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Volumn 311, Issue 2, 2003, Pages 405-414

Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity

Author keywords

Copper binding; Protein chaperone; Protein disulfide isomerase

Indexed keywords

APOPROTEIN; BATHOCUPROINEDISULFONIC ACID; CHAPERONE; CHELATING AGENT; COPPER; DITHIOTHREITOL; MONOMER; PROTEIN DISULFIDE ISOMERASE; REAGENT; REDUCING AGENT; TETRAMER; UNCLASSIFIED DRUG;

EID: 0242331275     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.226     Document Type: Article
Times cited : (47)

References (54)
  • 1
    • 0019317631 scopus 로고
    • Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds
    • Creighton T.E., Hillson D.A., Freedman R.B. Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds. J. Mol. Biol. 142:1980;43-62.
    • (1980) J. Mol. Biol. , vol.142 , pp. 43-62
    • Creighton, T.E.1    Hillson, D.A.2    Freedman, R.B.3
  • 2
    • 0033210414 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva R. Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum. Semin. Cell Dev. Biol. 10:1999;481-493.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 481-493
    • Noiva, R.1
  • 3
    • 0031939209 scopus 로고    scopus 로고
    • Protein disulfide isomerase
    • Gilbert H.F. Protein disulfide isomerase. Methods Enzymol. 290:1998;26-50.
    • (1998) Methods Enzymol. , vol.290 , pp. 26-50
    • Gilbert, H.F.1
  • 4
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles M.M., Gilbert H.F. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry. 30:1991;613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 5
    • 0026632893 scopus 로고
    • Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum
    • Zapun A., Creighton T.E., Rowling P.J., Freedman R.B. Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Proteins. 14:1992;10-15.
    • (1992) Proteins , vol.14 , pp. 10-15
    • Zapun, A.1    Creighton, T.E.2    Rowling, P.J.3    Freedman, R.B.4
  • 6
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby N.J., Penka E., Vincentelli R. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol. 276:1998;239-247.
    • (1998) J. Mol. Biol. , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 7
    • 0029819346 scopus 로고    scopus 로고
    • Identifying and characterizing a structural domain of protein disulfide isomerase
    • Darby N.J., Kemmink J., Creighton T.E. Identifying and characterizing a structural domain of protein disulfide isomerase. Biochemistry. 35:1996;10517-10528.
    • (1996) Biochemistry , vol.35 , pp. 10517-10528
    • Darby, N.J.1    Kemmink, J.2    Creighton, T.E.3
  • 8
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr. Biol. 7:1997;239-245.
    • (1997) Curr. Biol. , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 9
    • 0028225291 scopus 로고
    • Dissecting the mechanism of protein disulfide isomerase: Catalysis of disulfide bond formation in a model peptide
    • Darby N.J., Freedman R.B., Creighton T.E. Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide. Biochemistry. 33:1994;7937-7947.
    • (1994) Biochemistry , vol.33 , pp. 7937-7947
    • Darby, N.J.1    Freedman, R.B.2    Creighton, T.E.3
  • 10
    • 0032481380 scopus 로고    scopus 로고
    • ′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • ′ 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
  • 11
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A., Gilbert H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269:1994;7764-7771.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 12
    • 0027943682 scopus 로고
    • Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme
    • Puig A., Gilbert H.F. Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme. J. Biol. Chem. 269:1994;25889-25896.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25889-25896
    • Puig, A.1    Gilbert, H.F.2
  • 13
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi T., Helaakoski T., Tasanen K., Myllyla R., Huhtala M.L., Koivu J., Kivirikko K.I. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6:1987;643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 14
    • 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., Joiner B.J. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 265:1990;9801-9807.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9801-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 15
    • 0035808319 scopus 로고    scopus 로고
    • Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum
    • Primm T.P., Gilbert H.F. Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum. J. Biol. Chem. 276:2001;281-286.
    • (2001) J. Biol. Chem. , vol.276 , pp. 281-286
    • Primm, T.P.1    Gilbert, H.F.2
  • 17
    • 0030068075 scopus 로고    scopus 로고
    • ATP binding and hydrolysis by the multifunctional protein disulfide isomerase
