperature-sensitive hamster mutant cell line K12
    • Lee, A. S. The accumulation of three specific proteins related to glucoseregulated proteins in a temperature-sensitive hamster mutant cell line K12. J. Cell. Physiol. 106 (1981) 119-125.
    • (1981) J. Cell. Physiol. , vol.106 , pp. 119-125
    • Lee, A.S.1
  • 6
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari, D. M., Söling, H. D. The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339 (1999) 1-10.
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Söling, H.D.2
  • 7
    • 1842690851 scopus 로고    scopus 로고
    • Identification and characterization of structural domains of human ERp57: Association with calreticulin requires several domains
    • Silvennoinen, L., Myllyharju, J., Ruoppolo, M., Orrù, S., Caterino, M., Kivirikko, K. I. and Koivunen, P. Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains. J. Biol. Chem. 279 (2004) 13607-13615.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13607-13615
    • Silvennoinen, L.1    Myllyharju, J.2    Ruoppolo, M.3    Orrù, S.4    Caterino, M.5    Kivirikko, K.I.6    Koivunen, P.7
  • 10
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa, P., Ruddock, L. W., Darby, N. J. and Freedman, R. B. 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 (1998) 927-935.
    • (1998) EMBO J. , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 12
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick, T. P., Bangia, N., Peaper, D. R. and Cresswell, P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity16 (2002) 87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 14
    • 0030046449 scopus 로고    scopus 로고
    • 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
    • Donella-Deana, A., James, P., Staudenmann, W., Cesaro, L., Marin, O., Brunati, A. M., Ruzzene, M. and Pinna, L. A. 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 (1996) 18-25.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 18-25
    • Donella-Deana, A.1    James, P.2    Staudenmann, W.3    Cesaro, L.4    Marin, O.5    Brunati, A.M.6    Ruzzene, M.7    Pinna, L.A.8
  • 15
    • 29344442591 scopus 로고    scopus 로고
    • Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin
    • Kita, K., Okumura, N., Takao, T., Watanabe, M., Matsubara, T., Nishimura, O. and Nagai, K. Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin. FEBS Lett. 580 (2006) 199-205.
    • (2006) FEBS Lett. , vol.580 , pp. 199-205
    • Kita, K.1    Okumura, N.2    Takao, T.3    Watanabe, M.4    Matsubara, T.5    Nishimura, O.6    Nagai, K.7
  • 16
    • 0029658060 scopus 로고    scopus 로고
    • The covalent binding of [14C]acetaminophen to mouse hepatic microsomal proteins: The specific binding to calreticulin and the two forms of the thiol:Protein disulfide oxidoreductases
    • Zhou, L., McKenzie, B. A., Eccleston, E. D. Jr, Srivastava, S. P., Chen, N., Erickson, R. R. and Holtzman, J. L. The covalent binding of [14C]acetaminophen to mouse hepatic microsomal proteins: the specific binding to calreticulin and the two forms of the thiol: protein disulfide oxidoreductases. Chem. Res. Toxicol. 9 (1996) 1176-1182.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 1176-1182
    • Zhou, L.1    McKenzie, B.A.2    Eccleston Jr., E.D.3    Srivastava, S.P.4    Chen, N.5    Erickson, R.R.6    Holtzman, J.L.7
  • 17
    • 0026338345 scopus 로고
    • A metabolite of halothane covalently binds to an endoplasmic reticulum protein that is highly homologous to phosphatidylinositol-specific phospholipase C-alpha but has no activity
    • Martin, J. L., Pumford, N. R., LaRosa, A. C., Martin, B. M., Gonzaga, H. M., Beaven, M. A. and Pohl, L. R. A metabolite of halothane covalently binds to an endoplasmic reticulum protein that is highly homologous to phosphatidylinositol-specific phospholipase C-alpha but has no activity. Biochem. Biophys. Res. Commun. 178 (1991) 679-685.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 679-685
    • Martin, J.L.1    Pumford, N.R.2    Larosa, A.C.3    Martin, B.M.4    Gonzaga, H.M.5    Beaven, M.A.6    Pohl, L.R.7
  • 19
    • 0037106461 scopus 로고    scopus 로고
    • Endoplasmic reticulum resident proteins of normal human dermal fibroblasts are the major targets for oxidative stress induced by hydrogen peroxide
    • van der Vlies, D., Pap, E. H., Post, J. A., Celis, J. E. and Wirtz, K. W. Endoplasmic reticulum resident proteins of normal human dermal fibroblasts are the major targets for oxidative stress induced by hydrogen peroxide. Biochem. J. 366 (2002) 825-830.
