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Volumn 18, Issue 23, 1999, Pages 6718-6729

Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins

Author keywords

Calreticulin; Endoplasmic reticulum; Molecular chaperone; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALRETICULIN; CHAPERONE; GLYCOPROTEIN; LECTIN; OLIGOSACCHARIDE; PROTEIN; ZINC ION;

EID: 0033485263     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.23.6718     Document Type: Article
Times cited : (226)

References (36)
  • 1
    • 84987350951 scopus 로고
    • Immunoglobulins from egg yolk: Isolation and purification
    • Akita, E.M. and Nakai, S. (1992) Immunoglobulins from egg yolk: isolation and purification. J. Food Sci., 57, 629-634.
    • (1992) J. Food Sci. , vol.57 , pp. 629-634
    • Akita, E.M.1    Nakai, S.2
  • 2
    • 0028888054 scopus 로고
    • Molecular requirements for the interaction of class II major histocompalibility complex molecules and invariant chain with calnexin
    • Arunachalam, B. and Cresswell, P. (1995) Molecular requirements for the interaction of class II major histocompalibility complex molecules and invariant chain with calnexin. J. Biol. Chem., 270, 2784-2790.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2784-2790
    • Arunachalam, B.1    Cresswell, P.2
  • 4
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh, S., Burns, K. Andrin, C. and Michalak, M. (1995) Interaction of calreticulin with protein disulfide isomerase. J. Biol. Chem., 270, 31338-31344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 5
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity
    • Basu, S. and Srivastava, P.K. (1999) Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J. Exp. Med., 189, 797-802.
    • (1999) J. Exp. Med. , vol.189 , pp. 797-802
    • Basu, S.1    Srivastava, P.K.2
  • 6
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner, J. (1999) Hsp90 & Co. - a holding for folding. Trends Biochem. Sci., 24, 136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 8
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner, J., Grallert, H. and Jakob, U. (1998) Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol., 290, 323-338.
    • (1998) Methods Enzymol. , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell, 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0026665249 scopus 로고
    • Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94
    • Clairmont, C.A., De Maio, A. and Hirschberg, C.B. (1992) Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. J. Biol. Chem., 267, 3983-3990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3983-3990
    • Clairmont, C.A.1    De Maio, A.2    Hirschberg, C.B.3
  • 12
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott, J.G., Oliver, J.D. and High, S. (1997) The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem., 272, 13849-13855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 13
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperone hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B.C. and Morimoto, R.I. (1996) The human cytosolic molecular chaperone hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J., 15, 2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 14
    • 0027474622 scopus 로고
    • Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro
    • Hartman, D.J., Surin, B.P., Dixon, N.E., Hoogenraad, N.J. and Høj, P.B. (1993) Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro. Proc. Natl Acad. Sci. USA, 90, 2276-2280.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2276-2280
    • Hartman, D.J.1    Surin, B.P.2    Dixon, N.E.3    Hoogenraad, N.J.4    Høj, P.B.5
  • 16
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara, Y., Cohen-Doyle, M.F., Saito, Y. and Williams, D.B. (1999) Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol. Cell, 4, 331-341.
    • (1999) Mol. Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 17
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase
    • Jakob, U., Lilie, H., Meyer, I. and Buchner, J. (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. J. Biol. Chem., 270, 7288-7294.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 19
    • 0023037907 scopus 로고
    • Conformational changes induced by binding of divalent cations to calregulin
    • Khanna, N.C., Tokuda, M. and Waisman, D.M. (1986) Conformational changes induced by binding of divalent cations to calregulin. J. Biol. Chem., 261, 8883-8887.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8883-8887
    • Khanna, N.C.1    Tokuda, M.2    Waisman, D.M.3
  • 20
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.-H. and Michalak, M. (1997) Calreticulin. Cell, 88, 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.-H.1    Michalak, M.2