    • Guthapfel R., Gueguen P., Quemeneur E. ATP binding and hydrolysis by the multifunctional protein disulfide isomerase. J. Biol. Chem. 271:1996;2663-2666.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2663-2666
    • Guthapfel, R.1    Gueguen, P.2    Quemeneur, E.3
  • 18
    • 0020787176 scopus 로고
    • Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure
    • Lambert N., Freedman R.B. Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure. Biochem. J. 213:1983;225-234.
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 19
    • 0028070283 scopus 로고
    • Association and dissociation of protein disulfide isomerase
    • Yu X.C., Wang C.C., Tsou C.L. Association and dissociation of protein disulfide isomerase. Biochim. Biophys. Acta. 1207:1994;109-113.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 109-113
    • Yu, X.C.1    Wang, C.C.2    Tsou, C.L.3
  • 20
    • 0023676384 scopus 로고
    • Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cells
    • Akagi S., Yamamoto A., Yoshimori T., Masaki R., Ogawa R., Tashiro Y. Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cells. J. Histochem. Cytochem. 36:1988;1069-1074.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 1069-1074
    • Akagi, S.1    Yamamoto, A.2    Yoshimori, T.3    Masaki, R.4    Ogawa, R.5    Tashiro, Y.6
  • 21
  • 22
    • 0027379850 scopus 로고
    • Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats
    • Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T. Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats. Biochim. Biophys. Acta. 1158:1993;339-344.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 339-344
    • Yokoi, T.1    Nagayama, S.2    Kajiwara, R.3    Kawaguchi, Y.4    Horiuchi, R.5    Kamataki, T.6
  • 23
    • 0028093077 scopus 로고
    • Calcium binding properties of rabbit liver protein disulfide isomerase
    • Lebeche D., Lucero H.A., Kaminer B. Calcium binding properties of rabbit liver protein disulfide isomerase. Biochem. Biophys. Res. Commun. 202:1994;556-561.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 556-561
    • Lebeche, D.1    Lucero, H.A.2    Kaminer, B.3
  • 24
    • 0033613952 scopus 로고    scopus 로고
    • The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase
    • Lucero H.A., Kaminer B. The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase. J. Biol. Chem. 274:1999;3243-3251.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3243-3251
    • Lucero, H.A.1    Kaminer, B.2
  • 26
    • 0028242939 scopus 로고
    • Wilson disease and Menkes disease: New handles on heavy-metal transport
    • Bull P.C., Cox D.W. Wilson disease and Menkes disease: new handles on heavy-metal transport. Trends Genet. 10:1994;246-252.
    • (1994) Trends Genet. , vol.10 , pp. 246-252
    • Bull, P.C.1    Cox, D.W.2
  • 27
    • 0030898098 scopus 로고    scopus 로고
    • Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis
    • Klomp L.W., Lin S.J., Yuan D.S., Klausner R.D., Culotta V.C., Gitlin J.D. Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J. Biol. Chem. 272:1997;9221-9226.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9221-9226
    • Klomp, L.W.1    Lin, S.J.2    Yuan, D.S.3    Klausner, R.D.4    Culotta, V.C.5    Gitlin, J.D.6
  • 31
    • 85007176782 scopus 로고    scopus 로고
    • B. Sarkar, N. Spitale, Y.-M. She, S. Narindrasorasak, P. Yao, E. Roberts, S. Yang, in: Proceedings of the Third International Conference on Copper Homeostasis and its Disorder: Molecular and Cellular Aspects, October 4-8, 2002, Ischia, Italy
    • B. Sarkar, N. Spitale, Y.-M. She, S. Narindrasorasak, P. Yao, E. Roberts, S. Yang, in: Proceedings of the Third International Conference on Copper Homeostasis and its Disorder: Molecular and Cellular Aspects, October 4-8, 2002, Ischia, Italy.
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 85007190980 scopus 로고    scopus 로고
    • T.E. Creighton, Disulfide Bonds between Cysteines., ed., IRL Press at Oxford University Press, Oxford, 1993
    • T.E. Creighton, Disulfide Bonds between Cysteines., ed., IRL Press at Oxford University Press, Oxford, 1993.
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0017114103 scopus 로고
    • Copper and the oxidation of hemoglobin: A comparison of horse and human hemoglobins
    • Rifkind J.M., Lauer L.D., Chiang S.C., Li N.C. Copper and the oxidation of hemoglobin: a comparison of horse and human hemoglobins. Biochemistry. 15:1976;5337-5343.
    • (1976) Biochemistry , vol.15 , pp. 5337-5343
    • Rifkind, J.M.1    Lauer, L.D.2    Chiang, S.C.3    Li, N.C.4
  • 37
    • 0028945240 scopus 로고
    • A quantitative test for copper using bicinchoninic acid
    • Brenner A.J., Harris E.D. A quantitative test for copper using bicinchoninic acid. Anal. Biochem. 226:1995;80-84.
    • (1995) Anal. Biochem. , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 38
  • 40
    • 0021356888 scopus 로고
