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Volumn 58, Issue 10, 1999, Pages 1539-1546

Development and validation of an intact cell assay for protein tyrosine phosphatases using recombinant baculoviruses

Author keywords

Baculovirus; Inhibitor; p nitrophenyl phosphate; Pervanadate; Protein tyrosine phosphatase; Vanadate

Indexed keywords

PERVANADATE; PROTEIN TYROSINE PHOSPHATASE; VANADIC ACID;

EID: 0032880903     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(99)00242-7     Document Type: Article
Times cited : (16)

References (34)
  • 2
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • Neel B.G., 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
  • 3
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics and mechanism of catalysis
    • Zhang Z.Y. Protein-tyrosine phosphatases Biological function, structural characteristics and mechanism of catalysis . Crit Rev Biochem Mol Biol. 33:1998;1-52.
    • (1998) Crit Rev Biochem Mol Biol , vol.33 , pp. 1-52
    • Zhang, Z.Y.1
  • 4
    • 0025992709 scopus 로고
    • CD45: A leukocyte-specific member of the protein tyrosine phosphatase family
    • Trowbridge I.S., Ostergaard H.L., Johnson P. CD45 A leukocyte-specific member of the protein tyrosine phosphatase family . Biochim Biophys Acta. 1095:1991;46-56.
    • (1991) Biochim Biophys Acta , vol.1095 , pp. 46-56
    • Trowbridge, I.S.1    Ostergaard, H.L.2    Johnson, P.3
  • 5
    • 0027475743 scopus 로고
    • Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor
    • Cahir McFarland E.D., Hurley T.R., Pingel J.T., Sefton B.M., Shaw A., Thomas M.L. Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor. Proc Natl Acad Sci USA. 90:1993;1402-1406.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1402-1406
    • Cahir McFarland, E.D.1    Hurley, T.R.2    Pingel, J.T.3    Sefton, B.M.4    Shaw, A.5    Thomas, M.L.6
  • 6
    • 0026447125 scopus 로고
    • Regulation of basal tyrosine phosphorylation of the B cell antigen receptor complex by the protein tyrosine phosphatase, CD45
    • Lin J., Brown V.K., Justement L.B. Regulation of basal tyrosine phosphorylation of the B cell antigen receptor complex by the protein tyrosine phosphatase, CD45. J Immunol. 149:1992;3182-3190.
    • (1992) J Immunol , vol.149 , pp. 3182-3190
    • Lin, J.1    Brown, V.K.2    Justement, L.B.3
  • 9
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies demonstrates a role of protein-tyrosine-phosphatase-1B in negative regulation of the insulin action pathway
    • Ahmad F., Li P.M., Meyerovitch J., Goldstein B.J. Osmotic loading of neutralizing antibodies demonstrates a role of protein-tyrosine-phosphatase-1B in negative regulation of the insulin action pathway. J Biol Chem. 270:1995;20503-20508.
    • (1995) J Biol Chem , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 11
    • 0028077830 scopus 로고
    • Potent inhibition of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F2Pmp
    • Burke T.R. Jr, Kole H.K., Roller P.P. Potent inhibition of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F2Pmp. Biochem Biophys Res Commun. 204:1994;129-134.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 129-134
    • Burke T.R., Jr.1    Kole, H.K.2    Roller, P.P.3
  • 12
    • 0030582843 scopus 로고    scopus 로고
    • Selective inhibition of cyclooxygenase-1 and -2 using intact insect cell assays
    • Cromlish W., Kennedy B. Selective inhibition of cyclooxygenase-1 and -2 using intact insect cell assays. Biochem Pharmacol. 52:1996;1777-1785.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1777-1785
    • Cromlish, W.1    Kennedy, B.2
  • 15
    • 0029846429 scopus 로고    scopus 로고
    • CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells
    • Yanagi S., Sugawara H., Kurosaki M., Sabe H., Yamamura H., Kurosaki T. CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells. J Biol Chem. 271:1996;30487-30492.
    • (1996) J Biol Chem , vol.271 , pp. 30487-30492
    • Yanagi, S.1    Sugawara, H.2    Kurosaki, M.3    Sabe, H.4    Yamamura, H.5    Kurosaki, T.6
  • 16
    • 0027414922 scopus 로고
    • The baculovirus Autographa californica encodes a protein tyrosine phosphatase
    • Sheng Z., Charbonneau H. The baculovirus Autographa californica encodes a protein tyrosine phosphatase. J Biol Chem. 268:1993;4728-4733.
    • (1993) J Biol Chem , vol.268 , pp. 4728-4733
    • Sheng, Z.1    Charbonneau, H.2
  • 17
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G. The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell. 68:1992;545-560.
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 18
    • 0024287614 scopus 로고
    • Characterization of the major protein-tyrosine-phosphatases of human placenta
    • Tonks N.K., Diltz C.D., Fischer E.H. Characterization of the major protein-tyrosine-phosphatases of human placenta. J Biol Chem. 263:1988;6731-6737.
    • (1988) J Biol Chem , vol.263 , pp. 6731-6737
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 19
    • 0028157285 scopus 로고