    • (2002) Biochem. J. , vol.366 , pp. 825-830
    • van der Vlies, D.1    Pap, E.H.2    Post, J.A.3    Celis, J.E.4    Wirtz, K.W.5
  • 21
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman, R. B., Hirst, T. R. and Tuite, M. F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19 (1994) 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 23
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum
    • Urade, R., Nasu, M., Moriyama, T., Wada, K. and Kito, M. Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J. Biol. Chem. 267 (1992) 15152-15159.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15152-15159
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 24
    • 0028114733 scopus 로고
    • A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme
    • Murthy, M. S. and Pande, S. V. A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme. Biochem. J. 304 (1994) 31-34.
    • (1994) Biochem. J. , vol.304 , pp. 31-34
    • Murthy, M.S.1    Pande, S.V.2
  • 25
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J. and High, S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science275 (1997) 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 26
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari, M. and Helenius, A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature402 (1999) 90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 27
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver, J. D., Roderick, H. L., Llewellyn, D. H. and High, S. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10 (1999) 2573-2582.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 28
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop, C. E., Chakravarthi, S., Garbi, N., Hämmerling, G. J., Lovell, S. and Bulleid, N. J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 26 (2007) 28-40.
    • (2007) EMBO J. , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hämmerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 29
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist, J. A., Jensen, O. N., Mann, M. and Hämmerling, G. J. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17 (1998) 2186-2195.
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hämmerling, G.J.4
  • 30
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick, T. P., Bangia, N., Peaper, D. R. and Cresswell, P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity16 (2002) 87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 31
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thioloxidoreductase heterodimer
    • Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P. and Reinisch, K. M. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thioloxidoreductase heterodimer. Immunity30 (2009) 21-32.
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 32
    • 65649095933 scopus 로고    scopus 로고
    • ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
    • Zhang, Y., Kozlov, G., Pocanschi, C. L., Brockmeier, U., Ireland, B. S., Maattanen, P., Howe, C., Elliott, T., Gehring, K. and Williams, D. B. ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity. J. Biol. Chem. 284 (2009) 10160-10173.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10160-10173
    • Zhang, Y.1    Kozlov, G.2    Pocanschi, C.L.3    Brockmeier, U.4    Ireland, B.S.5    Maattanen, P.6    Howe, C.7    Elliott, T.8    Gehring, K.9    Williams, D.B.10
  • 33
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper, D. R. and Cresswell, P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc. Natl. Acad. Sci. USA105 (2008) 10477-10482.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 34
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi, N., Tanaka, S., Momburg, F., and Hammerling, G. J. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat. Immunol. 7 (2006) 93-102.
    • (2006) Nat. Immunol. , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 35
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+-dependent redox modulation of SERCA 2b by ERpERp57
    • Li, Y. and Camacho, P. Ca2+-dependent redox modulation of SERCA 2b by ERpERp57. J. Cell Biol. 164 (2004) 35-46.
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 36
  • 37
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins, M. ER-mediated phagocytosis: a new membrane for new functions. Nat. Rev. Immunol. 3 (2003) 280-291.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 280-291
    • Desjardins, M.1
  • 39
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucoseregulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano, N., Shibasaki, F., Sakai, R., Tanaka, T., Nishida, J., Yazaki, Y., Takenawa, T. and Hirai, H. Molecular cloning of the human glucoseregulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur. J. Biochem. 234 (1995) 336-342.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1    Shibasaki, F.2    Sakai, R.3    Tanaka, T.4    Nishida, J.5    Yazaki, Y.6    Takenawa, T.7    Hirai, H.8
  • 40
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson, S., Michalak, M., Opas, M. and Eggleton, P. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol. 11 (2001) 122-129.
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 41
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • Afshar, N., Black, B. E. and Paschal, B. M. Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell. Biol. 25 (2005) 8844-8853.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 42
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57
    • Ellerman, D. A., Myles, D. G. And Primakoff P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev. Cell. 10 (2006) 831-837.
