메뉴 건너뛰기




Volumn 130, Issue 5 SUPPL., 2000, Pages

The function of zinc metallothionein: A link between cellular zinc and redox state

Author keywords

ATP; Glutathione; Metallothionein; Redox regulation; Zinc

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; METALLOTHIONEIN; SELENIUM DERIVATIVE; SULFUR; ZINC;

EID: 0034058549     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/130.5.1455s     Document Type: Conference Paper
Times cited : (358)

References (42)
  • 1
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts, I. L., Nadassy, K. & Wodak, S. J. (1998) Analysis of zinc binding sites in protein crystal structures. Prot. Sci. 7: 1700-1716.
    • (1998) Prot. Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 3
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • Atar, D., Backx, P. H., Appel, M. M., Gao, W. D. & arban, E. (1995) Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels. J. Biol. Chem. 270: 2473-2477.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2473-2477
    • Atar, D.1    Backx, P.H.2    Appel, M.M.3    Gao, W.D.4    Arban, E.5
  • 5
    • 0027204255 scopus 로고
    • A putative glutathione-binding site in Cd, Zn-metallothionein identified by equilibrium binding and molecular-modeling studies
    • Brouwer, M., Hoexum-Brouwer, T. & Cashon, R. E. (1993) A putative glutathione-binding site in Cd, Zn-metallothionein identified by equilibrium binding and molecular-modeling studies. Biochem. J. 294: 219-225.
    • (1993) Biochem. J. , vol.294 , pp. 219-225
    • Brouwer, M.1    Hoexum-Brouwer, T.2    Cashon, R.E.3
  • 6
    • 0015978108 scopus 로고
    • Human hepatic metallothioneins
    • Bühler, R.H.O. an Kägi, J.H.R. (1974) Human hepatic metallothioneins. FEBS Lett. 39: 229-234.
    • (1974) FEBS Lett. , vol.39 , pp. 229-234
    • Bühler, R.H.O.1    Kägi, J.H.R.2
  • 7
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon, R. H. (1995) Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Rad. Biol. Med. 18: 775-794.
    • (1995) Free Rad. Biol. Med. , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 8
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis
    • Cai, J. & Jones, D. P. (1998) Superoxide in apoptosis. J. Biol. Chem. 273: 11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 9
    • 0024307951 scopus 로고
    • Activation of pyridoxal kinase by metallothionein
    • Churchich, J. E., Scholz, G. & Kwok, F. (1989) Activation of pyridoxal kinase by metallothionein. Biochim. Biophys. Acta 996: 181-186.
    • (1989) Biochim. Biophys. Acta , vol.996 , pp. 181-186
    • Churchich, J.E.1    Scholz, G.2    Kwok, F.3
  • 10
    • 0030020153 scopus 로고    scopus 로고
    • Cooperation of protein disulfide isomerase and redox environment in the regulation of NF-kappaB and AP1 binding to DNA
    • Clive, D. R. & Greene, J. J. (1996) Cooperation of protein disulfide isomerase and redox environment in the regulation of NF-kappaB and AP1 binding to DNA. Cell Biochem. Funct. 14: 49-55.
    • (1996) Cell Biochem. Funct. , vol.14 , pp. 49-55
    • Clive, D.R.1    Greene, J.J.2
  • 11
    • 0024789690 scopus 로고
    • Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example
    • Csermely, P., Sandor, P., Radics, L. & Somogyi, J. (1989) Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example. Biochem. Biophys. Res. Commun. 165: 838-844.
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 838-844
    • Csermely, P.1    Sandor, P.2    Radics, L.3    Somogyi, J.4
  • 12
    • 0031149804 scopus 로고    scopus 로고
    • Redox state changes in density-dependent regulation of proliferation
    • Hutter, D. E., Till, B. G. & Greene, J. J. (1997) Redox state changes in density-dependent regulation of proliferation. Exp. Cell Res. 232: 435-438.
    • (1997) Exp. Cell Res. , vol.232 , pp. 435-438
    • Hutter, D.E.1    Till, B.G.2    Greene, J.J.3
  • 13
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Washington, DC
    • Hwang, C., Sinskey, A. J. & Lodish, H. F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science (Washington, DC) 257: 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 14
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob, C., Maret, W. & Vallee, B. L. (1998a) Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc. Natl. Acad. Sci. U.S.A. 95: 3489-3494.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 15
    • 0032581362 scopus 로고    scopus 로고
    • Ebselen, a selenium-containing redox drug, releases zinc from metallothionein
    • Jacob, C., Maret, W. & Vallee, B. L. (1998b) Ebselen, a selenium-containing redox drug, releases zinc from metallothionein. Biochem. Biophys. Res. Commun. 248: 569-573.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 569-573
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 16
    • 0032584078 scopus 로고    scopus 로고
    • The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase
    • Jiang, L.-J., Maret, W. & Vallee, B. L. (1998a) The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 95: 3483-3488.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3483-3488
    • Jiang, L.-J.1    Maret, W.2    Vallee, B.L.3
  • 18
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zinc-thiol/ disulfide interchange
    • Maret, W. (1994) Oxidative metal release from metallothionein via zinc-thiol/ disulfide interchange. Proc. Natl. Acad. Sci. U.S.A. 91: 237-241.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 237-241
    • Maret, W.1
  • 19
    • 0029063792 scopus 로고
    • Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc
    • Maret, W. (1995) Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc. Neurochem. Int. 27: 111-117.
    • (1995) Neurochem. Int. , vol.27 , pp. 111-117
    • Maret, W.1
  • 20
    • 0030964915 scopus 로고    scopus 로고
    • Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Gal4
