메뉴 건너뛰기




Volumn 239, Issue 1, 1998, Pages 23-30

Interaction of heat stress glycoprotein GP50 with classical heat-shock proteins

Author keywords

[No Author keywords available]

Indexed keywords

3,3' DITHIOBIS(SUCCINIMIDYL PROPIONATE); CELL PROTEIN; GELATIN; GLYCOPROTEIN; GLYCOSYLATED PROTEIN; HEAT SHOCK PROTEIN; MANNOSE;

EID: 0031846286     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1997.3881     Document Type: Article
Times cited : (7)

References (37)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P., and Hartl, F. U. (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 3
    • 0001935815 scopus 로고
    • Thermotolerance in cultured mammalian cells
    • (K. J. Henle, Ed.), CRC Press, Boca Raton, FL
    • Henle, K. J. (1987). Thermotolerance in cultured mammalian cells. In "Thermotolerance" (K. J. Henle, Ed.), Vol. I, pp. 13-71, CRC Press, Boca Raton, FL.
    • (1987) Thermotolerance , vol.1 , pp. 13-71
    • Henle, K.J.1
  • 4
    • 0026561859 scopus 로고
    • Relationship of heat shock proteins and induced thermal resistance
    • Weber, L. A. (1992). Relationship of heat shock proteins and induced thermal resistance. Cell. Prolifer. 25,101-113.
    • (1992) Cell. Prolifer. , vol.25 , pp. 101-113
    • Weber, L.A.1
  • 5
    • 0023943561 scopus 로고
    • Enhanced glycosylation of a 50 kD protein during thermotolerance development in CHO cells
    • Henle, K. J., Norris, J. S., Nagle, W. A., and Moss, A. J. (1988). Enhanced glycosylation of a 50 kD protein during thermotolerance development in CHO cells. Int. J. Radiat. Biol. 53, 839-847.
    • (1988) Int. J. Radiat. Biol. , vol.53 , pp. 839-847
    • Henle, K.J.1    Norris, J.S.2    Nagle, W.A.3    Moss, A.J.4
  • 6
    • 0023730891 scopus 로고
    • Effect of hyperthermia on the activity of three glycosyltransferases in CHO cells
    • Henle, K. J., Stone, A., and Chatterjee, S. K. (1988). Effect of hyperthermia on the activity of three glycosyltransferases in CHO cells. Cancer Res. 48, 5717-5721.
    • (1988) Cancer Res. , vol.48 , pp. 5717-5721
    • Henle, K.J.1    Stone, A.2    Chatterjee, S.K.3
  • 7
    • 0026040203 scopus 로고
    • Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating
    • Henle, K. J., and Nagle, W. A. (1991). Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating. Exp. Cell Res. 196, 184-191.
    • (1991) Exp. Cell Res. , vol.196 , pp. 184-191
    • Henle, K.J.1    Nagle, W.A.2
  • 8
    • 0027273046 scopus 로고
    • Prompt protein glycosylation during acute heat stress
    • Henle, K. J., Kaushal, G. P., Nagle, W. A., and Nolen, G. T. (1993). Prompt protein glycosylation during acute heat stress. Exp. Cell Res. 207, 245-251.
    • (1993) Exp. Cell Res. , vol.207 , pp. 245-251
    • Henle, K.J.1    Kaushal, G.P.2    Nagle, W.A.3    Nolen, G.T.4
  • 9
    • 0028339062 scopus 로고
    • Heat shock glycoprotein GP50: Product of the retinoic acid-inducible J6 gene
    • Henle, K. J., Wang, S. Y., Nagle, W. A., and Lumpkin, C. K. (1994). Heat shock glycoprotein GP50: Product of the retinoic acid-inducible J6 gene. Exp. Cell Res. 210, 185-191.
    • (1994) Exp. Cell Res. , vol.210 , pp. 185-191
    • Henle, K.J.1    Wang, S.Y.2    Nagle, W.A.3    Lumpkin, C.K.4
  • 11
    • 0031555889 scopus 로고    scopus 로고
    • Protein glycosylation in a heat-resistant rat fibroblast cell model expressing human HSP70
    • Henle, K. J., Jethmalani, S. M., Li, L., and Li, G. C. (1997). Protein glycosylation in a heat-resistant rat fibroblast cell model expressing human HSP70. Biochem. Biophys. Res. Commun. 232, 26-32.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 26-32
    • Henle, K.J.1    Jethmalani, S.M.2    Li, L.3    Li, G.C.4
  • 12
    • 0026752651 scopus 로고
    • Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin
    • Wang, S-Y. (1992). Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin. J. Biol. Chem. 267, 15362-15366.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15362-15366
    • Wang, S.-Y.1
  • 13
    • 0025160574 scopus 로고
    • A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue
    • Wang, S-Y., and Gudas, L. (1990). A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue. J. Biol. Chem. 265, 15818-15822.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15818-15822
    • Wang, S.-Y.1    Gudas, L.2
  • 14
    • 0031562683 scopus 로고    scopus 로고
    • Partial homology of stress glycoprotein GP62 with HSP70
    • Jethmalani, S. M., and Henle, K. J. (1997). Partial homology of stress glycoprotein GP62 with HSP70. Exp. Cell. Res. 232, 8-16.
    • (1997) Exp. Cell. Res. , vol.232 , pp. 8-16
    • Jethmalani, S.M.1    Henle, K.J.2
  • 16
    • 0027304377 scopus 로고
    • Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90)
    • Margolese, L., Waneck, G. L., Suzuki, C. K., Degen, E., Flavell, R. A., and Williams, D. B. (1993). Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90). J. Biol. Chem. 268, 17959-17966.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17959-17966
