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Volumn 54, Issue 40, 2015, Pages 6284-6293

Kinetics of Zinc and Cadmium Exchanges between Metallothionein and Carbonic Anhydrase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINS; CADMIUM; CARBONIC ANHYDRASE; ELECTRODEPOSITION; ELECTROSPRAY IONIZATION; ENZYMES; MAMMALS; MASS SPECTROMETRY; METAL IONS; PROTEINS; ZINC;

EID: 84944226333     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00912     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 33749641286 scopus 로고    scopus 로고
    • Metallothionein redox cycle and function
    • Kang, Y. J. (2006) Metallothionein redox cycle and function Exp. Biol. Med. 231, 1459-1467
    • (2006) Exp. Biol. Med. , vol.231 , pp. 1459-1467
    • Kang, Y.J.1
  • 2
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret, W. and Vallee, B. L. (1998) Thiolate ligands in metallothionein confer redox activity on zinc clusters Proc. Natl. Acad. Sci. U. S. A. 95, 3478-3482 10.1073/pnas.95.7.3478
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 3
    • 78349307650 scopus 로고    scopus 로고
    • Role of metallothionein in cadmium traffic and toxicity in kidneys and other mammalian organs
    • Sabolić, I., Breljak, D., Škarica, M., and Herak-Kramberger, C. M. (2010) Role of metallothionein in cadmium traffic and toxicity in kidneys and other mammalian organs BioMetals 23, 897-926 10.1007/s10534-010-9351-z
    • (2010) BioMetals , vol.23 , pp. 897-926
    • Sabolić, I.1    Breljak, D.2    Škarica, M.3    Herak-Kramberger, C.M.4
  • 4
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: a link between cellular zinc and redox state
    • Maret, W. (2000) The function of zinc metallothionein: a link between cellular zinc and redox state J. Nutr. 130, 1455S-1458S
    • (2000) J. Nutr. , vol.130 , pp. 1455S-1458S
    • Maret, W.1
  • 5
    • 0026454919 scopus 로고
    • Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2
    • Braun, W., Vasak, M., Robbins, A., Stout, C., Wagner, G., Kägi, J., and Wüthrich, K. (1992) Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2 Proc. Natl. Acad. Sci. U. S. A. 89, 10124-10128 10.1073/pnas.89.21.10124
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10124-10128
    • Braun, W.1    Vasak, M.2    Robbins, A.3    Stout, C.4    Wagner, G.5    Kägi, J.6    Wüthrich, K.7
  • 6
    • 0021829810 scopus 로고
    • Distinct metal-binding configurations in metallothionein
    • Nielson, K. B., Atkin, C., and Winge, D. (1985) Distinct metal-binding configurations in metallothionein J. Biol. Chem. 260, 5342-5350
    • (1985) J. Biol. Chem. , vol.260 , pp. 5342-5350
    • Nielson, K.B.1    Atkin, C.2    Winge, D.3
  • 7
    • 0022397076 scopus 로고
    • Products of metal exchange reactions of metallothionein
    • Nettesheim, D. G., Engeseth, H. R., and Otvos, J. D. (1985) Products of metal exchange reactions of metallothionein Biochemistry 24, 6744-6751 10.1021/bi00345a003
    • (1985) Biochemistry , vol.24 , pp. 6744-6751
    • Nettesheim, D.G.1    Engeseth, H.R.2    Otvos, J.D.3
  • 8
    • 0023518497 scopus 로고
    • Cadmium uptake and toxicity via voltage-sensitive calcium channels
    • Hinkle, P. M., Kinsella, P., and Osterhoudt, K. (1987) Cadmium uptake and toxicity via voltage-sensitive calcium channels J. Biol. Chem. 262, 16333-16337
