메뉴 건너뛰기




Volumn 12, Issue 10, 1998, Pages 863-870

Redox priming of the insulin receptor β-chain associated with altered tyrosine kinase activity and insulin responsiveness in the absence of tyrosine autophosphorylation

Author keywords

BCNU; CHO HIR; Glutathione; Redox regulation; Signal transduction

Indexed keywords

ANTIOXIDANT; BUTHIONINE SULFOXIMINE; CARMUSTINE; GLUTATHIONE REDUCTASE; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE; VANADIC ACID;

EID: 0031750534     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.10.863     Document Type: Article
Times cited : (71)

References (35)
  • 1
    • 0028278931 scopus 로고
    • The insulin receptor: Structure, function, and signaling
    • Lee, J., and Pilch, P. F. (1994) The insulin receptor: structure, function, and signaling. Am. J. Physiol. 266, C319-C334
    • (1994) Am. J. Physiol. , vol.266
    • Lee, J.1    Pilch, P.F.2
  • 2
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase
    • Taylor, S. S., Radzio-Andzelm, E., and Hunter, T. (1995) How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase. FASEB J. 9, 1255-1260
    • (1995) FASEB J. , vol.9 , pp. 1255-1260
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 4
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R., Wie, I., Ellis, L., and Hendrickson, W. A. (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature (London) 372, 746-754
    • (1994) Nature (London) , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wie, I.2    Ellis, L.3    Hendrickson, W.A.4
  • 5
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S. R. (1997) Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 6
    • 0017261573 scopus 로고
    • Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system
    • Czech, M. P. (1976) Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system. J. Biol. Ckem. 251, 1164-1170
    • (1976) J. Biol. Ckem. , vol.251 , pp. 1164-1170
    • Czech, M.P.1
  • 7
    • 0020037168 scopus 로고
    • Similarities between insulin, hydrogen peroxide, concanavalin A, and anti-insulin receptor antibody stimulated glucose transport: Increase in the number of transport sites
    • Ludvigsen, C., and Jarett, L. (1982) Similarities between insulin, hydrogen peroxide, concanavalin A, and anti-insulin receptor antibody stimulated glucose transport: increase in the number of transport sites. Metabolism 31, 284-287
    • (1982) Metabolism , vol.31 , pp. 284-287
    • Ludvigsen, C.1    Jarett, L.2
  • 8
    • 0016284089 scopus 로고
    • Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin
    • Czech, M. P., Lawrence, J. C., Jr., and Lynn, W. S. (1974) Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. Proc. Natl. Acad. Sci. USA 71, 4173-4177
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4173-4177
    • Czech, M.P.1    Lawrence Jr., J.C.2    Lynn, W.S.3
  • 9
    • 0023655201 scopus 로고
    • Stimulation of insulin-like growth factor II receptor binding and insulin receptor kinase activity in rat adipocytes
    • Kadota, S., Fantus, I. G., Deragon, G., Guyda, H. J., and Posner, B. I. (1987) Stimulation of insulin-like growth factor II receptor binding and insulin receptor kinase activity in rat adipocytes. J. Biol. Chem. 262, 8252-8256
    • (1987) J. Biol. Chem. , vol.262 , pp. 8252-8256
    • Kadota, S.1    Fantus, I.G.2    Deragon, G.3    Guyda, H.J.4    Posner, B.I.5
  • 10
    • 0023442337 scopus 로고
    • Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide
    • Hayes, G. R., and Lockwood, D. H. (1987) Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide. Proc. Natl. Acad. Sci. USA 84, 8115-8119
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8115-8119
    • Hayes, G.R.1    Lockwood, D.H.2
  • 11
    • 0023931255 scopus 로고
    • Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells
    • Koshio, O., Akanuma, Y., and Kasuga, M. (1988) Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells. Biochem. J. 250, 95-101.
    • (1988) Biochem. J. , vol.250 , pp. 95-101
    • Koshio, O.1    Akanuma, Y.2    Kasuga, M.3
  • 12
    • 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, 2896-2902
    • (1990) J. Biol. Chem. , vol.265 , pp. 2896-2902
