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Volumn 21, Issue 24, 2002, Pages 6763-6770

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Author keywords

Glutathione; Molecular chaperone; Procollagen; Prolyl 4 hydroxylase; Protein disulfide isomerase

Indexed keywords

BINDING PROTEIN; CHAPERONE; GLUTATHIONE; GLUTATHIONE DISULFIDE; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN; POLYPEPTIDE; PROCOLLAGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE;

EID: 0037122001     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf685     Document Type: Article
Times cited : (86)

References (33)
  • 1
    • 12244296845 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum of unassembled procollagen C-propeptides
    • Bottomley, M.J., Batten, M.R., Lumb, R.A. and Bulleid, N.J. (2001) Quality control in the endoplasmic reticulum of unassembled procollagen C-propeptides. Curr. Biol., 11, 1-5.
    • (2001) Curr. Biol. , vol.11 , pp. 1-5
    • Bottomley, M.J.1    Batten, M.R.2    Lumb, R.A.3    Bulleid, N.J.4
  • 2
    • 0030812651 scopus 로고    scopus 로고
    • The C-propeptide of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis
    • Bulleid, N.J., Dalley, J.A. and Lees, J.F. (1997) The C-propeptide of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis. EMBO J., 16, 6694-6701.
    • (1997) EMBO J. , vol.16 , pp. 6694-6701
    • Bulleid, N.J.1    Dalley, J.A.2    Lees, J.F.3
  • 3
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai, H., Wang, C.-C. and Tsou, C.-L. (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem., 269, 24550-24552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.-C.2    Tsou, C.-L.3
  • 4
    • 0026648969 scopus 로고
    • Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the proα2(I) chain that preserves the gly-X-Y repeat pattern
    • Chessler, S.D. and Byers, P.H. (1992) Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the proα2(I) chain that preserves the gly-X-Y repeat pattern. J. Biol. Chem., 267, 7751-7757.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7751-7757
    • Chessler, S.D.1    Byers, P.H.2
  • 5
    • 0027182875 scopus 로고
    • BiP binds type I procollagen proαchains with mutations in the carboxy-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler, S.D. and Byers, P.H. (1993) BiP binds type I procollagen proαchains with mutations in the carboxy-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem., 268, 18226-18233.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 6
    • 0027959156 scopus 로고
    • Protein disulphide isomerase; building bridges in protein folding
    • Freedman, R.B., Hirst, T.R. and Tuite, M.F. (1994) Protein disulphide isomerase; building bridges in protein folding. Trends Biochem. Sci., 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 8
    • 0028190340 scopus 로고
    • Prolyl 4-hydroxylase: Defective assembly of α-subunit mutants indicates that α-subunit disulphide bonds are required for complex assembly
    • John, D.C.A. and Bulleid, N.J. (1994) Prolyl 4-hydroxylase: Defective assembly of α-subunit mutants indicates that α-subunit disulphide bonds are required for complex assembly. Biochemistry, 33, 14018-14025.
    • (1994) Biochemistry , vol.33 , pp. 14018-14025
    • John, D.C.A.1    Bulleid, N.J.2
  • 9
    • 0029795764 scopus 로고    scopus 로고
    • Intra-cellular dissociation and reassembly of prolyl 4-hydroxylase: The α-subunits associates with BiP allowing reassembly with the β-subunit
    • John, D.C.A. and Bulleid, N.J. (1996) Intra-cellular dissociation and reassembly of prolyl 4-hydroxylase: The α-subunits associates with BiP allowing reassembly with the β-subunit. Biochem. J., 317, 659-665.
    • (1996) Biochem. J. , vol.317 , pp. 659-665
    • John, D.C.A.1    Bulleid, N.J.2
  • 10
    • 0027415488 scopus 로고
    • Cell-free synthesis and assembly of prolyl 4-hydroxylase: The role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-subunit
    • John, D.C.A., Grant, M.E. and Bulleid, N.J. (1993) Cell-free synthesis and assembly of prolyl 4-hydroxylase: The role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-subunit. EMBO J., 12, 1587-1595.
    • (1993) EMBO J. , vol.12 , pp. 1587-1595
    • John, D.C.A.1    Grant, M.E.2    Bulleid, N.J.3
