메뉴 건너뛰기




Volumn 48, Issue 24, 2009, Pages 5700-5707

Effects of Zn2+, Ca2+, and Mg2+ on the structure of Zn7metallothionein-3: Evidence for an additional zinc binding site

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; BINDING CONSTANT; BINDING LIGANDS; ESSENTIAL METALS; FLEXIBLE HINGES; GEL FILTRATION; METAL-THIOLATE; METALLOPROTEIN; METALLOTHIONEIN-3; METALLOTHIONEINS; PROTEIN DIMERIZATION; PROTEIN DOMAINS; SPECTROMETRIC TECHNIQUES; SPECTROSCOPIC FEATURES; STOKES RADIUS; TIME-DEPENDENT; ZINC-BINDING SITES;

EID: 67649227284     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900366p     Document Type: Article
Times cited : (31)

References (31)
  • 1
    • 0033674209 scopus 로고    scopus 로고
    • Movement of zinc and its functional significance in the brain
    • Takeda, A. (2000) Movement of zinc and its functional significance in the brain. Brain Res. Brain Res. Rev. 34, 137-148.
    • (2000) Brain Res. Brain Res. Rev. , vol.34 , pp. 137-148
    • Takeda, A.1
  • 2
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and 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
  • 3
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson, C. J. (1989) Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol. 31, 145-238.
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 4
  • 5
    • 3242741010 scopus 로고    scopus 로고
    • Mammalian zinc transporters
    • Liuzzi, J. P., and Cousins, R. J. (2004) Mammalian zinc transporters. Annu. Rev. Nutr. 24, 151-172.
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 151-172
    • Liuzzi, J.P.1    Cousins, R.J.2
  • 6
    • 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., and 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
  • 7
    • 0037200013 scopus 로고    scopus 로고
    • Growth inhibitory factor prevents neurite extension and death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging
    • Uchida, Y., Gomi, F., Masumizu, T., and Miura, Y. (2002) Growth inhibitory factor prevents neurite extension and death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging. J. Biol. Chem. 277, 32353-32359.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32353-32359
    • Uchida, Y.1    Gomi, F.2    Masumizu, T.3    Miura, Y.4
  • 8
    • 0028932454 scopus 로고
    • Bioactivity of metallothionein-3 correlates with its novel β domain sequence rather than metal binding properties
    • Sewell, A. K., Jensen, L. T., Erickson, J. C., Palmiter, R. D., and Winge, D. R. (1995) Bioactivity of metallothionein-3 correlates with its novel β domain sequence rather than metal binding properties. Biochemistry 34, 4740-4747.
    • (1995) Biochemistry , vol.34 , pp. 4740-4747
    • Sewell, A.K.1    Jensen, L.T.2    Erickson, J.C.3    Palmiter, R.D.4    Winge, D.R.5
  • 9
    • 0034811882 scopus 로고    scopus 로고
    • Metallothionein-III antagonizes the neurotoxic and neurotrophic effects of amyloid β peptides
    • Irie, Y., and Keung, W. M. (2001) Metallothionein-III antagonizes the neurotoxic and neurotrophic effects of amyloid β peptides. Biochem. Biophys. Res. Commun. 282, 416-420.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 416-420
    • Irie, Y.1    Keung, W.M.2
  • 11
    • 0033977114 scopus 로고    scopus 로고
    • Seizures and neuronal damage in mice lacking vesicular zinc
    • DOI 10.1016/S0920-1211(99)00121-7, PII S0920121199001217
    • Cole, T. B., Robbins, C. A., Wenzel, H. J., Schwartzkroin, P. A., and Palmiter, R. D. (2000) Seizures and neuronal damage in mice lacking vesicular zinc. Epilepsy Res. 39, 153-169. (Pubitemid 30089587)
