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Volumn 43, Issue 1, 2007, Pages 100-110

Oxidation sensitivity of the catalytic cysteine of the protein-tyrosine phosphatases SHP-1 and SHP-2

Author keywords

Modified in gel assay; Ox PTP antibody; Oxidation; Protein tyrosine phosphatase; SH2 domains

Indexed keywords

CATHEPSIN B; CYSTEINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GROWTH FACTOR; HYBRID PROTEIN; HYDROGEN PEROXIDE; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2; STEROID RECEPTOR COACTIVATOR 1;

EID: 34249870112     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.03.021     Document Type: Article
Times cited : (55)

References (35)
  • 1
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • Neel B.G., and Tonks N.K. Protein tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 9 (1997) 193-204
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 4
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J.M., and Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 5
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: revisiting PTPs and the control of cell signaling
    • Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121 (2005) 667-670
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 6
    • 0033550050 scopus 로고    scopus 로고
    • Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid
    • Percival M.D., Ouellet M., Campagnolo C., Claveau D., and Li C. Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38 (1999) 13574-13583
    • (1999) Biochemistry , vol.38 , pp. 13574-13583
    • Percival, M.D.1    Ouellet, M.2    Campagnolo, C.3    Claveau, D.4    Li, C.5
  • 7
    • 33646072122 scopus 로고    scopus 로고
    • Inhibition of cathepsins and related proteases by amino acid, peptide, and protein hydroperoxides
    • Headlam H.A., Gracanin M., Rodgers K.J., and Davies M.J. Inhibition of cathepsins and related proteases by amino acid, peptide, and protein hydroperoxides. Free Radic. Biol. Med. 40 (2006) 1539-1548
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1539-1548
    • Headlam, H.A.1    Gracanin, M.2    Rodgers, K.J.3    Davies, M.J.4
  • 8
    • 0032557513 scopus 로고    scopus 로고
    • Oxidative stress inhibits calpain activity in situ
    • Guttmann R.P., and Johnson G.V. Oxidative stress inhibits calpain activity in situ. J. Biol. Chem. 273 (1998) 13331-13338
    • (1998) J. Biol. Chem. , vol.273 , pp. 13331-13338
    • Guttmann, R.P.1    Johnson, G.V.2
  • 9
    • 0037165630 scopus 로고    scopus 로고
    • Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide
    • Hampton M.B., Stamenkovic I., and Winterbourn C.C. Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide. FEBS Lett. 517 (2002) 229-232
    • (2002) FEBS Lett. , vol.517 , pp. 229-232
    • Hampton, M.B.1    Stamenkovic, I.2    Winterbourn, C.C.3
  • 10
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , 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
  • 11
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R.L., Congreve M., Tisi D., Carr R., and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423 (2003) 773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 12
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., Fukada T., and Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002) 387-399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 13
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., and Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 (2005) 183-189
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 14
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • Knebel A., Rahmsdorf H.J., Ullrich A., and Herrlich P. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 15 (1996) 5314-5325
    • (1996) EMBO J. , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herrlich, P.4
  • 15
    • 0008805915 scopus 로고    scopus 로고
    • Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction
    • Gross S., Knebel A., Tenev T., Neininger A., Gaestel M., Herrlich P., and Böhmer F.D. Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction. J. Biol. Chem. 274 (1999) 26378-26386
    • (1999) J. Biol. Chem. , vol.274 , pp. 26378-26386
    • Gross, S.1    Knebel, A.2    Tenev, T.3    Neininger, A.4    Gaestel, M.5    Herrlich, P.6    Böhmer, F.D.7
  • 16
    • 4444242254 scopus 로고    scopus 로고
    • UVA inactivates protein tyrosine phosphatases by calpain-mediated degradation
    • Gulati P., Markova B., Göttlicher M., Böhmer F.D., and Herrlich P.A. UVA inactivates protein tyrosine phosphatases by calpain-mediated degradation. EMBO Rep. 5 (2004) 812-817
    • (2004) EMBO Rep. , vol.5 , pp. 812-817
    • Gulati, P.1    Markova, B.2    Göttlicher, M.3    Böhmer, F.D.4    Herrlich, P.A.5
  • 19
    • 0001737772 scopus 로고    scopus 로고
    • Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation
    • Cunnick J.M., Dorsey J.F., Mei L., and Wu J. Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation. Biochem. Mol. Biol. Int. 45 (1998) 887-894
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 887-894
