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Volumn 58, Issue 12, 1999, Pages 1859-1867

Bis(N,N-dimethylhydroxamido)hydroxooxovanadate inhibition of protein tyrosine phosphatase activity in intact cells: Comparison with vanadate

Author keywords

Dimethylhydroxamidohydroxooxovanadate; Glucose transport; Glycogen synthesis; Insulin action; Protein tyrosine phosphatase; Vanadate

Indexed keywords

BIS(N,N DIMETHYLHYDROXAMIDO)HYDROXOOXOVANADATE; DEOXYGLUCOSE; GLYCOGEN; INSULIN RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 0032751619     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(99)00284-1     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases The yin and yang of protein phosphorylation and signaling . Cell. 80:1995;225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 2
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu J.M., Dixon J.E. Protein tyrosine phosphatases Mechanisms of catalysis and regulation . Curr Opin Chem Biol. 2:1998;633-641.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.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
    • 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
  • 5
    • 0027383705 scopus 로고
    • a of the active site cysteine and the function of the conserved histidine 402
    • a of the active site cysteine and the function of the conserved histidine 402 . Biochemistry. 32:1993;9340-9345.
    • (1993) Biochemistry , vol.32 , pp. 9340-9345
    • Zhang, Z.Y.1    Dixon, J.E.2
  • 6
    • 0028070371 scopus 로고
    • A synthetic tris-sulfotyrosyl dodecapeptide analogue of the insulin receptor 1146-kinase domain inhibits tyrosine dephosphorylation of the insulin receptor in situ
    • Liotta A.S., Kole H.K., Fales H.M., Roth J., Bernier M. A synthetic tris-sulfotyrosyl dodecapeptide analogue of the insulin receptor 1146-kinase domain inhibits tyrosine dephosphorylation of the insulin receptor in situ. J Biol Chem. 269:1994;22996-23001.
    • (1994) J Biol Chem , vol.269 , pp. 22996-23001
    • Liotta, A.S.1    Kole, H.K.2    Fales, H.M.3    Roth, J.4    Bernier, M.5
  • 8
    • 0028298024 scopus 로고
    • Protein tyrosine phosphatase substrate specificity: Size and phosphotyrosine positioning requirements in peptide substrates
    • Zhang Z.Y., Maclean D., McNamara D.J., Sawyer T.K., Dixon J.E. Protein tyrosine phosphatase substrate specificity Size and phosphotyrosine positioning requirements in peptide substrates . Biochemistry. 33:1994;2285-2290.
    • (1994) Biochemistry , vol.33 , pp. 2285-2290
    • Zhang, Z.Y.1    Maclean, D.2    McNamara, D.J.3    Sawyer, T.K.4    Dixon, J.E.5
  • 9
    • 0028990357 scopus 로고
    • Protein-tyrosine phosphatase inhibition by a peptide containing the phosphotyrosyl mimetic, L-O-malonyltyrosine
    • Kole H.K., Akamatsu M., Ye B., Yan X., Barford D., Roller P.P., Burke T.R. Jr. Protein-tyrosine phosphatase inhibition by a peptide containing the phosphotyrosyl mimetic, L-O-malonyltyrosine. Biochem Biophys Res Commun. 209:1995;817-822.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 817-822
    • Kole, H.K.1    Akamatsu, M.2    Ye, B.3    Yan, X.4    Barford, D.5    Roller, P.P.6    Burke T.R., Jr.7
  • 10
    • 0029930442 scopus 로고    scopus 로고
    • 4′-O-[2-(2-Fluoromalonyl)]-L-tyrosine: A phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides
    • Burke T.R. Jr, Ye B., Akamatsu M., Ford H. Jr, Yan X., Kole H., Wolf G., Shoelson S.E., Roller P.P. 4′-O-[2-(2-Fluoromalonyl)]-L-tyrosine A phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides . J Med Chem. 39:1996;1021-1027.
    • (1996) J Med Chem , vol.39 , pp. 1021-1027
    • Burke T.R., Jr.1    Ye, B.2    Akamatsu, M.3    Ford H., Jr.4    Yan, X.5    Kole, H.6    Wolf, G.7    Shoelson, S.E.8    Roller, P.P.9
  • 11
    • 0030467887 scopus 로고    scopus 로고
    • Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design
    • Burke T.R. Jr, Ye B., Yan X., Wang S., Jia Z., Chen L., Zhang Z.Y., Barford D. Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design. Biochemistry. 35:1996;15989-15996.
