Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate |
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Authors: | G Swarup S Cohen D L Garbers |
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Affiliation: | 1. Department of Pharmacology Vanderbilt University School of Medicine, Nashville, Tennessee 37232U.S.A.;2. Department of Physiology Vanderbilt University School of Medicine, Nashville, Tennessee 37232 U.S.A.;3. Department of Biochemistry Vanderbilt University School of Medicine, Nashville, Tennessee 37232 U.S.A.;4. the Howard Hughes Medical Institute Laboratory Vanderbilt University School of Medicine, Nashville, Tennessee 37232 U.S.A. |
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Abstract: | We have investigated the effect of vanadate on the phosphoserine- and phosphotyrosine-specific phosphoprotein phosphatase activities of A-431 cell membranes and have found that micromolar concentrations of vanadate strongly inhibit the membrane-dependent dephosphorylation of histones containing phosphotyrosine but that they do not inhibit the dephosphorylation of histones containing phosphoserine and phosphothreonine. In addition, the dephosphorylation of endogeneous membrane proteins of A-431 cells (which are known to be phosphorylated at tyrosine residues) was inhibited by vanadate. These results show that vanadate is a potent and selective inhibitor of phosphotyrosyl-protein phosphatase. |
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Keywords: | EGF epidermal growth factor phospho-Tyr-histones histones phosphorylated at tyrosine phospho-Ser-histones histones phosphorylated at serine and threonine |
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