    • Margolese, L.1    Waneck, G.L.2    Suzuki, C.K.3    Degen, E.4    Flavell, R.A.5    Williams, D.B.6
  • 17
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, U.4
  • 18
    • 0028837979 scopus 로고
    • Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant-type p53
    • Sugito, K., Yamane, M., Hattori, H., Hayashi, Y., Tohnai, I., Ueda, M., Tsuchida, N., and Ohtsuka, K. (1995). Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant-type p53. FEBS Lett. 358, 161-164.
    • (1995) FEBS Lett. , vol.358 , pp. 161-164
    • Sugito, K.1    Yamane, M.2    Hattori, H.3    Hayashi, Y.4    Tohnai, I.5    Ueda, M.6    Tsuchida, N.7    Ohtsuka, K.8
  • 19
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, U.1
  • 20
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U., and Buchner, J. (1994). Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 23
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick, J., Aviel, S., and Argon, Y. (1992). The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J. Biol. Chem. 267, 21303-21306.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 25
    • 0028227245 scopus 로고
    • The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
    • Wartmann M., and Davis, R. J. (1994). The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269, 6695-6701.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6695-6701
    • Wartmann, M.1    Davis, R.J.2
  • 26
    • 0025128697 scopus 로고
    • r 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex
    • r 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 29, 520-527.
    • (1990) Biochemistry , vol.29 , pp. 520-527
    • Bresnick, E.H.1    Dalman, F.C.2    Pratt, W.B.3
  • 28
    • 0023937216 scopus 로고
    • Isoform composition and stoichiometry of the approximately 90-kDa heat shock protein associated with glucocorticoid receptors
    • Mendel, D. B., and Orti, E. (1988). Isoform composition and stoichiometry of the approximately 90-kDa heat shock protein associated with glucocorticoid receptors. J. Biol. Chem. 263, 6695-6702.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6695-6702
    • Mendel, D.B.1    Orti, E.2
  • 29
    • 0025951225 scopus 로고
    • A collagen-binding protein in the endoplasmic reticulum of myoblasts exhibits relationship with serine protease inhibitors
    • Clarke, E. P., Cates, G. A., Ball, E. H., and Sanwal, B. D. (1991). A collagen-binding protein in the endoplasmic reticulum of myoblasts exhibits relationship with serine protease inhibitors. J. Biol. Chem. 266, 17230-17235.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17230-17235
    • Clarke, E.P.1    Cates, G.A.2    Ball, E.H.3    Sanwal, B.D.4
  • 30
    • 0026530626 scopus 로고
    • Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins
    • Clarke, E. P., and Sanwal, B. D. (1992). Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins. Biochim. Biophys. Acta 1129, 246-248.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 246-248
    • Clarke, E.P.1    Sanwal, B.D.2
  • 31
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M.-J., and Sambrook, J. (1988). The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 33
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T., and Helenius, A. (1992). Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell. Biol. 117, 505-513.
    • (1992) J. Cell. Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 34
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose, S., Weikl, T., Buegl, H., and Buchner, J. (1996). Chaperone function of Hsp90-associated proteins. Science 274, 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Buegl, H.3    Buchner, J.4
  • 35
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., Toft, D. O., and Morimoto, R. I. (1996). Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 36
    • 0029807530 scopus 로고    scopus 로고
    • A cyclophilin function in Hsp90-dependent signal transduction
    • Duina, A. A., Chang, H-C. J., Marsh, J. A., Lindquist, S., and Gaber R. F. (1996). A cyclophilin function in Hsp90-dependent signal transduction. Science 274, 1713-1715.
    • (1996) Science , vol.274 , pp. 1713-1715
    • Duina, A.A.1    Chang, H.-C.J.2    Marsh, J.A.3    Lindquist, S.4    Gaber, R.F.5
  • 37
    • 0029777481 scopus 로고    scopus 로고
    • Efficient folding of firefly luciferase after transport into mammalian microsomes in the absence of luminal chaperones and folding catalysts
    • Tyedmers, J., Brunke, M., Lechte, M., Sandholzer, U., Dierks, T., Schlotterhose, P., Schmidt, B., and Zimmermann, R. (1996). Efficient folding of firefly luciferase after transport into mammalian microsomes in the absence of luminal chaperones and folding catalysts. J. Biol. Chem. 271, 19509-19513.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19509-19513
    • Tyedmers, J.1    Brunke, M.2    Lechte, M.3    Sandholzer, U.4    Dierks, T.5    Schlotterhose, P.6    Schmidt, B.7    Zimmermann, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.