    • (1987) J. Biol. Chem. , vol.262 , pp. 16333-16337
    • Hinkle, P.M.1    Kinsella, P.2    Osterhoudt, K.3
  • 9
    • 0025151079 scopus 로고
    • Metallothionein and other cadmium-binding proteins: recent developments
    • Waalkes, M. P. and Goering, P. L. (1990) Metallothionein and other cadmium-binding proteins: recent developments Chem. Res. Toxicol. 3, 281-288 10.1021/tx00016a001
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 281-288
    • Waalkes, M.P.1    Goering, P.L.2
  • 10
    • 33751002324 scopus 로고    scopus 로고
    • Cadmium: Cellular effects, modifications of biomolecules, modulation of DNA repair and genotoxic consequences (a review)
    • Bertin, G. and Averbeck, D. (2006) Cadmium: Cellular effects, modifications of biomolecules, modulation of DNA repair and genotoxic consequences (a review) Biochimie 88, 1549-1559 10.1016/j.biochi.2006.10.001
    • (2006) Biochimie , vol.88 , pp. 1549-1559
    • Bertin, G.1    Averbeck, D.2
  • 11
    • 0035283151 scopus 로고    scopus 로고
    • The transcription factors MTF-1 and USF1 cooperate to regulate mouse metallothionein-I expression in response to the essential metal zinc in visceral endoderm cells during early development
    • Andrews, G. K., Lee, D. K., Ravindra, R., Lichtlen, P., Sirito, M., Sawadogo, M., and Schaffner, W. (2001) The transcription factors MTF-1 and USF1 cooperate to regulate mouse metallothionein-I expression in response to the essential metal zinc in visceral endoderm cells during early development EMBO J. 20, 1114-1122 10.1093/emboj/20.5.1114
    • (2001) EMBO J. , vol.20 , pp. 1114-1122
    • Andrews, G.K.1    Lee, D.K.2    Ravindra, R.3    Lichtlen, P.4    Sirito, M.5    Sawadogo, M.6    Schaffner, W.7
  • 12
    • 0034602175 scopus 로고    scopus 로고
    • The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene
    • Langmade, S. J., Ravindra, R., Daniels, P. J., and Andrews, G. K. (2000) The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene J. Biol. Chem. 275, 34803-34809 10.1074/jbc.M007339200
    • (2000) J. Biol. Chem. , vol.275 , pp. 34803-34809
    • Langmade, S.J.1    Ravindra, R.2    Daniels, P.J.3    Andrews, G.K.4
  • 13
    • 0019483405 scopus 로고
    • Transcriptional regulation of the mouse metallothionein-I gene by heavy metals
    • Durnam, D. and Palmiter, R. (1981) Transcriptional regulation of the mouse metallothionein-I gene by heavy metals J. Biol. Chem. 256, 5712-5716
    • (1981) J. Biol. Chem. , vol.256 , pp. 5712-5716
    • Durnam, D.1    Palmiter, R.2
  • 14
    • 0020328232 scopus 로고
    • The mouse metallothionein-I gene is transcriptionally regulated by cadmium following transfection into human or mouse cells
    • Mayo, K. E., Warren, R., and Palmiter, R. D. (1982) The mouse metallothionein-I gene is transcriptionally regulated by cadmium following transfection into human or mouse cells Cell 29, 99-108 10.1016/0092-8674(82)90094-0
    • (1982) Cell , vol.29 , pp. 99-108
    • Mayo, K.E.1    Warren, R.2    Palmiter, R.D.3
  • 15
    • 0017336408 scopus 로고
    • Control of zinc-thionein synthesis in rat liver
    • Squibb, K. S., Cousins, R. J., and Feldman, S. L. (1977) Control of zinc-thionein synthesis in rat liver Biochem. J. 164, 223-228 10.1042/bj1640223
    • (1977) Biochem. J. , vol.164 , pp. 223-228
    • Squibb, K.S.1    Cousins, R.J.2    Feldman, S.L.3
  • 17