    • (2006) Dev. Cell. , vol.10 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 43
    • 2442624604 scopus 로고    scopus 로고
    • Ribozyme knockdown functionally links a 1,25(OH)2D3 membrane binding protein (1,25D3-MARRS) and phosphate uptake in intestinal cells
    • Nemere, I., Farach-Carson, M. C., Rohe, B., Sterling, T. M., Norman, A. W., Boyan, B. D. and Safford, S. E. Ribozyme knockdown functionally links a 1, 25(OH)2D3 membrane binding protein (1, 25D3-MARRS) and phosphate uptake in intestinal cells. Proc. Natl. Acad. Sci. USA101 (2004) 7392-7397.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7392-7397
    • Nemere, I.1    Farach-Carson, M.C.2    Rohe, B.3    Sterling, T.M.4    Norman, A.W.5    Boyan, B.D.6    Safford, S.E.7
  • 44
    • 33947142458 scopus 로고    scopus 로고
    • 1alpha,25(OH)2D3 is an autocrine regulator of extracellular matrix turnover and growth factor release via ERp60 activated matrix vesicle metalloproteinases
    • Boyan, B. D., Wong, K. L., Fang, M. and Schwartz, Z. 1alpha, 25(OH)2D3 is an autocrine regulator of extracellular matrix turnover and growth factor release via ERp60 activated matrix vesicle metalloproteinases. J. Steroid. Biochem. Mol. Biol. 103 (2007) 467-472.
    • (2007) J. Steroid. Biochem. Mol. Biol. , vol.103 , pp. 467-472
    • Boyan, B.D.1    Wong, K.L.2    Fang, M.3    Schwartz, Z.4
  • 45
    • 78449264901 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-associated 3 (Pdia3) mediates the membrane response to 1,25-dihydroxyvitamin D3 in osteoblasts
    • Chen, J., Olivares-Navarrete, R., Wang, Y., Herman, T. R., Boyan, B. D. and Schwartz, Z. Protein-disulfide isomerase-associated 3 (Pdia3) mediates the membrane response to 1, 25-dihydroxyvitamin D3 in osteoblasts. J. Biol. Chem. 285 (2010) 37041-37050.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37041-37050
    • Chen, J.1    Olivares-Navarrete, R.2    Wang, Y.3    Herman, T.R.4    Boyan, B.D.5    Schwartz, Z.6
  • 46
    • 77949269051 scopus 로고    scopus 로고
    • Protein kinase C isotypes in signal transduction for the 1,25D3-MARRS receptor (ERp57/PDIA3) in steroid hormone-stimulated phosphate uptake
    • Tunsophon, S. and Nemere, I. Protein kinase C isotypes in signal transduction for the 1, 25D3-MARRS receptor (ERp57/PDIA3) in steroid hormone-stimulated phosphate uptake. Steroids75 (2010) 307-313.
    • (2010) Steroids , vol.75 , pp. 307-313
    • Tunsophon, S.1    Nemere, I.2
  • 47
    • 77957785488 scopus 로고    scopus 로고
    • Intestinal cell calcium uptake and the targeted knockout of the 1,25D3-MARRS (membrane-associated, rapid response steroid-binding) receptor/PDIA3/Erp57
    • Nemere, I., Garbi, N., Hämmerling, G. J. and Khanal, R. C. Intestinal cell calcium uptake and the targeted knockout of the 1, 25D3-MARRS (membrane-associated, rapid response steroid-binding) receptor/PDIA3/Erp57. J. Biol. Chem. 285 (2010) 31859-31866.
    • (2010) J. Biol. Chem. , vol.285 , pp. 31859-31866
    • Nemere, I.1    Garbi, N.2    Hämmerling, G.J.3    Khanal, R.C.4
  • 48
    • 76749153775 scopus 로고    scopus 로고
    • Involvement of 1,25D3-MARRS (membrane associated, rapid response steroid-binding), a novel vitamin D receptor, in growth inhibition of breast cancer cells
    • Richard, C. L., Farach-Carson, M. C., Rohe, B., Nemere, I. and Meckling, K. A. Involvement of 1, 25D3-MARRS (membrane associated, rapid response steroid-binding), a novel vitamin D receptor, in growth inhibition of breast cancer cells. Exp. Cell Res. 316 (2010) 695-703.
