메뉴 건너뛰기




Volumn 287, Issue 12, 2012, Pages 9322-9326

Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase β activity

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS; CATALYTIC DOMAINS; CELLULAR SIGNALING; ION CONCENTRATIONS; KEY ENZYMES; KINETIC ANALYSIS; METALLOENZYMES; ORDERS OF MAGNITUDE; PROTEIN-TYROSINE PHOSPHATASE; SMALL MOLECULE INHIBITOR; ZINC BINDING; ZINC IONS;

EID: 84863393278     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C111.320796     Document Type: Article
Times cited : (139)

References (47)
  • 1
    • 0032877635 scopus 로고    scopus 로고
    • Cell signaling by protein tyrosine phosphorylation
    • Fischer, E. H. (1999) Cell signaling by protein tyrosine phosphorylation. Adv. Enzyme Regul. 39, 359-369
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 359-369
    • Fischer, E.H.1
  • 3
    • 77955279589 scopus 로고    scopus 로고
    • PTP1B: A double agent in metabolism and oncogenesis
    • Yip, S. C., Saha, S., and Chernoff, J. (2010) PTP1B: a double agent in metabolism and oncogenesis. Trends Biochem. Sci. 35, 442-449
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 442-449
    • Yip, S.C.1    Saha, S.2    Chernoff, J.3
  • 4
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • DOI 10.1038/nature01680
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K., and Barford, D. (2003) Redox regulation of protein-tyrosine phosphatase 1B involves a sulfenyl amide intermediate. Nature 423, 769-773 (Pubitemid 36735701)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.-C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 5
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • DOI 10.1038/nature01681
    • van Montfort, R. L., Congreve, M., Tisi, D., Carr, R., and Jhoti, H. (2003) Oxidation state of the active-site cysteine in protein-tyrosine phosphatase 1B. Nature 423, 773-777 (Pubitemid 36735702)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 6
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2 domain-containing protein-tyrosine phosphatases by two backdoor cysteines
    • Chen, C. Y., Willard, D., and Rudolph, J. (2009) Redox regulation of SH2 domain-containing protein-tyrosine phosphatases by two backdoor cysteines. Biochemistry 48, 1399-1409
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 7
    • 66649131057 scopus 로고    scopus 로고
    • Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: Insights into redox regulation
    • Tsai, S. J., Sen, U., Zhao, L., Greenleaf, W. B., Dasgupta, J., Fiorillo, E., Orrú, V., Bottini, N., and Chen, X. S. (2009) Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: insights into redox regulation. Biochemistry 48, 4838-4845
    • (2009) Biochemistry , vol.48 , pp. 4838-4845
    • Tsai, S.J.1    Sen, U.2    Zhao, L.3    Greenleaf, W.B.4    Dasgupta, J.5    Fiorillo, E.6    Orrú, V.7    Bottini, N.8    Chen, X.S.9
  • 8
    • 77952399363 scopus 로고    scopus 로고
    • Insights into the reaction of protein-tyrosine phosphatase 1B: Crystal structures for transition state analogs of both catalytic steps
    • Brandão, T. A., Hengge, A. C., and Johnson, S. J. (2010) Insights into the reaction of protein-tyrosine phosphatase 1B: crystal structures for transition state analogs of both catalytic steps. J. Biol. Chem. 285, 15874-15883
    • (2010) J. Biol. Chem. , vol.285 , pp. 15874-15883
    • Brandão, T.A.1    Hengge, A.C.2    Johnson, S.J.3
  • 9
    • 0019877124 scopus 로고
    • Phosphotyrosyl-protein phosphatase: Specific inhibition by Zn
    • Brautigan, D. L., Bornstein, P., and Gallis, B. (1981) Phosphotyrosyl-protein phosphatase: specific inhibition by Zn. J. Biol. Chem. 256, 6519-6522
    • (1981) J. Biol. Chem. , vol.256 , pp. 6519-6522
    • Brautigan, D.L.1    Bornstein, P.2    Gallis, B.3
  • 10
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • DOI 10.1007/s00775-006-0150-5
    • Krezel, A., and Maret, W. (2006) Zinc-buffering capacity of a eukaryotic cell at physiological pZn. J. Biol. Inorg. Chem. 11, 1049-1062 (Pubitemid 44786393)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.8 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 11
