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Preferential Oxidation of the Second Phosphatase Domain of Receptor-Like PTP-α Revealed by an Antibody against Oxidized Protein Tyrosine Phosphatases
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Preferential Oxidation of the Second Phosphatase Domain of Receptor-Like PTP-α Revealed by an Antibody against Oxidized Protein Tyrosine Phosphatases
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Preferential Oxidation of the Second Phosphatase Domain of Receptor-Like PTP-α Revealed by an Antibody against Oxidized Protein Tyrosine Phosphatases
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Journal Article
Preferential Oxidation of the Second Phosphatase Domain of Receptor-Like PTP-α Revealed by an Antibody against Oxidized Protein Tyrosine Phosphatases
2004
Overview
Protein tyrosine phosphatases (PTPs) constitute a large enzyme family with important biological functions. Inhibition of PTP activity through reversible oxidation of the active-site cysteine residue is emerging as a general, yet poorly characterized, regulatory mechanism. In this study, we describe a generic antibody-based method for detection of oxidation-inactivated PTPs. Previous observations of oxidation of receptor-like PTP (RPTP) α after treatment of cells with H2O2were confirmed. Platelet-derived growth factor (PDGF)-induced oxidation of endogenous SHP-2, sensitive to treatment with the phosphatidylinositol 3-kinase inhibitor LY294002, was demonstrated. Furthermore, oxidation of RPTPα was shown after UV-irradiation. Interestingly, the catalytically inactive second PTP domain of RPTPα demonstrated higher susceptibility to oxidation. The experiments thus demonstrate previously unrecognized intrinsic differences between PTP domains to susceptibility to oxidation and suggest mechanisms for regulation of RPTPs with tandem PTP domains. The antibody strategy for detection of reversible oxidation is likely to facilitate further studies on regulation of PTPs and might be applicable to analysis of redox regulation of other enzyme families with active-site cysteine residues.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Animals
/ Enzymes
/ Humans
/ Hydrogen Peroxide - pharmacology
/ Iodoacetic Acid - pharmacology
/ Mice
/ Oxidation-Reduction - drug effects
/ Oxidation-Reduction - radiation effects
/ Oxidation-Reduction/drug effects/radiation effects
/ Platelet-Derived Growth Factor - pharmacology
/ Protein Tyrosine Phosphatases - chemistry
/ Protein Tyrosine Phosphatases - immunology
/ Protein Tyrosine Phosphatases - metabolism
/ Protein-Tyrosine-Phosphatase/chemistry/immunology/metabolism
/ Proteins