    • 77955435917 scopus 로고    scopus 로고
    • Mechanism of cadmium ion substitution in mammalian zinc metallothionein and metallothionein α domain: kinetic and structural studies
    • Ejnik, J., Shaw, C. F., III, and Petering, D. H. (2010) Mechanism of cadmium ion substitution in mammalian zinc metallothionein and metallothionein α domain: kinetic and structural studies Inorg. Chem. 49, 6525-6534 10.1021/ic1003148
    • (2010) Inorg. Chem. , vol.49 , pp. 6525-6534
    • Ejnik, J.1    Shaw, C.F.2    Petering, D.H.3
  • 19
    • 0034712970 scopus 로고    scopus 로고
    • A biological function for cadmium in marine diatoms
    • Lane, T. W. and Morel, F. M. M. (2000) A biological function for cadmium in marine diatoms Proc. Natl. Acad. Sci. U. S. A. 97, 4627-4631 10.1073/pnas.090091397
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4627-4631
    • Lane, T.W.1    Morel, F.M.M.2
  • 20
    • 40449131050 scopus 로고    scopus 로고
    • Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms
    • Xu, Y., Feng, L., Jeffrey, P. D., Shi, Y., and Morel, F. M. M. (2008) Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms Nature 452, 56-61 10.1038/nature06636
    • (2008) Nature , vol.452 , pp. 56-61
    • Xu, Y.1    Feng, L.2    Jeffrey, P.D.3    Shi, Y.4    Morel, F.M.M.5
  • 22
    • 36148941729 scopus 로고    scopus 로고
    • Characterization of the conformational changes in recombinant human metallothioneins using ESI-MS and molecular modeling
    • Chan, J., Huang, Z., Watt, I., Kille, P., and Stillman, M. J. (2007) Characterization of the conformational changes in recombinant human metallothioneins using ESI-MS and molecular modeling Can. J. Chem. 85, 898-912 10.1139/v07-111
    • (2007) Can. J. Chem. , vol.85 , pp. 898-912
    • Chan, J.1    Huang, Z.2    Watt, I.3    Kille, P.4    Stillman, M.J.5
  • 23
    • 0014217388 scopus 로고
    • Mechanism of action of carbonic anhydrase: Substrate, sulfonamide, and anion binding
    • Coleman, J. E. (1967) Mechanism of action of carbonic anhydrase: Substrate, sulfonamide, and anion binding J. Biol. Chem. 242, 5212-5219
    • (1967) J. Biol. Chem. , vol.242 , pp. 5212-5219
    • Coleman, J.E.1
  • 24
    • 0014217558 scopus 로고
    • Combination of bovine carbonic anhydrase with a fluorescent sulfonamide
    • Chen, R. F. and Kernohan, J. C. (1967) Combination of bovine carbonic anhydrase with a fluorescent sulfonamide J. Biol. Chem. 242, 5813-5823
    • (1967) J. Biol. Chem. , vol.242 , pp. 5813-5823
    • Chen, R.F.1    Kernohan, J.C.2
  • 25
    • 84907856282 scopus 로고    scopus 로고
    • The zinc balance: Competitive zinc metalation of carbonic anhydrase and metallothionein 1A
    • Pinter, T. B. J. and Stillman, M. J. (2014) The zinc balance: Competitive zinc metalation of carbonic anhydrase and metallothionein 1A Biochemistry 53, 6276-6285 10.1021/bi5008673
    • (2014) Biochemistry , vol.53 , pp. 6276-6285
    • Pinter, T.B.J.1    Stillman, M.J.2
  • 26
    • 34548283175 scopus 로고    scopus 로고
    • Use of stable isotopically enriched proteins and directly coupled high-performance liquid chromatography inductively coupled plasma mass spectrometry for quantitatively monitoring the transfer of metals between proteins