    • (2010) Exp. Cell Res. , vol.316 , pp. 695-703
    • Richard, C.L.1    Farach-Carson, M.C.2    Rohe, B.3    Nemere, I.4    Meckling, K.A.5
  • 49
    • 77950629508 scopus 로고    scopus 로고
    • Nuclear translocation of the 1,25D3-MARRS (membrane associated rapid response to steroids) receptor protein and NFkappaB in differentiating NB4 leukemia cells
    • Wu, W., Beilhartz, G., Roy, Y., Richard, C. L., Curtin, M., Brown, L., Cadieux, D., Coppolino, M., Farach-Carson, M. C., Nemere, I. and Meckling, K. A. Nuclear translocation of the 1, 25D3-MARRS (membrane associated rapid response to steroids) receptor protein and NFkappaB in differentiating NB4 leukemia cells. Exp. Cell Res. 316 (2010) 1101-1108.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1101-1108
    • Wu, W.1    Beilhartz, G.2    Roy, Y.3    Richard, C.L.4    Curtin, M.5    Brown, L.6    Cadieux, D.7    Coppolino, M.8    Farach-Carson, M.C.9    Nemere, I.10    Meckling, K.A.11
  • 50
    • 0027104218 scopus 로고
    • Association of solubilized angiotensin II receptors with phospholipase C-alpha in murine neuroblastoma NIE-115 cells
    • Mah, S. J., Ades, A. M., Mir, R., Siemens, I. R., Williamson, J. R. and Fluharty, S. J. Association of solubilized angiotensin II receptors with phospholipase C-alpha in murine neuroblastoma NIE-115 cells. Mol. Pharmacol. 42 (1992) 217-226.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 217-226
    • Mah, S.J.1    Ades, A.M.2    Mir, R.3    Siemens, I.R.4    Williamson, J.R.5    Fluharty, S.J.6
  • 51
    • 0024317196 scopus 로고
    • Solubilization of rat liver vasopressin receptors as a complex with a guanine-nucleotide-binding protein and phosphoinositidespecific phospholipase C
    • Aiyar, N., Bennett, C. F., Nambi, P., Valinski, W., Angioli, M., Minnich, M. and Crooke, S. T. Solubilization of rat liver vasopressin receptors as a complex with a guanine-nucleotide-binding protein and phosphoinositidespecific phospholipase C. Biochem. J. 261 (1989) 63-70.
    • (1989) Biochem. J. , vol.261 , pp. 63-70
    • Aiyar, N.1    Bennett, C.F.2    Nambi, P.3    Valinski, W.4    Angioli, M.5    Minnich, M.6    Crooke, S.T.7
  • 52
    • 0027178944 scopus 로고
    • Purification of a 57kDa nuclear matrix protein associated with thiol:Protein-disulfide oxidoreductase and phospholipase C activities
    • Altieri, F., Maras, B., Eufemi, M., Ferraro, A. and Turano, C. Purification of a 57kDa nuclear matrix protein associated with thiol: protein-disulfide oxidoreductase and phospholipase C activities. Biochem. Biophys. Res. Commun. 194 (1993) 992-1000.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 992-1000
    • Altieri, F.1    Maras, B.2    Eufemi, M.3    Ferraro, A.4    Turano, C.5
  • 53
    • 0027281905 scopus 로고
    • The reported cDNA sequence for phospholipase C alpha encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C
    • Srivastava, S. P., Fuchs, J. A. and Holtzman, J. L. The reported cDNA sequence for phospholipase C alpha encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C. Biochem. Biophys. Res. Commun. 193 (1993) 971-978.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 971-978
    • Srivastava, S.P.1    Fuchs, J.A.2    Holtzman, J.L.3
  • 54
    • 36048968942 scopus 로고    scopus 로고
    • Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis
    • Tokutomi, Y., Araki, N., Kataoka, K., Yamamoto, E. and Kim-Mitsuyama, S. Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis. Biochem. Biophys. Res. Commun. 364 (2007) 822-830.
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 822-830
    • Tokutomi, Y.1    Araki, N.2    Kataoka, K.3    Yamamoto, E.4    Kim-Mitsuyama, S.5
  • 55
    • 77949815874 scopus 로고    scopus 로고
    • Disulfide isomerase glucose-regulated protein 58 is required for the nuclear localization and degradation of retinoic acid receptor alpha
    • Zhu, L., Santos, N. C. and Kim, K. H. Disulfide isomerase glucose-regulated protein 58 is required for the nuclear localization and degradation of retinoic acid receptor alpha. Reproduction139 (2010) 717-731.
