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Volumn 120, Issue 3, 1996, Pages 525-530

A role of PDI in the reductive cleavage of mixed disulfides

Author keywords

Glutathione; Human lysozyme; Protein disulfide isomerase; Protein folding; Reductive cleavage of disulfide bond

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); CYSTEINE DERIVATIVE; DISULFIDE; GLUTATHIONE DERIVATIVE; LYSOZYME; PROTEIN DISULFIDE ISOMERASE;

EID: 0029784084     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021445     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger, R.F., Epstein, C.J., and Anfinsen, C.B. (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238, 628-635
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 2
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins:protein disulfide-isomerase
    • Wold, F. and Moldave, K., eds. Academic Press, New York
    • Hillson, D.A., Lambert, N., and Freedman, R.B. (1984) Formation and isomerization of disulfide bonds in proteins:protein disulfide-isomerase in Methods in Enzymology (Wold, F. and Moldave, K., eds.) Vol. 107, pp. 281-294, Academic Press, New York
    • (1984) Methods in Enzymology , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 3
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
    • Bulleid, N.J. and Freedman, R.B. (1988) Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 335, 649-651
    • (1988) Nature , vol.335 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • Cheng, S., Gong, Q., Parkison, C., Robinson, E.A., Appella, E., Merlino, G.T., and Pastan, I. (1987) The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J. Biol. Chem. 262, 11221-11227
    • (1987) J. Biol. Chem. , vol.262 , pp. 11221-11227
    • Cheng, S.1    Gong, Q.2    Parkison, C.3    Robinson, E.A.4    Appella, E.5    Merlino, G.T.6    Pastan, I.7
  • 7
    • 0023653293 scopus 로고
    • Sequence of membrane-associated thyroid hormone binding protein from bovine liver: Its identity with protein disulphide isomerase
    • Yamauchi, K., Yamamoto, T., Hayashi, H., Koya, S., Takikawa, H., Toyoshima, K., and Horiuchi, R. (1987) Sequence of membrane-associated thyroid hormone binding protein from bovine liver: Its identity with protein disulphide isomerase. Biochem. Biophys. Res. Commun. 146, 1485-1492
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 1485-1492
    • Yamauchi, K.1    Yamamoto, T.2    Hayashi, H.3    Koya, S.4    Takikawa, H.5    Toyoshima, K.6    Horiuchi, R.7
  • 8
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells, W.W., Xu, O.P., Yang, Y., and Rocque, P.A. (1990) Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265, 15361-15364
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, O.P.2    Yang, Y.3    Rocque, P.A.4
  • 9
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis, G.-B. and Holmgren, A. (1980) Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255, 10261-10265
    • (1980) J. Biol. Chem. , vol.255 , pp. 10261-10265
    • Kallis, G.-B.1    Holmgren, A.2
  • 10
    • 0025801897 scopus 로고
    • The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
    • Hawkins, H.C. and Freedman, R.B. (1991) The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase. Biochem. J. 275, 335-339
    • (1991) Biochem. J. , vol.275 , pp. 335-339
    • Hawkins, H.C.1    Freedman, R.B.2
  • 11
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Nelson, J.W. and Creighton, T.E. (1994) Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33, 5974-5983
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 12
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli
    • Vouri, K., Myllylä, R., Pihlajaniemi, T., and Kivirikko, K.I. (1992) Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. J. Biol. Chem. 267, 7211-7214
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vouri, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 13
    • 0025861453 scopus 로고
    • Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase
    • Morjana, N.A. and Gilbert, H.F. (1991) Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase. Biochemistry 30, 4985-4990
    • (1991) Biochemistry , vol.30 , pp. 4985-4990
    • Morjana, N.A.1    Gilbert, H.F.2
  • 14
    • 0025115651 scopus 로고
    • Secretion in yeast of mutant human lysozymes with and without glutathione bound tocysteine 95
    • Taniyama, Y., Seko, C., and Kikuchi, M. (1990) Secretion in yeast of mutant human lysozymes with and without glutathione bound tocysteine 95. J. Biol. Chem. 265, 16767-16771
    • (1990) J. Biol. Chem. , vol.265 , pp. 16767-16771