    • (1996) Biochemistry , vol.35 , pp. 15989-15996
    • Burke T.R., Jr.1    Ye, B.2    Yan, X.3    Wang, S.4    Jia, Z.5    Chen, L.6    Zhang, Z.Y.7    Barford, D.8
  • 12
    • 0032503030 scopus 로고    scopus 로고
    • Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases
    • Huyer G., Kelly J., Moffat J., Zamboni R., Jia Z., Gresser M.J., Ramachandran C. Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases. Anal Biochem. 258:1998;19-30.
    • (1998) Anal Biochem , vol.258 , pp. 19-30
    • Huyer, G.1    Kelly, J.2    Moffat, J.3    Zamboni, R.4    Jia, Z.5    Gresser, M.J.6    Ramachandran, C.7
  • 13
    • 0033555247 scopus 로고    scopus 로고
    • [Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases
    • Desmarais S., Friesen R.W., Zamboni R., Ramachandran C. [Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases. Biochem J. 337:1999;219-223.
    • (1999) Biochem J , vol.337 , pp. 219-223
    • Desmarais, S.1    Friesen, R.W.2    Zamboni, R.3    Ramachandran, C.4
  • 14
    • 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
  • 15
    • 0029917244 scopus 로고    scopus 로고
    • Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis
    • Denu J.M., Lohse D.L., Vijayalakshmi J., Saper M.A., Dixon J.E. Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis. Proc Natl Acad Sci USA. 93:1996;2493-2498.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2493-2498
    • Denu, J.M.1    Lohse, D.L.2    Vijayalakshmi, J.3    Saper, M.A.4    Dixon, J.E.5
  • 17
    • 0025060803 scopus 로고
    • Insulin-mimetic effects of vanadate. Possible implications for future treatment of diabetes
    • Shechter Y. Insulin-mimetic effects of vanadate. Possible implications for future treatment of diabetes. Diabetes. 39:1990;1-5.
    • (1990) Diabetes , vol.39 , pp. 1-5
    • Shechter, Y.1
  • 18
    • 19544378308 scopus 로고    scopus 로고
    • Mechanisms of actions of vanadium in mediating the biological effects of insulin
    • Elberg G., Li J., Shechter Y. Mechanisms of actions of vanadium in mediating the biological effects of insulin. Adv Environ Sci Technol. 31:1998;277-296.
    • (1998) Adv Environ Sci Technol , vol.31 , pp. 277-296
    • Elberg, G.1    Li, J.2    Shechter, Y.3
  • 19
    • 0024474941 scopus 로고
    • 2 potentiates phosphorylation of novel putative substrates for the insulin receptor kinase in intact Fao cells
    • 2 potentiates phosphorylation of novel putative substrates for the insulin receptor kinase in intact Fao cells. J Biol Chem. 264:1989;10126-10132.
    • (1989) J Biol Chem , vol.264 , pp. 10126-10132
    • Heffetz, D.1    Zick, Y.2
  • 20
    • 0024797725 scopus 로고
    • Inhibition of phosphotyrosine phosphatases reveals candidate substrates of the PDGF receptor kinase
    • Zippel R., Morello L., Brambilla R., Comoglio P.M., Alberghina L., Sturani E. Inhibition of phosphotyrosine phosphatases reveals candidate substrates of the PDGF receptor kinase. Eur J Cell Biol. 50:1989;428-434.
    • (1989) Eur J Cell Biol , vol.50 , pp. 428-434
    • Zippel, R.1    Morello, L.2    Brambilla, R.3    Comoglio, P.M.4    Alberghina, L.5    Sturani, E.6
  • 21
    • 0025314959 scopus 로고
    • Activation of permeabilized HL60 cells by vanadate: Evidence for divergent signalling pathways
    • Trudel S., Downey G.P., Grinstein S., Paquet M.R. Activation of permeabilized HL60 cells by vanadate Evidence for divergent signalling pathways . Biochem J. 269:1990;127-131.