  • 11
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • Harding, J.J. and Crabbe, M.J.C. (eds). CRC Press, London, UK
    • Kivirikko, K.I., Myllyla, R. and Pihlajaniemi, T. (1992) Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In Harding, J.J. and Crabbe, M.J.C. (eds), Post Translational Modification of Proteins. CRC Press, London, UK, pp. 1-51.
    • (1992) Post Translational Modification of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllyla, R.2    Pihlajaniemi, T.3
  • 12
    • 0030875033 scopus 로고    scopus 로고
    • Interactions between protein disulphide isomerase and peptides
    • Klappa, P., Hawkins, H.C. and Freedman, R.B. (1997) Interactions between protein disulphide isomerase and peptides. Eur. J. Biochem., 248, 37-42.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 37-42
    • Klappa, P.1    Hawkins, H.C.2    Freedman, R.B.3
  • 13
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principle 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. (1998) The b′ domain provides the principle peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J., 17, 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
  • 14
    • 0037155282 scopus 로고    scopus 로고
    • Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47
    • Koide, T., Takahara, Y., Asada, S. and Nagata, K. (2002) Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47. J. Biol. Chem., 277, 6178-6182.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6178-6182
    • Koide, T.1    Takahara, Y.2    Asada, S.3    Nagata, K.4
  • 15
    • 0027967277 scopus 로고
    • The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and II procollagen
    • Lees, J.F. and Bulleid, N.J. (1994) The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and II procollagen. J. Biol. Chem., 269, 24354-24360.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24354-24360
    • Lees, J.F.1    Bulleid, N.J.2
  • 16
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady state kinetics and the utilisation of the oxidising equivalents of the isomerase
    • Lyles, M.M. and Gilbert, H.F. (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady state kinetics and the utilisation of the oxidising equivalents of the isomerase. Biochemistry, 30, 619-625.
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 17
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani, A., Fassio, A., Benham, A, Simmen, T., Braakman, I. and Sitia, R. (2001) Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J., 20, 6288-6296.
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 18
    • 0019881795 scopus 로고
    • Dissociation and reassociation of prolyl 4-hydroxylase subunits after cross-linking of monomers
    • Nietfeld, J.J., van der Kraan, J. and Kemp, A. (1981) Dissociation and reassociation of prolyl 4-hydroxylase subunits after cross-linking of monomers. Biochim. Biophys. Acta, 661, 21-27.
    • (1981) Biochim. Biophys. Acta , vol.661 , pp. 21-27
    • Nietfeld, J.J.1    Van der Kraan, J.2    Kemp, A.3
  • 19
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M.-L., Koivu, J. and Kivirikko, K.I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J., 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.-L.5    Koivu, J.6    Kivirikko, K.I.7
  • 20
    • 0035815678 scopus 로고    scopus 로고
    • Domains b′ and a′ of protein disulfide isomerase fulfil the minimal requirement for function as a subunit of prolyl 4-hydroxylase
    • Pirneskoski, A., Ruddock, L.W., Klappa, P., Freedman, R.B., Kivirikko, K.I. and Koivunen, P. (2001) Domains b′ and a′ of protein disulfide isomerase fulfil the minimal requirement for function as a subunit of prolyl 4-hydroxylase. J. Biol. Chem., 276, 11287-11293.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11287-11293
    • Pirneskoski, A.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4    Kivirikko, K.I.5    Koivunen, P.6
  • 21
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases and potential for therapy
    • Prockop, D.J. and Kivirikko, K.I. (1995) Collagens: Molecular biology, diseases and potential for therapy. Annu. Rev. Biochem., 64, 403-434.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 22
