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Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine

von Montfort, Claudia
Sharov, Victor S.
Metzger, Sabine
Schoeneich, Christian
Sies, Helmut
Klotz, Lars-Oliver
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Abstract
Singlet oxygen (1O2), an electronically excited form of molecular oxygen, is a mediator of biological effects of ultraviolet A radiation, stimulating signaling cascades in human cells. We demonstrate here that 1O2 generated by photosensitization or by thermodecomposition of 3,3′-(1,4-naphthylidene)dipropionate-1,4-endoperoxide inactivates isolated protein tyrosine phosphatases (PTPases). PTPase activities of PTP1B or CD45 were abolished by low concentrations of 1O2, but were largely restored by post-treatment with dithiothreitol. Electrospray ionization mass spectrometry analysis of tryptic digests of PTP1B exposed to 1O2 revealed oxidation of active-site Cys215 as the only cysteine residue oxidized. In summary, 1O2 may activate signaling cascades by interfering with phosphotyrosine dephosphorylation.
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2006
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Walter de Gruyter
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Montfort et al. "Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine." Biological Chemistry. Volume 387, Issue 10/11, Pages 1399–1404, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, November 2006. http://dx.doi.org/10.1515/BC.2006.175
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