    • (1990) Biochem J , vol.269 , pp. 127-131
    • Trudel, S.1    Downey, G.P.2    Grinstein, S.3    Paquet, M.R.4
  • 22
    • 0025166531 scopus 로고
    • Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electropermeabilized human neutrophils
    • Grinstein S., Furuya W., Lu D.J., Mills G.B. Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electropermeabilized human neutrophils. J Biol Chem. 265:1990;318-327.
    • (1990) J Biol Chem , vol.265 , pp. 318-327
    • Grinstein, S.1    Furuya, W.2    Lu, D.J.3    Mills, G.B.4
  • 23
    • 0027223920 scopus 로고
    • Effect of orthovanadate on tyrosine phosphorylation of p120 GTPase-activating protein rat liver macrophages (Kupffer cells)
    • Chao W., Liu H., Olson M.S. Effect of orthovanadate on tyrosine phosphorylation of p120 GTPase-activating protein rat liver macrophages (Kupffer cells). Biochem Biophys Res Commun. 191:1993;55-60.
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 55-60
    • Chao, W.1    Liu, H.2    Olson, M.S.3
  • 24
    • 0029558020 scopus 로고
    • Modulation of insulin action by vanadate: Evidence of a role for phosphotyrosine phosphatase activity to alter cellular signaling
    • Fantus I.G., Deragon G., Lai R., Tang S. Modulation of insulin action by vanadate Evidence of a role for phosphotyrosine phosphatase activity to alter cellular signaling . Mol Cell Biochem. 153:1995;103-112.
    • (1995) Mol Cell Biochem , vol.153 , pp. 103-112
    • Fantus, I.G.1    Deragon, G.2    Lai, R.3    Tang, S.4
  • 25
    • 0344642611 scopus 로고    scopus 로고
    • Inhibition of a Src homology 2 domain containing protein tyrosine phosphatase by vanadate in the primary culture of hepatocytes
    • Pugazhenthi S., Tanha F., Dahl B., Khandelwal R.L. Inhibition of a Src homology 2 domain containing protein tyrosine phosphatase by vanadate in the primary culture of hepatocytes. Arch Biochem Biophys. 335:1996;273-282.
    • (1996) Arch Biochem Biophys , vol.335 , pp. 273-282
    • Pugazhenthi, S.1    Tanha, F.2    Dahl, B.3    Khandelwal, R.L.4
  • 26
    • 0030967205 scopus 로고    scopus 로고
    • Role of oxidative stress in the action of vanadium phosphotyrosine phosphatase inhibitors. Redox independent activation of NF-κB
    • Krejsa C.M., Nadler S.G., Esselstyn J.M., Kavanagh T.J., Ledbetter J.A., Schieven G.L. Role of oxidative stress in the action of vanadium phosphotyrosine phosphatase inhibitors. Redox independent activation of NF-κB. J Biol Chem. 272:1997;11541-11549.
    • (1997) J Biol Chem , vol.272 , pp. 11541-11549
    • Krejsa, C.M.1    Nadler, S.G.2    Esselstyn, J.M.3    Kavanagh, T.J.4    Ledbetter, J.A.5    Schieven, G.L.6
  • 27
    • 0031125106 scopus 로고    scopus 로고
    • Reactions of vanadate with N,N-dimethylhydroxylamine: Aqueous equilibria and the crystal structure of the uncharged oxygen bridged dimer of bis(N,N-dimethylhydroxamido)hydroxooxovanadate
    • Paul P.C., Angus-Dunne S.J., Batchelor R.J., Einstein F.W.B., Tracey A.S. Reactions of vanadate with N,N-dimethylhydroxylamine Aqueous equilibria and the crystal structure of the uncharged oxygen bridged dimer of bis(N,N-dimethylhydroxamido)hydroxooxovanadate . Can J Chem. 75:1997;429-440.
    • (1997) Can J Chem , vol.75 , pp. 429-440
    • Paul, P.C.1    Angus-Dunne, S.J.2    Batchelor, R.J.3    Einstein, F.W.B.4    Tracey, A.S.5
  • 28
    • 0031785046 scopus 로고    scopus 로고
    • Kinetics and molecular modelling studies of the inhibition of protein tyrosine phosphatases by N,N-dimethylhydroxylamine complexes of vanadium(V)
    • Nxumalo F., Glover N.R., Tracey A.S. Kinetics and molecular modelling studies of the inhibition of protein tyrosine phosphatases by N,N-dimethylhydroxylamine complexes of vanadium(V). J Biol Inorg Chem. 3:1998;534-542.