    • (2010) Reproduction , vol.139 , pp. 717-731
    • Zhu, L.1    Santos, N.C.2    Kim, K.H.3
  • 57
    • 0037023701 scopus 로고    scopus 로고
    • Cytokine signaling: STATS in plasma membrane rafts
    • Sehgal, P. B., Guo, G. G., Shah, M., Kumar, V. and Patel, K. Cytokine signaling: STATS in plasma membrane rafts. J. Biol. Chem. 277 (2002) 12067-12074.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12067-12074
    • Sehgal, P.B.1    Guo, G.G.2    Shah, M.3    Kumar, V.4    Patel, K.5
  • 58
    • 0036016555 scopus 로고    scopus 로고
    • Association of the chaperone glucose-regulated protein 58 (GRP58/ER-60/ERp57) with Stat3 in cytosol and plasma membrane complexes
    • Guo, G. G., Patel, K., Kumar, V., Shah, M., Fried, V. A., Etlinger, J. D. and Sehgal, P. B. Association of the chaperone glucose-regulated protein 58 (GRP58/ER-60/ERp57) with Stat3 in cytosol and plasma membrane complexes. J. Interferon Cytokine Res. 22 (2002) 555-563.
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 555-563
    • Guo, G.G.1    Patel, K.2    Kumar, V.3    Shah, M.4    Fried, V.A.5    Etlinger, J.D.6    Sehgal, P.B.7
  • 61
    • 0036087077 scopus 로고    scopus 로고
    • Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter
    • Wyse, B., Ali, N. and Ellison, D. H. Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter. Am. J. Physiol. Renal Physiol. 282 (2002) F424-430.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.282
    • Wyse, B.1    Ali, N.2    Ellison, D.H.3
  • 63
    • 53149137847 scopus 로고    scopus 로고
    • ERP57 membrane translocation dictates the immunogenicity of tumor cell death by controlling the membrane translocation of calreticulin
    • Obeid, M. ERP57 membrane translocation dictates the immunogenicity of tumor cell death by controlling the membrane translocation of calreticulin. J. Immunol. 181 (2008) 2533-2543.
    • (2008) J. Immunol. , vol.181 , pp. 2533-2543
    • Obeid, M.1
  • 65
    • 28244469041 scopus 로고    scopus 로고
    • Redox regulation of the nutrientsensitive raptor-mTOR pathway and complex
    • Sarbassov, D. D. and Sabatini, D. M. Redox regulation of the nutrientsensitive raptor-mTOR pathway and complex. J. Biol. Chem. 280 (2005) 39505-39509.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39505-39509
    • Sarbassov, D.D.1    Sabatini, D.M.2
  • 66
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L. and Elazar, Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 26 (2007) 1749-1760.
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 67
    • 0027750972 scopus 로고
    • 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
    • Ohtani, H., Wakui, H., Ishino, T., Komatsuda, A. and Miura, A. B. 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. Histochemistry100 (1993) 423-429.
    • (1993) Histochemistry , vol.100 , pp. 423-429
    • Ohtani, H.1    Wakui, H.2    Ishino, T.3    Komatsuda, A.4    Miura, A.B.5
  • 68
    • 0036221159 scopus 로고    scopus 로고
    • Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells
    • Coppari, S., Altieri, F., Ferraro, A., Chichiarelli, S., Eufemi, M. and Turano, C. Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells. J. Cell. Biochem. 85 (2002) 325-333.
    • (2002) J. Cell. Biochem. , vol.85 , pp. 325-333
    • Coppari, S.1    Altieri, F.2    Ferraro, A.3    Chichiarelli, S.4    Eufemi, M.5    Turano, C.6
  • 69
    • 0037228781 scopus 로고    scopus 로고
    • A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues
    • Krynetski, E. Y., Krynetskaia, N. F., Bianchi, M. E. and Evans, W. E. A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues. Cancer Res. 63 (2003) 100-106.