    • Maret, W., Larsen, K. S. & Vallee, B. L. (1997) Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Gal4. Proc. Natl. Acad. Sci. U.S.A. 94: 2233-2237.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2233-2237
    • Maret, W.1    Larsen, K.S.2    Vallee, B.L.3
  • 21
    • 0001950228 scopus 로고    scopus 로고
    • The glutathione redox state and zinc mobilization from metallothionein and other proteins with zinc-sulfur coordination sites
    • Shaw, A. C., ed., Taylor & Francis, Washington, DC
    • Maret, W. (1998) The glutathione redox state and zinc mobilization from metallothionein and other proteins with zinc-sulfur coordination sites. In: Glutathione in the Nervous System (Shaw, A. C., ed.), pp. 257-273, Taylor & Francis, Washington, DC.
    • (1998) Glutathione in the Nervous System , pp. 257-273
    • Maret, W.1
  • 22
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret, W. & Vallee, B. L. (1998) Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc. Natl. Acad. Sci. U.S.A. 95: 3478-3482.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 24
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. (1988) Glutathione metabolism and its selective modification. J. Biol. Chem. 263: 17205-17208.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 25
    • 0027204069 scopus 로고
    • Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse
    • Michalska, A. E. & Choo, K.H.A. (1993) Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse. Proc. Natl. Acad. Sci. U.S.A. 90: 8088-8092.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8088-8092
    • Michalska, A.E.1    Choo, K.H.A.2
  • 26
    • 0028836796 scopus 로고
    • Cell cycle regulation of metallothionein in human colonie cancer cells
    • Nagel, W. W. & Vallee, B. L. (1995) Cell cycle regulation of metallothionein in human colonie cancer cells. Proc. Natl. Acad. Sci. U.S.A. 92: 579-583.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 579-583
    • Nagel, W.W.1    Vallee, B.L.2
  • 27
    • 0025919750 scopus 로고
    • Stereospecificity of the metal ATP complex in flavokinase from rat small intestine
    • Nakano, H. & McCormick, D. B. (1991) Stereospecificity of the metal ATP complex in flavokinase from rat small intestine. J. Biol. Chem. 266: 22125-22128.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22125-22128
    • Nakano, H.1    McCormick, D.B.2
  • 28
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter, R. D. (1998) The elusive function of metallothioneins. Proc. Natl. Acad. Sci. U.S.A. 95: 8428-8430.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 29
    • 0015239110 scopus 로고
    • Metal complexes of phosphoglucomutase in vivo
    • Peck, E. J. & Ray, W. J. (1971) Metal complexes of phosphoglucomutase in vivo. J. Biol. Chem. 246: 1160-1167.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1160-1167
    • Peck, E.J.1    Ray, W.J.2
  • 32
    • 0027533505 scopus 로고
    • Ebselen, a selenoorganic compound as glutathione peroxidase mimic
    • Sies, H. (1993) Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Rad. Biol. Med. 14: 313-323.
    • (1993) Free Rad. Biol. Med. , vol.14 , pp. 313-323
    • Sies, H.1
  • 33
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons, T.J.B. (1991) Intracellular free zinc and zinc buffering in human red blood cells. J. Membr. Biol. 123: 63-71.
    • (1991) J. Membr. Biol. , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 34
    • 0030019808 scopus 로고    scopus 로고
    • The in vitro ejection of zinc from human immunodeficiency virus (HIV) type I nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity
    • Tummino, P. J., Scholten, J. D., Harvey, P. J., Holler, T. P., Maloney, L., Gogliotti, R., Domagala, J. & Hupe, D. (1996) The in vitro ejection of zinc from human immunodeficiency virus (HIV) type I nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity. Proc. Natl. Acad. Sci. U.S.A. 93: 969-973.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 969-973
    • Tummino, P.J.1    Scholten, J.D.2    Harvey, P.J.3    Holler, T.P.4    Maloney, L.5    Gogliotti, R.6    Domagala, J.7    Hupe, D.8
  • 36
    • 9244222705 scopus 로고    scopus 로고
    • Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells
    • Tyagi, S. C., Kumar, S. C. & Borders, S. (1996) Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells. J. Cell. Biochem. 61: 139-151.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 139-151
    • Tyagi, S.C.1    Kumar, S.C.2    Borders, S.3
  • 37
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida, Y., Takio, K., Titani, K., Ihara, Y. & Tomonaga, M. (1991) The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 7: 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 38
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L. & Auld, D. S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29: 5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 39
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L. & Falchuk, K. H. (1993) The biochemical basis of zinc physiology. Physiol. Rev. 73: 79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 40
    • 0029060897 scopus 로고
    • The function of metallothionein
    • Vallee, B. L. (1995) The function of metallothionein. Neurochem. Int. 27: 23-33.
    • (1995) Neurochem. Int. , vol.27 , pp. 23-33
    • Vallee, B.L.1
  • 41
    • 0001677003 scopus 로고
    • Metallothioneins
    • King, R. B., ed., Wiley, New York
    • Vašák, M. & Kägi, J.H.R. (1994) Metallothioneins. In: Encyclopedia of Inorganic Chemistry, vol. 4 (King, R. B., ed.), pp. 2229-2241. Wiley, New York.
    • (1994) Encyclopedia of Inorganic Chemistry , vol.4 , pp. 2229-2241
    • Vašák, M.1    Kägi, J.H.R.2
  • 42
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Washington, DC
    • Zheng, M., Åslund, F. & Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science (Washington, DC) 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Åslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.