    • (2000) Epilepsy Research , vol.39 , Issue.2 , pp. 153-169
    • Cole, T.B.1    Robbins, C.A.2    Wenzel, H.J.3    Schwartzkroin, P.A.4    Palmiter, R.D.5
  • 13
    • 22244464935 scopus 로고    scopus 로고
    • Growth inhibitory factor (GIF) directly interacts with G-protein Rab3a
    • Kang, Q. H., Chen, Q. L., Ren, H. W., and Ru, B. G. (2001) Growth inhibitory factor (GIF) directly interacts with G-protein Rab3a. Prog. Biochem. Biophys. 28, 880-884.
    • (2001) Prog. Biochem. Biophys. , vol.28 , pp. 880-884
    • Kang, Q.H.1    Chen, Q.L.2    Ren, H.W.3    Ru, B.G.4
  • 14
    • 14644397252 scopus 로고    scopus 로고
    • 7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A
    • DOI 10.1021/bi047636d
    • Knipp, M., Meloni, G., Roschitzki, B., and Vašák, M. (2005) Zn7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A. Biochemistry 44, 3159-3165. (Pubitemid 40321988)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3159-3165
    • Knipp, M.1    Meloni, G.2    Roschitzki, B.3    Vasak, M.4
  • 15
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • 2+ from brain tissue during activity. Nature 308, 734-736.
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 16
    • 0033520117 scopus 로고    scopus 로고
    • Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters
    • Faller, P., Hasler, D. W., Zerbe, O., Klauser, S., Winge, D. R., and Vašák, M. (1999) Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters. Biochemistry 38, 10158-10167. (Pubitemid 129515353)
    • (1999) Biochemistry , vol.38 , Issue.31 , pp. 10158-10167
    • Faller, P.1    Hasler, D.W.2    Zerbe, O.3    Klauser, S.4    Winge, D.R.5    Vasak, M.6
  • 17
    • 0035949634 scopus 로고    scopus 로고
    • Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3
    • DOI 10.1021/bi010827l
    • Oz, G., Zangger, K., and Armitage, I. M. (2001) Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3. Biochemistry 40, 11433-11441. (Pubitemid 32911286)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11433-11441
    • Oz, G.1    Zangger, K.2    Armitage, I.M.3
  • 18
    • 31444449685 scopus 로고    scopus 로고
    • Solution structure and dynamics of human metallothionein-3 (MT-3)
    • DOI 10.1016/j.febslet.2005.12.099, PII S0014579306000135
    • Wang, H., Zhang, Q., Cai, B., Li, H., Sze, K. H., Huang, Z. X., Wu, H. M., and Sun, H. (2006) Solution structure and dynamics of human metallothionein-3 (MT-3). FEBS Lett. 580, 795-800. (Pubitemid 43152298)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 795-800
    • Wang, H.1    Zhang, Q.2    Cai, B.3    Li, H.4    Sze, K.-H.5    Huang, Z.-X.6    Wu, H.-M.7    Sun, H.8
  • 19
    • 0037076545 scopus 로고    scopus 로고
    • Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively
    • DOI 10.1021/bi025664v
    • Palumaa, P., Eriste, E., Njunkova, O., Pokras, L., Jornvall, H., and Sillard, R. (2002) Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Biochemistry 41, 6158-6163. (Pubitemid 34498922)
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 6158-6163
    • Palumaa, P.1    Eriste, E.2    Njunkova, O.3    Pokras, L.4    Jornvall, H.5    Sillard, R.6
  • 20
    • 0026318278 scopus 로고
    • Metal removal and substitution in vertebrate and invertebrate metallothioneins
    • Vašák, M. (1991) Metal removal and substitution in vertebrate and invertebrate metallothioneins. Methods Enzymol. 205, 452-458.
    • (1991) Methods Enzymol. , vol.205 , pp. 452-458
    • Vašák, M.1
  • 21
    • 22544466415 scopus 로고    scopus 로고