  • 22
    • 0344495003 scopus 로고    scopus 로고
    • Calnexin, calreticulin and glycoprolein folding within the endoplasmic reticulum
    • Ernst, B., Sinay, P. and Hart, G. (eds), Wiley-VCH, Weinheim, Germany, in press
    • Leach, M. and Williams, D.B. (1999) Calnexin, calreticulin and glycoprolein folding within the endoplasmic reticulum. In Ernst, B., Sinay, P. and Hart, G. (eds), Oligosaccharides in Chemistry and Biology - A Comprehensive Handbook. Wiley-VCH, Weinheim, Germany, in press.
    • (1999) Oligosaccharides in Chemistry and Biology - A Comprehensive Handbook
    • Leach, M.1    Williams, D.B.2
  • 23
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heal-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee, G.J., Roseman, A.M., Saibil, H.R. and Vierling, E. (1997) A small heat shock protein stably binds heal-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J., 16, 659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 24
    • 0026320296 scopus 로고
    • The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
    • Liberek, K., Skowyra, D., Zylicz, M., Johnson, C. and Georgopoulos, C. (1991) The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem., 266, 14491-14496.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14491-14496
    • Liberek, K.1    Skowyra, D.2    Zylicz, M.3    Johnson, C.4    Georgopoulos, C.5
  • 25
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human αB crystallin
    • Muchowski, P.J. and Clark, J.I. (1998) ATP-enhanced molecular chaperone functions of the small heat shock protein human αB crystallin. Proc. Natl Acad. Sci. USA, 95, 1004-1009.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 27
    • 0026329037 scopus 로고
    • Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein
    • Ohta, M., Hamako, J., Yamamoto, S., Hatta, H., Kim, M., Yamamoto, T., Oka, S., Mizuochi, T. and Matsuura, F. (1991) Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein. Glycoconj. J., 8, 400-413.
    • (1991) Glycoconj. J. , vol.8 , pp. 400-413
    • Ohta, M.1    Hamako, J.2    Yamamoto, S.3    Hatta, H.4    Kim, M.5    Yamamoto, T.6    Oka, S.7    Mizuochi, T.8    Matsuura, F.9
  • 28
    • 0029160540 scopus 로고
    • Transient, lectinlike association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J.R., Ora, A., Van, P.N. and Helenius, A. (1995) Transient, lectinlike association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol Cell, 6, 1173-1184.
    • (1995) Mol. Biol Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 29
    • 0024951488 scopus 로고
    • Localization of intracellular zinc under conditions of altered permeability control of the plasma membrane
    • Reddy, AG., Devi, B.G., Rao, S.B. and Gupta, P.D. (1989) Localization of intracellular zinc under conditions of altered permeability control of the plasma membrane. Cytobios, 60, 21-26.
    • (1989) Cytobios , vol.60 , pp. 21-26
    • Reddy, A.G.1    Devi, B.G.2    Rao, S.B.3    Gupta, P.D.4
  • 30
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • Rodan, A.R., Simons, J.F., Trombetta, E.S. and Helenius, A. (1996) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J., 15, 6921-6930.
    • (1996) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 31
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M. and Parodi, A.J. (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J., 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 32
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro, R.G., Zhu, Q., Bhoyroo, V. and Söling, H.-D. (1996) Definition of the lectin-like properties of the molecular chaperone, calreticulin and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol Chem., 271, 11588-11594.
    • (1996) J. Biol Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.-D.4
  • 33
    • 0032111954 scopus 로고    scopus 로고
    • Chaperone properties of calreticulin
    • Sværke, C. and Houen, G. (1998) Chaperone properties of calreticulin. Acta Chem. Scand, 52, 942-949.
    • (1998) Acta Chem. Scand , vol.52 , pp. 942-949
    • Sværke, C.1    Houen, G.2
  • 34
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos, A., Michalak, M., Lehrman, M.A. and Williams, D.B. (1998) Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry, 37, 3480-3490.
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 36
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun, A., Darby, N.J., Tessier, D.C. Michalak, M., Bergeron, J.J.M. and Thomas, D.Y. (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem., 273, 6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.M.5    Thomas, D.Y.6


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