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym, R. A., Thompson, R. B., Stoddard, A. K., and Fierke, C. A. (2006) Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor. ACS Chem. Biol. 1, 103-111
    • (2006) ACS Chem. Biol. , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 13
    • 67649229609 scopus 로고    scopus 로고
    • Transient fluctuations of intracellular zinc ions in cell proliferation
    • Li, Y., and Maret, W. (2009) Transient fluctuations of intracellular zinc ions in cell proliferation. Exp. Cell Res. 315, 2463-2470
    • (2009) Exp. Cell Res. , vol.315 , pp. 2463-2470
    • Li, Y.1    Maret, W.2
  • 15
    • 52949092707 scopus 로고    scopus 로고
    • Selective inhibition of mitogen-activated protein kinase phosphatases by zinc accounts for extracellular signal-regulated kinase 1/2-dependent oxidative neuronal cell death
    • Ho, Y., Samarasinghe, R., Knoch, M. E., Lewis, M., Aizenman, E., and DeFranco, D. B. (2008) Selective inhibition of mitogen-activated protein kinase phosphatases by zinc accounts for extracellular signal-regulated kinase 1/2-dependent oxidative neuronal cell death. Mol. Pharmacol. 74, 1141-1151
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1141-1151
    • Ho, Y.1    Samarasinghe, R.2    Knoch, M.E.3    Lewis, M.4    Aizenman, E.5    DeFranco, D.B.6
  • 16
    • 77949536140 scopus 로고    scopus 로고
    • Toxicological disruption of signaling homeostasis: Tyrosine phosphatases as targets
    • Samet, J. M., and Tal, T. L. (2010) Toxicological disruption of signaling homeostasis: tyrosine phosphatases as targets. Annu. Rev. Pharmacol. Toxicol. 50, 215-235
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 215-235
    • Samet, J.M.1    Tal, T.L.2
  • 18
    • 0025781647 scopus 로고
    • Purification and characterization of a human recombinant T-cell protein-tyrosine phosphatase from a baculovirus expression system
    • Zander, N. F., Lorenzen, J. A., Cool, D. E., Tonks, N. K., Daum, G., Krebs, E. G., and Fischer, E. H. (1991) Purification and characterization of a human recombinant T-cell protein-tyrosine phosphatase from a baculovirus expression system. Biochemistry 30, 6964-6970
    • (1991) Biochemistry , vol.30 , pp. 6964-6970
    • Zander, N.F.1    Lorenzen, J.A.2    Cool, D.E.3    Tonks, N.K.4    Daum, G.5    Krebs, E.G.6    Fischer, E.H.7
  • 19
    • 0344010194 scopus 로고    scopus 로고
    • Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling
    • DOI 10.1016/S0014-4827(03)00406-3
    • Haase, H., and Maret, W. (2003) Intracellular zinc fluctuations modulate protein-tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Exp. Cell Res. 291, 289-298 (Pubitemid 37485719)
    • (2003) Experimental Cell Research , vol.291 , Issue.2 , pp. 289-298
    • Haase, H.1    Maret, W.2
  • 20
    • 40949108071 scopus 로고    scopus 로고
    • Thionein/metallothionein control Zn(II) availability and the activity of enzymes
    • Krezel, A., and Maret, W. (2008) Thionein/metallothionein control Zn(II) availability and the activity of enzymes. J. Biol. Inorg. Chem. 13, 401-409
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 401-409
    • Krezel, A.1    Maret, W.2
  • 21
    • 61849121844 scopus 로고    scopus 로고
    • Zinc transporters and cancer: A potential role for ZIP7 as a hub for tyrosine kinase activation
    • Hogstrand, C., Kille, P., Nicholson, R. I., and Taylor, K. M. (2009) Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation. Trends Mol. Med. 15, 101-111
    • (2009) Trends Mol. Med. , vol.15 , pp. 101-111
    • Hogstrand, C.1    Kille, P.2    Nicholson, R.I.3    Taylor, K.M.4
  • 22
    • 0019287147 scopus 로고
    • Insulin-like effect of zinc on adipocytes
    • Coulston, L., and Dandona, P. (1980) Insulin-like effect of zinc on adipocytes. Diabetes 29, 665-667 (Pubitemid 12201316)
    • (1980) Diabetes , vol.29 , Issue.8 , pp. 665-667
    • Coulston, L.1    Dandona, P.2
  • 23
    • 24744446561 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants
    • DOI 10.1007/s10534-005-3707-9
    • Haase, H., and Maret, W. (2005) Protein-tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants. BioMetals 18, 333-338 (Pubitemid 41298017)
    • (2005) BioMetals , vol.18 , Issue.4 , pp. 333-338
    • Haase, H.1    Maret, W.2
  • 24
    • 79952744484 scopus 로고    scopus 로고
    • Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory
    • Sindreu, C., Palmiter, R. D., and Storm, D. R. (2011) Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory. Proc. Natl. Acad. Sci. U.S.A. 108, 3366-3370
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3366-3370
    • Sindreu, C.1    Palmiter, R.D.2    Storm, D.R.3
  • 25
    • 0028273420 scopus 로고
    • Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase β (HPTPβ) using synthetic phosphopeptides
    • Harder, K. W., Owen, P., Wong, L. K., Aebersold, R., Clark-Lewis, I., and Jirik, F. R. (1994) Characterization and kinetic analysis of the intracellular domain of human protein-tyrosine phosphatase β (HPTPβ) using synthetic phosphopeptides. Biochem. J. 298, 395-401 (Pubitemid 24072483)
    • (1994) Biochemical Journal , vol.298 , Issue.2 , pp. 395-401
    • Harder, K.W.1    Owen, P.2    Wong, L.K.H.3    Aebersold, R.4    Clark-Lewis, I.5    Jirik, F.R.6
  • 28
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • DOI 10.1006/abio.1996.0171
    • Zor, T., and Selinger, Z. (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 236, 302-308 (Pubitemid 26136110)
    • (1996) Analytical Biochemistry , vol.236 , Issue.2 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 29
    • 0035068698 scopus 로고    scopus 로고
    • Coordination of heavy metals by dithiothreitol, a commonly used thiol group protectant
    • DOI 10.1016/S0162-0134(00)00212-9, PII S0162013400002129
    • Krezel, A., Lesniak, W., Jezowska-Bojczuk, M., Mlynarz, P., Brasuñ, J., Kozlowski, H., and Bal, W. (2001) Coordination of heavy metals by dithiothreitol, a commonly used thiol group protectant. J. Inorg. Biochem. 84, 77-88 (Pubitemid 32284915)
    • (2001) Journal of Inorganic Biochemistry , vol.84 , Issue.1-2 , pp. 77-88
    • Kreel, A.1    Leniak, W.2    Jeowska-Bojczuk, M.3    Mlynarz, P.4    Brasu, J.5    Kozlowski, H.6    Bal, W.7
  • 30
    • 0027464656 scopus 로고
    • Purification and characterization of a protein tyrosine phosphatase containing SH2 domains
    • Zhao, Z., Bouchard, P., Diltz, C. D., Shen, S. H., and Fischer, E. H. (1993) Purification and characterization of a protein-tyrosine phosphatase containing SH2 domains. J. Biol. Chem. 268, 2816-2820 (Pubitemid 23057914)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.4 , pp. 2816-2820
    • Zhao, Z.1    Bouchard, P.2    Diltz, C.D.3    Shen, S.-H.4    Fischer, E.H.5
  • 31
    • 0242600595 scopus 로고    scopus 로고
    • Coordination properties of tris(2-carboxyethyl)phosphine, a newly introduced thiol reductant, and its oxide
    • Krezel, A., Latajka, R., Bujacz, G. D., and Bal, W. (2003) Coordination properties of tris(2-carboxyethyl)phosphine, a newly introduced thiol reductant, and its oxide. Inorg. Chem. 42, 1994-2003
    • (2003) Inorg. Chem. , vol.42 , pp. 1994-2003
    • Krezel, A.1    Latajka, R.2    Bujacz, G.D.3    Bal, W.4
  • 32
    • 28244436461 scopus 로고    scopus 로고
    • Complexation equilibria of Zn(II), Pb(II), and Cd(II) with reduced glutathione (GSH) and biologically important zwitterionic buffers
    • Anwar, Z. M. (2005) Complexation equilibria of Zn(II), Pb(II), and Cd(II) with reduced glutathione (GSH) and biologically important zwitterionic buffers. J. Chin. Chem. Soc. 52, 863-871
    • (2005) J. Chin. Chem. Soc. , vol.52 , pp. 863-871
    • Anwar, Z.M.1
  • 33
    • 34848847551 scopus 로고    scopus 로고
    • Dual nanomolar and picomolar Zn(II) binding properties of metallothionein
    • DOI 10.1021/ja071979s
    • Krezel, A., and Maret, W. (2007) Dual nanomolar and picomolar Zn(II) binding properties of metallothionein. J. Am. Chem. Soc. 129, 10911-10921 (Pubitemid 350067501)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.35 , pp. 10911-10921