    • Activation of peripheral large granular lymphocytes with the serine/threonine phosphatase inhibitor, okadaic acid
    • McVicar D.W., Mason A.T., Bere E.W., Ortaldo J.R. Activation of peripheral large granular lymphocytes with the serine/threonine phosphatase inhibitor, okadaic acid. Eur J Immunol. 24:1994;165-170.
    • (1994) Eur J Immunol , vol.24 , pp. 165-170
    • McVicar, D.W.1    Mason, A.T.2    Bere, E.W.3    Ortaldo, J.R.4
  • 20
    • 0028176373 scopus 로고
    • Tumor necrosis factor-α, a new tumor promoter, engendered by biochemical studies of okadaic acid
    • Fujiki H., Suganuma M. Tumor necrosis factor-α, a new tumor promoter, engendered by biochemical studies of okadaic acid. J Biochem (Tokyo). 115:1994;1-5.
    • (1994) J Biochem (Tokyo) , vol.115 , pp. 1-5
    • Fujiki, H.1    Suganuma, M.2
  • 21
    • 0028302780 scopus 로고
    • A/GSK-3α in A431 cells
    • A/GSK-3α in A431 cells. J Biol Chem. 269:1994;14341-14344.
    • (1994) J Biol Chem , vol.269 , pp. 14341-14344
    • Yu, J.-S.1    Yang, S.-D.2
  • 22
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.-R., Kwon K.-S., Kim S.-R., Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem. 273:1998;15366-15372.
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.-R.1    Kwon, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 24
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae Y.S., Kang S.W., Seo M.S., Baines I.C., Tekle E., Chock P.B., Rhee S.G. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem. 272:1997;217-221.
    • (1997) J Biol Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 25
    • 0025193521 scopus 로고
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J Biol Chem. 265:1990;2896-2902.
    • (1990) J Biol Chem , vol.265 , pp. 2896-2902
    • Heffetz, D.1    Bushkin, I.2    Dror, R.3    Zick, Y.4
  • 26
    • 0030600199 scopus 로고    scopus 로고
    • Phenylarsine oxide and vanadate: Apparent paradox of inhibition of protein phosphotyrosine phosphatases in rat adipocytes
    • Li J., Elberg G., Shechter Y. Phenylarsine oxide and vanadate Apparent paradox of inhibition of protein phosphotyrosine phosphatases in rat adipocytes . Biochim Biophys Acta. 1312:1996;223-230.
    • (1996) Biochim Biophys Acta , vol.1312 , pp. 223-230
    • Li, J.1    Elberg, G.2    Shechter, Y.3
  • 27
    • 0020463759 scopus 로고
    • Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate
    • Swarup G., Cohen S., Garbers D.L. Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate. Biochem Biophys Res Commun. 107:1982;1104-1109.
    • (1982) Biochem Biophys Res Commun , vol.107 , pp. 1104-1109
    • Swarup, G.1    Cohen, S.2    Garbers, D.L.3
  • 28
    • 0021991110 scopus 로고
    • Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats
    • Heyliger C.E., Tahiliani A.G., McNeil J.H. Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats. Science. 227:1985;1474-1477.
    • (1985) Science , vol.227 , pp. 1474-1477
    • Heyliger, C.E.1    Tahiliani, A.G.2    McNeil, J.H.3
  • 29
    • 0028805449 scopus 로고
    • Metabolic effects of sodium metavanadate in humans with insulin-dependent and noninsulin-dependent diabetes mellitus in vivo and in vitro studies
    • Goldfine A.B., Simonson D.C., Folli F., Patti M.-E., Kahn C.R. Metabolic effects of sodium metavanadate in humans with insulin-dependent and noninsulin-dependent diabetes mellitus in vivo and in vitro studies. J Clin Endocrinol Metab. 80:1995;3311-3320.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 3311-3320
    • Goldfine, A.B.1    Simonson, D.C.2    Folli, F.3    Patti, M.-E.4    Kahn, C.R.5
  • 30
    • 0023270045 scopus 로고
    • Peroxides of vanadium: A novel and potent insulin-mimetic agent which activates the insulin receptor kinase
    • Kadota S., Fantus I.G., Deragon G., Guyda H.J., Hersh B., Posner B.I. Peroxides of vanadium A novel and potent insulin-mimetic agent which activates the insulin receptor kinase . Biochem Biophys Res Commun. 147:1987;259-266.
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 259-266
    • Kadota, S.1    Fantus, I.G.2    Deragon, G.3    Guyda, H.J.4    Hersh, B.5    Posner, B.I.6
  • 31
    • 0024416087 scopus 로고
    • Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase
    • Fantus I.G., Kadota S., Deragon G., Foster B., Posner B.I. Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry. 28:1989;8864-8871.
    • (1989) Biochemistry , vol.28 , pp. 8864-8871
    • Fantus, I.G.1    Kadota, S.2    Deragon, G.3    Foster, B.4    Posner, B.I.5
  • 33
    • 0029614706 scopus 로고
    • Peroxovanadium compounds: Biological actions and mechanism of insulin-mimesis
    • Bevan A.P., Drake P.G., Yale J.-F., Shaver A., Posner B.I. Peroxovanadium compounds Biological actions and mechanism of insulin-mimesis . Mol Cell Biochem. 153:1995;49-58.
    • (1995) Mol Cell Biochem , vol.153 , pp. 49-58
    • Bevan, A.P.1    Drake, P.G.2    Yale, J.-F.3    Shaver, A.4    Posner, B.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.