    • (1998) J Biol Inorg Chem , vol.3 , pp. 534-542
    • Nxumalo, F.1    Glover, N.R.2    Tracey, A.S.3
  • 29
    • 0025149102 scopus 로고
    • Effects of amino acid replacements within the tetrabasic cleavage site on the processing of the human insulin receptor precursor expressed in Chinese hamster ovary cells
    • Yoshimasa Y., Paul J.I., Whittaker J., Steiner D.F. Effects of amino acid replacements within the tetrabasic cleavage site on the processing of the human insulin receptor precursor expressed in Chinese hamster ovary cells. J Biol Chem. 265:1990;17230-17237.
    • (1990) J Biol Chem , vol.265 , pp. 17230-17237
    • Yoshimasa, Y.1    Paul, J.I.2    Whittaker, J.3    Steiner, D.F.4
  • 30
    • 0028797745 scopus 로고
    • Insulin stimulation of glycogen synthesis and glycogen synthase activity is blocked by wortmannin and rapamycin in 3T3-L1 adipocytes: Evidence for the involvement of phosphoinositide 3-kinase and p70 ribosomal protein-S6 kinase
    • Shepherd P.R., Nave B.T., Siddle K. Insulin stimulation of glycogen synthesis and glycogen synthase activity is blocked by wortmannin and rapamycin in 3T3-L1 adipocytes Evidence for the involvement of phosphoinositide 3-kinase and p70 ribosomal protein-S6 kinase . Biochem J. 305:1995;25-28.
    • (1995) Biochem J , vol.305 , pp. 25-28
    • Shepherd, P.R.1    Nave, B.T.2    Siddle, K.3
  • 31
    • 0030984321 scopus 로고    scopus 로고
    • New insights into the role and mechanism of glycogen synthase activation by insulin
    • Lawrence J.C., Roach P.J. New insights into the role and mechanism of glycogen synthase activation by insulin. Diabetes. 46:1997;541-547.
    • (1997) Diabetes , vol.46 , pp. 541-547
    • Lawrence, J.C.1    Roach, P.J.2
  • 32
    • 0345496910 scopus 로고    scopus 로고
    • Catalytic effects of vanadium on phosphoryl transfer enzymes
    • Mendz G.L. Catalytic effects of vanadium on phosphoryl transfer enzymes. Adv Environ Sci Technol. 30:1998;307-332.
    • (1998) Adv Environ Sci Technol , vol.30 , pp. 307-332
    • Mendz, G.L.1
  • 33
    • 0023219921 scopus 로고
    • Oral administration of vanadate normalizes blood glucose levels in streptozotocin-treated rats. Characterization and mode of action
    • Meyerovitch J., Farfel Z., Sack J., Shechter Y. Oral administration of vanadate normalizes blood glucose levels in streptozotocin-treated rats. Characterization and mode of action. J Biol Chem. 262:1987;6658-6662.
    • (1987) J Biol Chem , vol.262 , pp. 6658-6662
    • Meyerovitch, J.1    Farfel, Z.2    Sack, J.3    Shechter, Y.4
  • 34
    • 0024443899 scopus 로고
    • Long term improvement of glucose homeostasis by vanadate in obese hyperinsulinemic fa/fa rats
    • Brichard S.M., Pottier A.M., Henquin J.-C. Long term improvement of glucose homeostasis by vanadate in obese hyperinsulinemic fa/fa rats. Endocrinology. 125:1989;2510-2516.
    • (1989) Endocrinology , vol.125 , pp. 2510-2516
    • Brichard, S.M.1    Pottier, A.M.2    Henquin, J.-C.3
  • 35
    • 0025119641 scopus 로고
    • Marked improvement of glucose homeostasis in diabetic ob/ob mice given oral vanadate
    • Brichard S.M., Bailey C.J., Henquin J.-C. Marked improvement of glucose homeostasis in diabetic ob/ob mice given oral vanadate. Diabetes. 39:1990;1326-1332.
