Editor-in-Chief: Brüne, Bernhard
Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred
IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162
CiteScore 2018: 3.09
SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820
Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine
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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