    • (2003) Cancer Res. , vol.63 , pp. 100-106
    • Krynetski, E.Y.1    Krynetskaia, N.F.2    Bianchi, M.E.3    Evans, W.E.4
  • 70
    • 66449132564 scopus 로고    scopus 로고
    • Chromatin-associated proteins HMGB1/2 and PDIA3 trigger cellular response to chemotherapy-induced DNA damage
    • Krynetskaia, N. F., Phadke, M. S., Jadhav, S. H. and Krynetskiy, E. Y. Chromatin-associated proteins HMGB1/2 and PDIA3 trigger cellular response to chemotherapy-induced DNA damage. Mol. Cancer Ther. 8 (2009) 864-872.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 864-872
    • Krynetskaia, N.F.1    Phadke, M.S.2    Jadhav, S.H.3    Krynetskiy, E.Y.4
  • 71
    • 65349153918 scopus 로고    scopus 로고
    • Comparative proteomic analysis of paclitaxel sensitive A2780 epithelial ovarian cancer cell line and its resistant counterpart A2780TC1 by 2D-DIGE: The role of ERp57
    • Cicchillitti, L., Di Michele, M., Urbani, A., Ferlini, C., Donat, M. B., Scambia, G. and Rotilio, D. Comparative proteomic analysis of paclitaxel sensitive A2780 epithelial ovarian cancer cell line and its resistant counterpart A2780TC1 by 2D-DIGE: the role of ERp57. J. Proteome Res. 8 (2009) 1902-1912.
    • (2009) J. Proteome Res. , vol.8 , pp. 1902-1912
    • Cicchillitti, L.1    Di Michele, M.2    Urbani, A.3    Ferlini, C.4    Donat, M.B.5    Scambia, G.6    Rotilio, D.7
  • 72
    • 77954157573 scopus 로고    scopus 로고
    • Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of beta-actin
    • Cicchillitti, L., Della Corte, A., Di Michele, M., Donati, M. B., Rotilio, D. and Scambia, G. Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: the involvement of specific conformational states of beta-actin. Int. J. Oncol. 37 (2010) 445-454.
    • (2010) Int. J. Oncol. , vol.37 , pp. 445-454
    • Cicchillitti, L.1    della Corte, A.2    Di Michele, M.3    Donati, M.B.4    Rotilio, D.5    Scambia, G.6
  • 73
    • 0033559687 scopus 로고    scopus 로고
    • Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA
    • Ferraro, A., Altieri, F., Coppari, S., Eufemi, M., Chichiarelli, S. and Turano, C. Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA. J. Cell. Biochem. 72 (1999) 528-539.
    • (1999) J. Cell. Biochem. , vol.72 , pp. 528-539
    • Ferraro, A.1    Altieri, F.2    Coppari, S.3    Eufemi, M.4    Chichiarelli, S.5    Turano, C.6
  • 74
    • 0036301509 scopus 로고    scopus 로고
    • The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a(′) domain
    • Grillo, C., Coppari, S., Turano, C. and Altieri, F. The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a(′) domain. Biochem. Biophys. Res. Commun. 295 (2002) 67-73.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 67-73
    • Grillo, C.1    Coppari, S.2    Turano, C.3    Altieri, F.4
  • 76
    • 33747838884 scopus 로고    scopus 로고
    • Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function
    • Schultz-Norton, J. R., McDonald, W. H., Yates, J. R. and Nardulli, A. M. Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function. Mol. Endocrinol. 20 (2006) 1982-1995.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1982-1995
    • Schultz-Norton, J.R.1    McDonald, W.H.2    Yates, J.R.3    Nardulli, A.M.4
  • 77
    • 77949879489 scopus 로고    scopus 로고
    • ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum
    • Coe, H., Jung, J., Groenendyk, J., Prins, D. and Michalak, M. ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J. Biol. Chem. 285 (2010) 6725-6738.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6725-6738
    • Coe, H.1    Jung, J.2    Groenendyk, J.3    Prins, D.4    Michalak, M.5
  • 78
    • 2442459084 scopus 로고    scopus 로고
    • Plasma membrane rafts and chaperones in cytokine/STAT signaling
    • Sehgal, P. B. Plasma membrane rafts and chaperones in cytokine/STAT signaling. Acta Biochim. Pol. 50 (2003) 583-594.
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 583-594
    • Sehgal, P.B.1
  • 79
    • 0033534719 scopus 로고    scopus 로고
    • Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism
    • Markus, M. and Benezra, R. Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism. J. Biol. Chem. 274 (1999) 1040-1049.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1040-1049
    • Markus, M.1    Benezra, R.2
  • 80
    • 50849127125 scopus 로고    scopus 로고
    • ERp57-associated mitochondrial micro-calpain truncates apoptosis-inducing factor
    • Ozaki, T., Yamashita, T. and Ishiguro, S. ERp57-associated mitochondrial micro-calpain truncates apoptosis-inducing factor. Biochim. Biophys. Acta1783 (2008) 1955-1963.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1955-1963
    • Ozaki, T.1    Yamashita, T.2    Ishiguro, S.3
  • 82
    • 33847066363 scopus 로고    scopus 로고
    • Regulation of expression of 1,25D3-MARRS/ERp57/PDIA3 in rat IEC-6 cells by TGF beta and 1,25(OH)2D3
    • Rohe, B., Safford, S. E., Nemere, I., Farach-Carson, M. C. Regulation of expression of 1, 25D3-MARRS/ERp57/PDIA3 in rat IEC-6 cells by TGF beta and 1, 25(OH)2D3. Steroids72 (2007) 144-150.
