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J Biol Chem, Vol. 274, Issue 49, 34543-34546, December 3, 1999

COMMUNICATION
Roles of Superoxide Radical Anion in Signal Transduction Mediated by Reversible Regulation of Protein-tyrosine Phosphatase 1B

William C. Barrett, Jon P. DeGnore^§, Yen-Fang Keng^¶, Zhong-Yin Zhang^¶, Moon B. Yim, and P. Boon Chock

From the  Laboratory of Biochemistry and the ^§ Laboratory of Biophysical Chemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 and the ^¶ Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461

Growth factors induce intracellular production of reactive oxygen species in non-phagocytic cells and elevation of their phosphorylated protein tyrosine level. The latter can be achieved by activating protein-tyrosine kinases and/or inactivating protein-tyrosine phosphatases (PTPs). A highly abundant PTP, PTP-1B, is known to be inactivated by oxidation of its catalytic site Cys-215. We show that O₂ is kinetically more efficient and chemically more specific oxidant than H₂O₂ for inactivating PTP-1B. The second-order rate constant for the O₂- and H₂O₂-mediated inactivation is 334 ± 45 M¹ s¹ and 42.8 ± 3.8 M¹ s¹, respectively. PTP-1B oxidized by H₂O₂ exhibits significantly more oxidized methionine residues and shows a lower degree of reversibility. The initial oxidative product, the Cys-215 sulfenic derivative, can easily be oxidized further to its irreversible sulfinic and sulfonic derivatives. This step is prevented by glutathionylation of the sulfenic derivative to form a S-glutathionylated PTP-1B, which can be reactivated by dithiothreitol or thioltransferase. Thus, a signal transduction mechanism mediated by the O₂ and the participation of glutathione is proposed for the regulation of PTP-1B. This mechanism is supported by the in vivo demonstration that glutathionylated PTP-1B at Cys-215 is formed in A431 cells when they were treated with epidermal growth factor.

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