    • Heffetz, D.1    Bushkin, I.2    Dror, R.3    Zick, Y.4
  • 14
    • 0024416087 scopus 로고
    • Pervanadate (peroxide(s) of vanadate) mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase
    • Fantus, G., Kadota, S., Deragon, G., Foster, B., and Posner, B. I. (1989) Pervanadate (peroxide(s) of vanadate) mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry 28, 8864-8871
    • (1989) Biochemistry , vol.28 , pp. 8864-8871
    • Fantus, G.1    Kadota, S.2    Deragon, G.3    Foster, B.4    Posner, B.I.5
  • 15
    • 0023192743 scopus 로고
    • Differential sensitivity of the insulin-receptor kinase to thiol and oxidizing agents in the absence and presence of insulin
    • Wilden, P. A., and Pessin, J. E. (1987) Differential sensitivity of the insulin-receptor kinase to thiol and oxidizing agents in the absence and presence of insulin. Biochem. J. 245, 325-331
    • (1987) Biochem. J. , vol.245 , pp. 325-331
    • Wilden, P.A.1    Pessin, J.E.2
  • 16
    • 0029038858 scopus 로고
    • Thiol-specific biotinylation of the insulin receptor in permeabilized cells enhances receptor function
    • Bernier, M., Nadiv, O., and Kole, H. K. (1995) Thiol-specific biotinylation of the insulin receptor in permeabilized cells enhances receptor function. Biochemistry 34, 8357-8364
    • (1995) Biochemistry , vol.34 , pp. 8357-8364
    • Bernier, M.1    Nadiv, O.2    Kole, H.K.3
  • 17
    • 0027173479 scopus 로고
    • Sulphydryl agents modulate insulin- and epidermal growth factor (EGF) receptor kinase via reaction with intracellular receptor domains: Differential effects on basal versus activated receptors
    • Clark, S., and Konstantopoulos, N. (1993) Sulphydryl agents modulate insulin- and epidermal growth factor (EGF) receptor kinase via reaction with intracellular receptor domains: differential effects on basal versus activated receptors. Biochem. J. 292, 217-223
    • (1993) Biochem. J. , vol.292 , pp. 217-223
    • Clark, S.1    Konstantopoulos, N.2
  • 18
    • 0028941088 scopus 로고
    • Mutagenic structure/function analysis of the cytoplasmic cysteines of the insulin receptor
    • Macaulay, S. L., Polites, M., Frenkel, M. J, Hewish, D. R., and Ward, C. W. (1995) Mutagenic structure/function analysis of the cytoplasmic cysteines of the insulin receptor. Biochem. J. 306, 811-820
    • (1995) Biochem. J. , vol.306 , pp. 811-820
    • Macaulay, S.L.1    Polites, M.2    Frenkel, M.J.3    Hewish, D.R.4    Ward, C.W.5
  • 19
    • 0025753381 scopus 로고
    • Insulin sensitivity and insulin clearance in human immunodeficiency virus-infected men
    • Hommes, M. J. T., Romijn, J. A., Endert, E., Schattetikerk, J. K. M. E., and Sauerwein, H. P. (1991) Insulin sensitivity and insulin clearance in human immunodeficiency virus-infected men. Metabolism 40, 651-656
    • (1991) Metabolism , vol.40 , pp. 651-656
    • Hommes, M.J.T.1    Romijn, J.A.2    Endert, E.3    Schattetikerk, J.K.M.E.4    Sauerwein, H.P.5
  • 20
    • 0030457787 scopus 로고    scopus 로고
    • Elevated hepatic γ-glutamylcysteine synthetase activity and abnormal sulfate levels in liver and muscle tissue may explain cysteine and glutathione levels in SIV-infected rhesus macaques
    • Gross, A., Hack, V., Stahl-Hennig, C., and Dröge, W. (1996) Elevated hepatic γ-glutamylcysteine synthetase activity and abnormal sulfate levels in liver and muscle tissue may explain cysteine and glutathione levels in SIV-infected rhesus macaques. AIDS Res. Hum. Retrovir. 12, 1639-1641
    • (1996) AIDS Res. Hum. Retrovir. , vol.12 , pp. 1639-1641
    • Gross, A.1    Hack, V.2    Stahl-Hennig, C.3    Dröge, W.4
  • 21
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by an early damage of mitochondrial functions. Evidences for the involvement of milochondrial radical generation
    • Schulze-Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacobs, W., and Fiers, W. (1992) Cytotoxic activity of tumor necrosis factor is mediated by an early damage of mitochondrial functions. Evidences for the involvement of milochondrial radical generation. J. Biol. Chem. 267, 5317-5323
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacobs, W.5    Fiers, W.6
  • 24
    • 0024595926 scopus 로고