    • (2007) Steroids , vol.72 , pp. 144-150
    • Rohe, B.1    Safford, S.E.2    Nemere, I.3    Farach-Carson, M.C.4
  • 83
    • 34247195447 scopus 로고    scopus 로고
    • Targeting homeostatic mechanisms of endoplasmic reticulum stress to increase susceptibility of cancer cells to fenretinide-induced apoptosis: The role of stress proteins ERdj5 and ERp57
    • Corazzari, M., Lovat, P. E., Armstrong, J. L., Fimia, G. M., Hill, D. S., Birch-Machin, M., Redfern, C. P. and Piacentini, M. Targeting homeostatic mechanisms of endoplasmic reticulum stress to increase susceptibility of cancer cells to fenretinide-induced apoptosis: the role of stress proteins ERdj5 and ERp57. Br. J. Cancer96 (2007) 1062-1071.
    • (2007) Br. J. Cancer , vol.96 , pp. 1062-1071
    • Corazzari, M.1    Lovat, P.E.2    Armstrong, J.L.3    Fimia, G.M.4    Hill, D.S.5    Birch-Machin, M.6    Redfern, C.P.7    Piacentini, M.8
  • 87
    • 67650071063 scopus 로고    scopus 로고
    • Knockdown of ERp57 increases BiP/GRP78 induction and protects against hyperoxia and tunicamycin-induced apoptosis
    • Xu, D., Perez, R. E., Rezaiekhaligh, M. H., Bourdi, M. and Truog, W. E. Knockdown of ERp57 increases BiP/GRP78 induction and protects against hyperoxia and tunicamycin-induced apoptosis. Am. J. Physiol. Lung Cell. Mol. Physiol. 297 (2009) L44-51.
    • (2009) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.297
    • Xu, D.1    Perez, R.E.2    Rezaiekhaligh, M.H.3    Bourdi, M.4    Truog, W.E.5
  • 88
    • 45249097366 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine
    • Dukes, A. A., van Laar, V. S., Cascio, M. and Hastings, T. G. Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine. J. Neurochem. 106 (2008) 333-346.
    • (2008) J. Neurochem. , vol.106 , pp. 333-346
    • Dukes, A.A.1    van Laar, V.S.2    Cascio, M.3    Hastings, T.G.4
  • 89
    • 35848965047 scopus 로고    scopus 로고
    • Cell stress induced by the parkinsonian mimetic, 6-hydroxydopamine, is concurrent with oxidation of the chaperone, ERp57, and aggresome formation
    • Kim-Han, J. S. and O'Malley, K. L. Cell stress induced by the parkinsonian mimetic, 6-hydroxydopamine, is concurrent with oxidation of the chaperone, ERp57, and aggresome formation. Antioxid. Redox Signal. 9 (2007) 2255-2264.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2255-2264
    • Kim-Han, J.S.1    O'Malley, K.L.2
  • 90
    • 77949369883 scopus 로고    scopus 로고
    • Proteomic characterization of the striatum and midbrain treated with 6-hydroxydopamine: Alteration of 58-kDa glucose-regulated protein and C/EBP homologous protein
    • Akazawa, Y. O., Saito, Y., Nishio, K., Horie, M., Kinumi, T., Masuo, Y., Yoshida, Y., Ashida, H. and Niki, E. Proteomic characterization of the striatum and midbrain treated with 6-hydroxydopamine: alteration of 58-kDa glucose-regulated protein and C/EBP homologous protein. Free Radic. Res. 44 (2010) 410-421.
    • (2010) Free Radic. Res. , vol.44 , pp. 410-421
    • Akazawa, Y.O.1    Saito, Y.2    Nishio, K.3    Horie, M.4    Kinumi, T.5    Masuo, Y.6    Yoshida, Y.7    Ashida, H.8    Niki, E.9


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