    • Krezel, A.1    Maret, W.2
  • 34
    • 1542794374 scopus 로고
    • Ligand-exchange kinetics and solution equilibria of cadmium, zinc, and lead nitrilotriacetate
    • Rabenstein, D. L., and Kula, R. J. (1969) Ligand-exchange kinetics and solution equilibria of cadmium, zinc, and lead nitrilotriacetate. J. Am. Chem. Soc. 91, 2492-2503
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 2492-2503
    • Rabenstein, D.L.1    Kula, R.J.2
  • 36
    • 52949135993 scopus 로고    scopus 로고
    • ZIP7-mediated intracellular zinc transport contributes to aberrant growth factor signaling in antihormone-resistant breast cancer Cells
    • Taylor, K. M., Vichova, P., Jordan, N., Hiscox, S., Hendley, R., and Nicholson, R. I. (2008) ZIP7-mediated intracellular zinc transport contributes to aberrant growth factor signaling in antihormone-resistant breast cancer Cells. Endocrinology 149, 4912-4920
    • (2008) Endocrinology , vol.149 , pp. 4912-4920
    • Taylor, K.M.1    Vichova, P.2    Jordan, N.3    Hiscox, S.4    Hendley, R.5    Nicholson, R.I.6
  • 37
    • 58749098604 scopus 로고    scopus 로고
    • Zinc signals are essential for lipopolysaccharide-induced signal transduction in monocytes
    • Haase, H., Ober-Blöbaum, J. L., Engelhardt, G., Hebel, S., Heit, A., Heine, H., and Rink, L. (2008) Zinc signals are essential for lipopolysaccharide-induced signal transduction in monocytes. J. Immunol. 181, 6491-6502
    • (2008) J. Immunol. , vol.181 , pp. 6491-6502
    • Haase, H.1    Ober-Blöbaum, J.L.2    Engelhardt, G.3    Hebel, S.4    Heit, A.5    Heine, H.6    Rink, L.7
  • 38
    • 0033592739 scopus 로고    scopus 로고
    • Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the Angiopoietin receptor Tie-2
    • DOI 10.1038/sj.onc.1202992
    • Fachinger, G., Deutsch, U., and Risau, W. (1999) Functional interaction of vascular endothelial protein-tyrosine phosphatase with the angiopoietin receptor Tie-2. Oncogene 18, 5948-5953 (Pubitemid 29520451)
    • (1999) Oncogene , vol.18 , Issue.43 , pp. 5948-5953
    • Fachinger, G.1    Deutsch, U.2    Risau, W.3
  • 39
    • 33745107561 scopus 로고    scopus 로고
    • Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development
    • DOI 10.1182/blood-2006-01-0141
    • Bäumer, S., Keller, L., Holtmann, A., Funke, R., August, B., Gamp, A., Wolburg, H., Wolburg-Buchholz, K., Deutsch, U., and Vestweber, D. (2006) Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development. Blood 107, 4754-4762 (Pubitemid 43882626)
    • (2006) Blood , vol.107 , Issue.12 , pp. 4754-4762
    • Baumer, S.1    Keller, L.2    Holtmann, A.3    Funke, R.4    August, B.5    Gamp, A.6    Wolburg, H.7    Wolburg-Buchholz, K.8    Deutsch, U.9    Vestweber, D.10
  • 41
    • 84856994470 scopus 로고    scopus 로고
    • Rink, L., ed . IOS Press, Amsterdam, The Netherlands
    • Jansen, J., and Rink, L. (2011) in Zinc in Human Health (Rink, L., ed) pp. 514-529, IOS Press, Amsterdam, The Netherlands
    • (2011) Zinc in Human Health , pp. 514-529
    • Jansen, J.1    Rink, L.2
  • 43
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons, T. J. (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.1
  • 44
    • 0021645190 scopus 로고
    • Zinc: What is its role in biology?
    • Williams, R. J. (1984) Zinc: what is its role in biology? Endeavour 8, 65-70
    • (1984) Endeavour , vol.8 , pp. 65-70
    • Williams, R.J.1
  • 45
    • 80755153625 scopus 로고    scopus 로고
    • Redox biochemistry of mammalian metallothioneins
    • Maret, W. (2011) Redox biochemistry of mammalian metallothioneins. J. Biol. Inorg. Chem. 16, 1079-1086
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 1079-1086
    • Maret, W.1
  • 47
    • 77958056047 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases as drug targets: Strategies and challenges of inhibitor development
    • Barr, A. J. (2010) Protein-tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development. Future Med. Chem. 2, 1563-1576
    • (2010) Future Med. Chem. , vol.2 , pp. 1563-1576
    • Barr, A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.