    • Low concentrations of acid soluble thiol (cysteine) in the blood plasma of HIV-1 infected patients
    • Eck, H.-P., Gmünder, H., Hartmann, M., Peizoldt, D., Daniel, V., and Dröge, W. (1989) Low concentrations of acid soluble thiol (cysteine) in the blood plasma of HIV-1 infected patients. Biol. Chem. Hoppe-Seyler 370, 101-108
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 101-108
    • Eck, H.-P.1    Gmünder, H.2    Hartmann, M.3    Peizoldt, D.4    Daniel, V.5    Dröge, W.6
  • 25
    • 0018666729 scopus 로고
    • Potent and specific inhibitor of glutathione synthesis by buthionine sulfoximine (S-h-butylhomocysteine sulfoximine)
    • Griffith, O., and Meister A. (1979) Potent and specific inhibitor of glutathione synthesis by buthionine sulfoximine (S-h-butylhomocysteine sulfoximine). J. Biol. Chem. 254, 7558-7560
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.1    Meister, A.2
  • 26
    • 0017687764 scopus 로고
    • Severe generalized glutathione reductase deficiency after antitumor chemotherapy with BCNU
    • Frischer, H., and Ahmad T. (1977) Severe generalized glutathione reductase deficiency after antitumor chemotherapy with BCNU. J. Lab. Clin. Med. 89, 1080-1082
    • (1977) J. Lab. Clin. Med. , vol.89 , pp. 1080-1082
    • Frischer, H.1    Ahmad, T.2
  • 27
    • 0023839663 scopus 로고
    • Inhibition of glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea
    • Karplus, P. A., Krauth-Siegel, R. L., Schirmer, R. H., and Schulz, G. E. (1988) Inhibition of glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. Eur. J. Biochem. 171, 193-198
    • (1988) Eur. J. Biochem. , vol.171 , pp. 193-198
    • Karplus, P.A.1    Krauth-Siegel, R.L.2    Schirmer, R.H.3    Schulz, G.E.4
  • 28
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 30
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., van der Geer, P., and Hunter, T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-149
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van der Geer, P.2    Hunter, T.3
  • 31
    • 0027277107 scopus 로고
    • Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor
    • Feener, E. P., Backer, J. M., King, G. L., Wilden, P. A., and Sun, X. J. (1993) Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor. J. Biol. Chem. 268, 11256-11264
    • (1993) J. Biol. Chem. , vol.268 , pp. 11256-11264
    • Feener, E.P.1    Backer, J.M.2    King, G.L.3    Wilden, P.A.4    Sun, X.J.5
  • 32
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • Seres, T., Ravichandran, V., Moriguchi, T., Rokutan, K., Thomas, J. A., and Johnston, R. B., Jr. (1996) Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress. J. Immunol. 156, 1973-1980
    • (1996) J. Immunol. , vol.156 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston Jr., R.B.6
  • 33
    • 0026502692 scopus 로고
    • Insulin-induced surface redistribution regulates internalization of the insulin receptor and requires its autophosphorylation
    • Carpentier, J.-L., Paccaud, J.-P., Gorden, P., Rutter, W. J., and Orci, L. (1992) Insulin-induced surface redistribution regulates internalization of the insulin receptor and requires its autophosphorylation. Proc. Natl. Acad. Sci. USA 89, 162-166
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 162-166
    • Carpentier, J.-L.1    Paccaud, J.-P.2    Gorden, P.3    Rutter, W.J.4    Orci, L.5
  • 34
    • 0030841111 scopus 로고    scopus 로고
    • Effects of sulfhydryl modification reagents on the kinase activity of the epidermal growth factor receptor
    • Woltjer, R. L., and Staros, J. V. (1997) Effects of sulfhydryl modification reagents on the kinase activity of the epidermal growth factor receptor. Biochemistry 36, 9911-9916
    • (1997) Biochemistry , vol.36 , pp. 9911-9916
    • Woltjer, R.L.1    Staros, J.V.2
  • 35
    • 0025825989 scopus 로고
    • Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum
    • Bauskin, A. R., Alkalay, I., and Ben-Neriah, Y. (1991) Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum. Cell 66, 685-696
    • (1991) Cell , vol.66 , pp. 685-696
    • Bauskin, A.R.1    Alkalay, I.2    Ben-Neriah, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.