    • Preferential binding of copper to the beta domain of metallothionein
    • Nielson K.B., Winge D.R. Preferential binding of copper to the beta domain of metallothionein. J. Biol. Chem. 259:1984;4941-4946.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4941-4946
    • Nielson, K.B.1    Winge, D.R.2
  • 41
    • 0034739907 scopus 로고    scopus 로고
    • Reactivity of Cd7-metallothionein with Cu(II) ions: Evidence for a cooperative formation of Cd3, Cu(I)5-metallothionein
    • Vaher M., Romero-Isart N., Vasak M., Palumaa P. Reactivity of Cd7-metallothionein with Cu(II) ions: evidence for a cooperative formation of Cd3, Cu(I)5-metallothionein. J. Inorg. Biochem. 83:2001;1-6.
    • (2001) J. Inorg. Biochem. , vol.83 , pp. 1-6
    • Vaher, M.1    Romero-Isart, N.2    Vasak, M.3    Palumaa, P.4
  • 42
    • 0031215133 scopus 로고    scopus 로고
    • Copper-binding motifs in catalysis, transport, detoxification and signaling
    • Koch K.A., Pena M.M., Thiele D.J. Copper-binding motifs in catalysis, transport, detoxification and signaling. Chem. Biol. 4:1997;549-560.
    • (1997) Chem. Biol. , vol.4 , pp. 549-560
    • Koch, K.A.1    Pena, M.M.2    Thiele, D.J.3
  • 44
    • 0037135627 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake
    • Puig S., Lee J., Lau M., Thiele D.J. Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake. J. Biol. Chem. 277:2002;26021-26030.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26021-26030
    • Puig, S.1    Lee, J.2    Lau, M.3    Thiele, D.J.4
  • 45
    • 0037389858 scopus 로고    scopus 로고
    • A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites
    • Arnesano F., Banci L., Bertini I., Mangani S., Thompsett A.R. A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites. Proc. Natl. Acad. Sci. USA. 100:2003;3814-3819.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3814-3819
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Mangani, S.4    Thompsett, A.R.5
  • 46
  • 47
    • 0029973729 scopus 로고    scopus 로고
    • Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy
    • Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry. 35:1996;7684-7691.
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 48
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont A.K., Huffman D.L., Lamb A.L., O'Halloran T.V., Rosenzweig A.C. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 7:2000;766-771.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 49
    • 0034647447 scopus 로고    scopus 로고
    • Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus
    • Yeh A.P., Chatelet C., Soltis S.M., Kuhn P., Meyer J., Rees D.C. Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. J. Mol. Biol. 300:2000;587-595.
    • (2000) J. Mol. Biol. , vol.300 , pp. 587-595
    • Yeh, A.P.1    Chatelet, C.2    Soltis, S.M.3    Kuhn, P.4    Meyer, J.5    Rees, D.C.6
  • 50
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • Huffman D.L., O'Halloran T.V. Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J. Biol. Chem. 275:2000;18611-18614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 51
    • 0029163450 scopus 로고
    • Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes
    • Terada K., Manchikalapudi P., Noiva R., Jauregui H.O., Stockert R.J., Schilsky M.L. Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes. J. Biol. Chem. 270:1995;20410-20416.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20410-20416
    • Terada, K.1    Manchikalapudi, P.2    Noiva, R.3    Jauregui, H.O.4    Stockert, R.J.5    Schilsky, M.L.6
  • 52
    • 0025045118 scopus 로고
    • Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal
    • Yoshimori T., Semba T., Takemoto H., Akagi S., Yamamoto A., Tashiro Y. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J. Biol. Chem. 265:1990;15984-15990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15984-15990
    • Yoshimori, T.1    Semba, T.2    Takemoto, H.3    Akagi, S.4    Yamamoto, A.5    Tashiro, Y.6
  • 53
    • 0026740150 scopus 로고
    • Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver
    • Wroblewski V.J., Masnyk M., Khambatta S.S., Becker G.W. Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver. Diabetes. 41:1992;539-547.
    • (1992) Diabetes , vol.41 , pp. 539-547
    • Wroblewski, V.J.1    Masnyk, M.2    Khambatta, S.S.3    Becker, G.W.4
  • 54
    • 0026049436 scopus 로고
    • Characterization of a N-bromoacetyl-L-thyroxine affinity-labeled 55-kilodalton protein as protein disulfide isomerase in cultured glial cells
    • Safran M., Leonard J.L. Characterization of a N-bromoacetyl-L-thyroxine affinity-labeled 55-kilodalton protein as protein disulfide isomerase in cultured glial cells. Endocrinology. 129:1991;2011-2016.
    • (1991) Endocrinology , vol.129 , pp. 2011-2016
    • Safran, M.1    Leonard, J.L.2


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