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig, A. and Gilbert, H.F. (1994) Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem., 269, 7764-7771.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 23
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulphide isomerase from its thioredoxin-like active site
    • Quan, H., Fan, G. and Wang, C.-C. (1995) Independence of the chaperone activity of protein disulphide isomerase from its thioredoxin-like active site. J. Biol. Chem., 270, 17078-17080.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.-C.3
  • 24
    • 0034657132 scopus 로고    scopus 로고
    • Hsp47: A molecular chaperone that interacts with and stabilises correctly folded procollagen
    • Tasab, M., Batten, M.R. and Bulleid, N.J. (2000) Hsp47: A molecular chaperone that interacts with and stabilises correctly folded procollagen. EMBO J., 19, 2204-2211.
    • (2000) EMBO J. , vol.19 , pp. 2204-2211
    • Tasab, M.1    Batten, M.R.2    Bulleid, N.J.3
  • 25
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulphide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W.I. and Rapoport, T.A. (2001) Protein disulphide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell, 104, 937-948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 26
    • 0026672695 scopus 로고
    • Site-directed mutagenesis of human protein disulphide isomerase: Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells
    • Vuori, K., Pihlajaniemi, T., Myllyla, R. and Kivirriko, K.I., (1992) Site-directed mutagenesis of human protein disulphide isomerase: Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells. EMBO J., 11, 4213-4218.
    • (1992) EMBO J. , vol.11 , pp. 4213-4218
    • Vuori, K.1    Pihlajaniemi, T.2    Myllyla, R.3    Kivirriko, K.I.4
  • 27
    • 0033591252 scopus 로고    scopus 로고
    • Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase
    • Walmsley, A.R., Batten, M.R., Lad, U. and Bulleid, N.J. (1999) Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase. J. Biol. Chem., 274, 14884- 14892.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14884-14892
    • Walmsley, A.R.1    Batten, M.R.2    Lad, U.3    Bulleid, N.J.4
  • 28
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau, J.R., Combs, K.A., Spinner, S.N. and Joiner, B.J. (1990) Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem., 265, 9800-9807.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 29
    • 0026052386 scopus 로고
    • Protein disulphide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein
    • Wetterau, J.R., Combs, K.A., McLean, L.R., Spinner, S.N. and Aggerbeck, L.P. (1991) Protein disulphide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein. Biochemistry, 30, 9728-9735.
    • (1991) Biochemistry , vol.30 , pp. 9728-9735
    • Wetterau, J.R.1    Combs, K.A.2    McLean, L.R.3    Spinner, S.N.4    Aggerbeck, L.P.5
  • 30
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane-proteins in semipermeabilized mammalian-cells
    • Wilson, R., Allen, A.J., Oliver, J., Brookman, J.L., High, S. and Bulleid, N.J. (1995) The translocation, folding, assembly and redox-dependent degradation of secretory and membrane-proteins in semipermeabilized mammalian-cells. Biochem. J., 307, 679-687.
    • (1995) Biochem. J. , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 31
    • 0032540353 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen
    • Wilson, R., Lees, J.F. and Bulleid, N.J. (1998) Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen. J. Biol. Chem., 273, 9637-9643.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9637-9643
    • Wilson, R.1    Lees, J.F.2    Bulleid, N.J.3
  • 32
    • 0037016671 scopus 로고    scopus 로고
    • Catalytic activity and chaperone function of human protein disulphide isomerase are required for the efficient refolding of proinsulin
    • Winter J., Klappa, P., Freedman, R.B., Lille, H. and Rudolph, R. (2002) Catalytic activity and chaperone function of human protein disulphide isomerase are required for the efficient refolding of proinsulin. J. Biol. Chem., 277, 310-317.
    • (2002) J. Biol. Chem. , vol.277 , pp. 310-317
    • Winter, J.1    Klappa, P.2    Freedman, R.B.3    Lille, H.4    Rudolph, R.5


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