    • Taniyama, Y.1    Seko, C.2    Kikuchi, M.3
  • 15
    • 0027279470 scopus 로고
    • PDI and glutathionemediated reduction of the glutathionylated variant of human lysozyme
    • Hayano, T., Inaka, K., Otsu, M., Taniyama, Y., Miki, K., Matsushima, M., and Kikuchi, M. (1993) PDI and glutathionemediated reduction of the glutathionylated variant of human lysozyme. FEBS Lett. 328, 203-208
    • (1993) FEBS Lett. , vol.328 , pp. 203-208
    • Hayano, T.1    Inaka, K.2    Otsu, M.3    Taniyama, Y.4    Miki, K.5    Matsushima, M.6    Kikuchi, M.7
  • 16
    • 0028896188 scopus 로고
    • Structure of a glutathionylated human lysozyme: A folding intermediate mimic in the formation of a disulfide bond
    • Inaka, K., Miki, K., Kikuchi, M., Taniyama, Y., and Matsushima, M. (1995) Structure of a glutathionylated human lysozyme: A folding intermediate mimic in the formation of a disulfide bond. Acta Cryst. D51, 619-625
    • (1995) Acta Cryst. , vol.D51 , pp. 619-625
    • Inaka, K.1    Miki, K.2    Kikuchi, M.3    Taniyama, Y.4    Matsushima, M.5
  • 17
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J., and Lodish, H.F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 18
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere, M.C.A., Sturley, S.L., and Raines, R.T. (1995) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270, 28006-28009
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.A.1    Sturley, S.L.2    Raines, R.T.3
  • 19
    • 0020787176 scopus 로고
    • Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure
    • Lambert, N. and Freedman, R.B. (1983) Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure. Biochem. J. 213, 225-234
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 21
    • 0015578109 scopus 로고
    • Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae
    • Toh-e, A., Ueda, Y., Kakimoto, S., and Oshima, Y. (1973) Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae. J. Bacterial. 113, 727-738
    • (1973) J. Bacterial. , vol.113 , pp. 727-738
    • Toh-e, A.1    Ueda, Y.2    Kakimoto, S.3    Oshima, Y.4
  • 22
  • 23
    • 0027992695 scopus 로고
    • Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0
    • Song, H., Inaka, K., Maenaka, K., and Matsushima, M. (1994) Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0. J. Mol. Biol. 244, 522-540
    • (1994) J. Mol. Biol. , vol.244 , pp. 522-540
    • Song, H.1    Inaka, K.2    Maenaka, K.3    Matsushima, M.4
  • 28
    • 0023140814 scopus 로고
    • Crystallographic R- factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J., and Karplus, M. (1987) Crystallographic R- factor refinement by molecular dynamics. Science 35, 458-460
    • (1987) Science , vol.35 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 30
    • 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
  • 31
    • 0029620311 scopus 로고
    • Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell
    • Hayano, T., Hirose, M., and Kikuchi, M. (1995) Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377, 505-511
    • (1995) FEBS Lett. , vol.377 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 32
    • 0025769871 scopus 로고
    • Formation of enzyme-substrate disulfide linkage during catalysis by protein disulfide isomerase
    • Hu, C.-H. and Tsou, C.-L. (1991) Formation of enzyme-substrate disulfide linkage during catalysis by protein disulfide isomerase. FEBS Lett. 290, 87-89
    • (1991) FEBS Lett. , vol.290 , pp. 87-89
    • Hu, C.-H.1    Tsou, C.-L.2
  • 33
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva, R., Freedman, R.B., and Lennarz, W.J. (1993) Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J. Biol. Chem. 268, 19210-19217
    • (1993) J. Biol. Chem. , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 34
    • 0021795061 scopus 로고
    • Labeling of cysteinecontaining peptides with 2-nitro-5-thiobenzoic acid
    • Sliwkowski, M.X. and Levine, R.L. (1985) Labeling of cysteinecontaining peptides with 2-nitro-5-thiobenzoic acid. Anal. Biochem. 147, 369-373
    • (1985) Anal. Biochem. , vol.147 , pp. 369-373
    • Sliwkowski, M.X.1    Levine, R.L.2
  • 35
    • 0028310850 scopus 로고
    • Protein-S-S-glutathione mixed disulfides as models of unfolded protein
    • Ruoppolo, M. and Freedman, R.B. (1994) Protein-S-S-glutathione mixed disulfides as models of unfolded protein. Biochemistry 33, 76547662
    • (1994) Biochemistry , vol.33 , pp. 76547662
    • Ruoppolo, M.1    Freedman, R.B.2


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