    • (1990) Diabetes , vol.39 , pp. 1326-1332
    • Brichard, S.M.1    Bailey, C.J.2    Henquin, J.-C.3
  • 36
    • 0025779733 scopus 로고
    • Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus
    • Meyerovitch J., Rothenberg P., Shechter Y., Bonner-Wei S., Kahn C.R. Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus. J Clin Invest. 87:1991;1286-1294.
    • (1991) J Clin Invest , vol.87 , pp. 1286-1294
    • Meyerovitch, J.1    Rothenberg, P.2    Shechter, Y.3    Bonner-Wei, S.4    Kahn, C.R.5
  • 37
    • 0026635175 scopus 로고
    • Oral vanadate decreases muscle insulin resistance in obese fa/fa rats
    • Brichard S.M., Ongemba L.N., Henquin J.-C. Oral vanadate decreases muscle insulin resistance in obese fa/fa rats. Diabetologia. 35:1992;522-527.
    • (1992) Diabetologia , vol.35 , pp. 522-527
    • Brichard, S.M.1    Ongemba, L.N.2    Henquin, J.-C.3
  • 38
    • 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
  • 39
    • 0029049705 scopus 로고
    • Oral vanadyl sulfate improves hepatic and peripheral insulin sensitivity in patients with non-insulin-dependent diabetes mellitus
    • Cohen N., Halberstam M., Shlimovich P., Chang C.J., Shamoon H., Rossetti L. Oral vanadyl sulfate improves hepatic and peripheral insulin sensitivity in patients with non-insulin-dependent diabetes mellitus. J Clin Invest. 95:1995;2501-2509.
    • (1995) J Clin Invest , vol.95 , pp. 2501-2509
    • Cohen, N.1    Halberstam, M.2    Shlimovich, P.3    Chang, C.J.4    Shamoon, H.5    Rossetti, L.6
  • 40
    • 0002362976 scopus 로고
    • Vanadates as phosphate analogs in biochemistry
    • (Ed. Chasteen ND), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Gresser MJ and Tracey AS, Vanadates as phosphate analogs in biochemistry. In: Vanadium in Biological Systems (Ed. Chasteen ND), pp. 63-79. Kluwer Academic Publishers, Dordrecht, The Netherlands, 1990.
    • (1990) In: Vanadium in Biological Systems , pp. 63-79
    • Gresser, M.J.1    Tracey, A.S.2
  • 42
    • 0347174705 scopus 로고    scopus 로고
    • Peroxo, hydroxylamido and Acac derived vanadium complexes: Chemistry, biochemistry, and insulin-mimetic action of selected vanadium compounds
    • Crans D.C. Peroxo, hydroxylamido and Acac derived vanadium complexes Chemistry, biochemistry, and insulin-mimetic action of selected vanadium compounds . ACS Symp Ser. 711:1998;82-103.
    • (1998) ACS Symp Ser , vol.711 , pp. 82-103
    • Crans, D.C.1
  • 43
    • 17544362069 scopus 로고    scopus 로고
    • Intracluster restriction of Fc receptor γ-chain tyrosine phosphorylation subverted by a protein-tyrosine phosphatase inhibitor
    • Pfefferkorn L.C., Swink S.L. Intracluster restriction of Fc receptor γ-chain tyrosine phosphorylation subverted by a protein-tyrosine phosphatase inhibitor. J Biol Chem. 271:1996;11099-11105.
    • (1996) J Biol Chem , vol.271 , pp. 11099-11105
    • Pfefferkorn, L.C.1    Swink, S.L.2
  • 44
    • 0031722683 scopus 로고    scopus 로고
    • Reactions of vanadium(V) complexes of N,N-dimethylhydroxylamine with sulfur-containing ligands: Implications for protein tyrosine phosphatase inhibition
    • Nxumalo F., Tracey A.S. Reactions of vanadium(V) complexes of N,N-dimethylhydroxylamine with sulfur-containing ligands Implications for protein tyrosine phosphatase inhibition . J Biol Inorg Chem. 3:1998;527-533.
    • (1998) J Biol Inorg Chem , vol.3 , pp. 527-533
    • Nxumalo, F.1    Tracey, A.S.2


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