    • Detection of neuronal growth inhibitory factor (metallothionein-3) in polyacrylamide gels and by Western blot analysis
    • Meloni, G., Knipp, M., and Vašák, M. (2005) Detection of neuronal growth inhibitory factor (metallothionein-3) in polyacrylamide gels and by Western blot analysis. J. Biochem. Biophys. Methods 64, 76-81.
    • (2005) J. Biochem. Biophys. Methods , vol.64 , pp. 76-81
    • Meloni, G.1    Knipp, M.2    Vašák, M.3
  • 22
    • 0019018003 scopus 로고
    • Reactivity of the thiol group in human and bovine albumin at pH 3-9, as measured by exchange with 2,2′-dithiodipyridine
    • Pedersen, A. O., and Jacobsen, J. (1980) Reactivity of the thiol group in human and bovine albumin at pH 3-9, as measured by exchange with 2,2′-dithiodipyridine. Eur. J. Biochem. 106, 291-295.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 291-295
    • Pedersen, A.O.1    Jacobsen, J.2
  • 23
    • 39749187675 scopus 로고
    • Theory of gel filtration and its experimental verification
    • Laurent, T. C., and Killander, J. (1964) Theory of gel filtration and its experimental verification. J. Chromatogr. 14, 317-330.
    • (1964) J. Chromatogr. , vol.14 , pp. 317-330
    • Laurent, T.C.1    Killander, J.2
  • 24
    • 0026647117 scopus 로고
    • Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy
    • Messerle, B. A., Schaffer, A., Vašák, M., Kagi, J. H., and Wuthrich, K. (1992) Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. J. Mol. Biol. 225, 433-443.
    • (1992) J. Mol. Biol. , vol.225 , pp. 433-443
    • Messerle, B.A.1    Schaffer, A.2    Vašák, M.3    Kagi, J.H.4    Wuthrich, K.5
  • 25
    • 0037058903 scopus 로고    scopus 로고
    • Recent developments in the electronic spectroscopy of amides and R-helical polypeptides
    • Woody, R. W., and Koslowski, A. (2002) Recent developments in the electronic spectroscopy of amides and R-helical polypeptides. Biophys. Chem. 101-102, 535-551.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 535-551
    • Woody, R.W.1    Koslowski, A.2
  • 26
    • 0021760922 scopus 로고
    • Dynamic structure of metallothionein
    • Vašák, M., Berger, C., and Kagi, J. H. (1984) Dynamic structure of metallothionein. FEBS Lett. 168, 174-178.
    • (1984) FEBS Lett. , vol.168 , pp. 174-178
    • Vašák, M.1    Berger, C.2    Kagi, J.H.3
  • 27
    • 0032216842 scopus 로고    scopus 로고
    • 113Cd NMR to metallothioneins
    • 113Cd NMR to metallothioneins. Biodegradation 9, 501-512.
    • (1998) Biodegradation , vol.9 , pp. 501-512
    • Vašák, M.1
  • 28
    • 0032468144 scopus 로고    scopus 로고
    • NMR spectroscopic studies of I = 1/2 metal ions in biological systems
    • Oz, G., Pountney, D. L., and Armitage, I. M. (1998) NMR spectroscopic studies of I = 1/2 metal ions in biological systems. Biochem. Cell Biol. 76, 223-234.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 223-234
    • Oz, G.1    Pountney, D.L.2    Armitage, I.M.3
  • 30
    • 0032888705 scopus 로고    scopus 로고
    • Correlated measurements of free and total intracellular calcium concentration in central nervous system neurons
    • Pozzo-Miller, L. D., Pivovarova, N. B., Connor, J. A., Reese, T. S., and Andrews, S. B. (1999) Correlated measurements of free and total intracellular calcium concentration in central nervous system neurons. Microsc. Res. Tech. 46, 370-379.
    • (1999) Microsc. Res. Tech. , vol.46 , pp. 370-379
    • Pozzo-Miller, L.D.1    Pivovarova, N.B.2    Connor, J.A.3    Reese, T.S.4    Andrews, S.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.