    • Cunnick, J.M.1    Dorsey, J.F.2    Mei, L.3    Wu, J.4
  • 20
    • 1242342002 scopus 로고    scopus 로고
    • Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases
    • Persson C., Sjöblom T., Groen A., Kappert K., Engström U., Hellman U., Heldin C.H., den Hertog J., and Östman A. Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 101 (2004) 1886-1891
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1886-1891
    • Persson, C.1    Sjöblom, T.2    Groen, A.3    Kappert, K.4    Engström, U.5    Hellman, U.6    Heldin, C.H.7    den Hertog, J.8    Östman, A.9
  • 21
    • 22744444805 scopus 로고    scopus 로고
    • Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP
    • Kwon J., Qu C.K., Maeng J.S., Falahati R., Lee C., and Williams M.S. Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP. EMBO J. 24 (2005) 2331-2341
    • (2005) EMBO J. , vol.24 , pp. 2331-2341
    • Kwon, J.1    Qu, C.K.2    Maeng, J.S.3    Falahati, R.4    Lee, C.5    Williams, M.S.6
  • 22
    • 0031924794 scopus 로고    scopus 로고
    • SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain
    • Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., and Siminovitch K.A. SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol. 18 (1998) 2089-2099
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2089-2099
    • Kozlowski, M.1    Larose, L.2    Lee, F.3    Le, D.M.4    Rottapel, R.5    Siminovitch, K.A.6
  • 25
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel B.G., Gu H., and Pao L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28 (2003) 284-293
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 26
    • 0032521428 scopus 로고    scopus 로고
    • Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
    • Barford D., and Neel B.G. Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2. Structure 6 (1998) 249-254
    • (1998) Structure , vol.6 , pp. 249-254
    • Barford, D.1    Neel, B.G.2
  • 27
    • 10644275378 scopus 로고    scopus 로고
    • An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases
    • Persson C., Kappert K., Engström U., Östman A., and Sjöblom T. An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases. Methods 35 (2005) 37-43
    • (2005) Methods , vol.35 , pp. 37-43
    • Persson, C.1    Kappert, K.2    Engström, U.3    Östman, A.4    Sjöblom, T.5
  • 28
    • 0031041185 scopus 로고    scopus 로고
    • Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera
    • Tenev T., Keilhack H., Tomic S., Stoyanov B., Stein-Gerlach M., Lammers R., Krivtsov A.V., Ullrich A., and Böhmer F.D. Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera. J. Biol. Chem. 272 (1997) 5966-5973
    • (1997) J. Biol. Chem. , vol.272 , pp. 5966-5973
    • Tenev, T.1    Keilhack, H.2    Tomic, S.3    Stoyanov, B.4    Stein-Gerlach, M.5    Lammers, R.6    Krivtsov, A.V.7    Ullrich, A.8    Böhmer, F.D.9
  • 29
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C., and Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7 (1987) 2745-2752
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 31
    • 0029151931 scopus 로고
    • Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C
    • Tomic S., Greiser U., Lammers R., Kharitonenkov A., Imyanitov E., Ullrich A., and Böhmer F.D. Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C. J. Biol. Chem. 270 (1995) 21277-21284
    • (1995) J. Biol. Chem. , vol.270 , pp. 21277-21284
    • Tomic, S.1    Greiser, U.2    Lammers, R.3    Kharitonenkov, A.4    Imyanitov, E.5    Ullrich, A.6    Böhmer, F.D.7
  • 32
    • 10644227929 scopus 로고    scopus 로고
    • Development of a modified in-gel assay to identify protein tyrosine phosphatases that are oxidized and inactivated in vivo
    • Meng T.C., Hsu S.F., and Tonks N.K. Development of a modified in-gel assay to identify protein tyrosine phosphatases that are oxidized and inactivated in vivo. Methods 35 (2005) 28-36
    • (2005) Methods , vol.35 , pp. 28-36
    • Meng, T.C.1    Hsu, S.F.2    Tonks, N.K.3
  • 33
    • 0028180211 scopus 로고
    • RNA splicing regulates the activity of a SH2 domain-containing protein tyrosine phosphatase
    • Mei L., Doherty C.A., and Huganir R.L. RNA splicing regulates the activity of a SH2 domain-containing protein tyrosine phosphatase. J. Biol. Chem. 269 (1994) 12254-12262
    • (1994) J. Biol. Chem. , vol.269 , pp. 12254-12262
    • Mei, L.1    Doherty, C.A.2    Huganir, R.L.3
  • 34
    • 0242585485 scopus 로고    scopus 로고
    • Identification of protein tyrosine phosphatases associating with the PDGF receptor
    • Markova B., Herrlich P., Rönnstrand L., and Böhmer F.D. Identification of protein tyrosine phosphatases associating with the PDGF receptor. Biochemistry 42 (2003) 2691-2699
    • (2003) Biochemistry , vol.42 , pp. 2691-2699
    • Markova, B.1    Herrlich, P.2    Rönnstrand, L.3    Böhmer, F.D.4
  • 35
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M., Yu Z.X., Ferrans V.J., Irani K., and Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270 (1995) 296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5


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