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Reversible regulation of SHP‐1 tyrosine phosphatase activity by oxidation
Author(s) -
Cunnick Jess M.,
Dorsey Jay F.,
Mei Lin,
Wu Jie
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.7510450506
Subject(s) - protein tyrosine phosphatase , chemistry , tyrosine , phosphatase , biochemistry , microbiology and biotechnology , biology , phosphorylation
Increasing evidence indicates that redox regulation is an important signaling mechanism. Protein tyrosine phosphatases (PTPases) are sensitive to oxidative inactivation and are potential targets of redox regulation. In this study, we analyzed the reversibility of oxidative inactivation of the PTPase SHP‐1, which negatively regulates protein tyrosine kinase signaling. H 2 O 2 inactivated SHP‐1 in vitro . Incubation of the H 2 O 2 ‐inactivated SHP‐1 with dithiothreitol recovered 44–99% of the PTPase activity, depending on the H 2 O 2 concentrations used to inactivate SHP‐1. Glutathione and N‐acetylcysteine also reactivated H 2 O 2 ‐treated SHP‐1. Stimulation of SHP‐1‐transfected HeLa cells with H 2 O 2 rapidly decreased SHP‐1 activity, which was completely reversed within 15 min. Thus, oxidative inactivation of SHP‐1 is a reversible process.