    • Mason, A. Z., Moeller, R., Thrippleton, K. A., and Lloyd, D. (2007) Use of stable isotopically enriched proteins and directly coupled high-performance liquid chromatography inductively coupled plasma mass spectrometry for quantitatively monitoring the transfer of metals between proteins Anal. Biochem. 369, 87-104 10.1016/j.ab.2007.06.015
    • (2007) Anal. Biochem. , vol.369 , pp. 87-104
    • Mason, A.Z.1    Moeller, R.2    Thrippleton, K.A.3    Lloyd, D.4
  • 27
    • 0031766835 scopus 로고    scopus 로고
    • Monitoring metal ion flux in reactions of metallothionein and drug-modified metallothionein by electrospray mass spectrometry
    • Zaia, J., Fabris, D., Wei, D., Karpel, R. L., and Fenselau, C. (1998) Monitoring metal ion flux in reactions of metallothionein and drug-modified metallothionein by electrospray mass spectrometry Protein Sci. 7, 2398-2404 10.1002/pro.5560071117
    • (1998) Protein Sci. , vol.7 , pp. 2398-2404
    • Zaia, J.1    Fabris, D.2    Wei, D.3    Karpel, R.L.4    Fenselau, C.5
  • 28
    • 84899553443 scopus 로고    scopus 로고
    • The role of metallothionein interactions with other proteins
    • Zalewska, M., Trefon, J., and Milnerowicz, H. (2014) The role of metallothionein interactions with other proteins Proteomics 14, 1343-1356 10.1002/pmic.201300496
    • (2014) Proteomics , vol.14 , pp. 1343-1356
    • Zalewska, M.1    Trefon, J.2    Milnerowicz, H.3
  • 29
    • 0032504163 scopus 로고    scopus 로고
    • Modulation of DNA binding of a tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair
    • Roesijadi, G., Bogumil, R., Vasák, M., and Kägi, J. H. (1998) Modulation of DNA binding of a tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair J. Biol. Chem. 273, 17425-17432 10.1074/jbc.273.28.17425
    • (1998) J. Biol. Chem. , vol.273 , pp. 17425-17432
    • Roesijadi, G.1    Bogumil, R.2    Vasák, M.3    Kägi, J.H.4
  • 30
    • 2442721444 scopus 로고    scopus 로고
    • Interprotein metal ion exchange between cadmium-carbonic anhydrase and apo-or zinc-metallothionein
    • Ejnik, J., Muñoz, A., Gan, T., Shaw, C. F., III, and Petering, D. (1999) Interprotein metal ion exchange between cadmium-carbonic anhydrase and apo-or zinc-metallothionein J. Biol. Inorg. Chem. 4, 784-790 10.1007/s007750050351
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 784-790
    • Ejnik, J.1    Muñoz, A.2    Gan, T.3    Shaw, C.F.4    Petering, D.5
  • 31
    • 34848847551 scopus 로고    scopus 로고
    • Dual nanomolar and picomolar Zn (II) binding properties of metallothionein
    • Kręzel, A. and Maret, W. (2007) Dual nanomolar and picomolar Zn (II) binding properties of metallothionein J. Am. Chem. Soc. 129, 10911-10921 10.1021/ja071979s
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10911-10921
    • Kręzel, A.1    Maret, W.2
  • 33
    • 0000750473 scopus 로고
    • Metal-binding properties of human erythrocyte carbonic anhydrases
    • Lindskog, S. and Nyman, P. O. (1964) Metal-binding properties of human erythrocyte carbonic anhydrases Biochim. Biophys. Acta, Spec. Sect. Enzymol. Subj. 85, 462-474 10.1016/0926-6569(64)90310-4
    • (1964) Biochim. Biophys. Acta, Spec. Sect. Enzymol. Subj. , vol.85 , pp. 462-474
    • Lindskog, S.1    Nyman, P.O.2
  • 34
    • 0027495961 scopus 로고
    • Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II
    • Kiefer, L. L., Krebs, J. F., Paterno, S. A., and Fierke, C. A. (1993) Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II Biochemistry 32, 9896-9900 10.1021/bi00089a004
    • (1993) Biochemistry , vol.32 , pp. 9896-9900
    • Kiefer, L.L.1    Krebs, J.F.2    Paterno, S.A.3    Fierke, C.A.4
  • 35
    • 0017413628 scopus 로고
    • Coordination chemical studies on metalloenzymes II. Kinetic behavior of various types of chelating agents towards bovine carbonic anhydrase
    • Kidani, Y. and Hirose, J. (1977) Coordination chemical studies on metalloenzymes II. Kinetic behavior of various types of chelating agents towards bovine carbonic anhydrase J. Biochem. (Tokyo) 81, 1383-1391
    • (1977) J. Biochem. (Tokyo) , vol.81 , pp. 1383-1391
    • Kidani, Y.1    Hirose, J.2
  • 36
    • 0013836276 scopus 로고
    • Human carbonic anhydrase. Protein conformation and metal ion binding
    • Coleman, J. E. (1965) Human carbonic anhydrase. Protein conformation and metal ion binding Biochemistry 4, 2644-2655 10.1021/bi00888a014
    • (1965) Biochemistry , vol.4 , pp. 2644-2655
    • Coleman, J.E.1
  • 37
    • 84907856282 scopus 로고    scopus 로고
    • The zinc balance: Competitive zinc metalation of carbonic anhydrase and metallothionein 1A
    • Pinter, T. B. and Stillman, M. J. (2014) The zinc balance: Competitive zinc metalation of carbonic anhydrase and metallothionein 1A Biochemistry 53, 6276-6285 10.1021/bi5008673
    • (2014) Biochemistry , vol.53 , pp. 6276-6285
    • Pinter, T.B.1    Stillman, M.J.2
  • 38
    • 2942516407 scopus 로고    scopus 로고
    • Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein
    • Mason, A. Z., Perico, N., Moeller, R., Thrippleton, K., Potter, T., and Lloyd, D. (2004) Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein Mar. Environ. Res. 58, 371-375 10.1016/j.marenvres.2004.03.082
    • (2004) Mar. Environ. Res. , vol.58 , pp. 371-375
    • Mason, A.Z.1    Perico, N.2    Moeller, R.3    Thrippleton, K.4    Potter, T.5    Lloyd, D.6
  • 39
    • 84920837145 scopus 로고    scopus 로고
    • Metalation kinetics of the human α-metallothionein 1a fragment is dependent on the fluxional structure of the apo-protein
    • Irvine, G. W., Duncan, K. E., Gullons, M., and Stillman, M. J. (2015) Metalation kinetics of the human α-metallothionein 1a fragment is dependent on the fluxional structure of the apo-protein Chem.-Eur. J. 21, 1269-1279 10.1002/chem.201404283
    • (2015) Chem. - Eur. J. , vol.21 , pp. 1269-1279
    • Irvine, G.W.1    Duncan, K.E.2    Gullons, M.3    Stillman, M.J.4
  • 40
    • 0019085620 scopus 로고
    • Ligand substitution reactions of metallothioneins with EDTA and apo-carbonic anhydrase
    • Li, T.-Y., Kraker, A. J., Shaw, C. F., and Petering, D. H. (1980) Ligand substitution reactions of metallothioneins with EDTA and apo-carbonic anhydrase Proc. Natl. Acad. Sci. U. S. A. 77, 6334-6338 10.1073/pnas.77.11.6334
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6334-6338
    • Li, T.-Y.1    Kraker, A.J.2    Shaw, C.F.3    Petering, D.H.4
  • 41
    • 0024218271 scopus 로고
    • Refined structure of human carbonic anhydrase II at 2.0 Å resolution
    • Eriksson, A. E., Jones, T. A., and Liljas, A. (1988) Refined structure of human carbonic anhydrase II at 2.0 Å resolution Proteins: Struct., Funct., Genet. 4, 274-282 10.1002/prot.340040406
    • (1988) Proteins: Struct., Funct., Genet. , vol.4 , pp. 274-282
    • Eriksson, A.E.1    Jones, T.A.2    Liljas, A.3


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