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Biological Chemistry

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

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1437-4315
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Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine

Claudia von Montfort
  • Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany
  • Other articles by this author:
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/ Victor S. Sharov
  • Department of Pharmaceutical Chemistry, Center for Neurobiology and Immunology Research, Higuchi Biosciences Center, University of Kansas, Lawrence, KS 66047, USA
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/ Sabine Metzger
  • Biologisch-Medizinisches Forschungszentrum, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany
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/ Christian Schöneich
  • Department of Pharmaceutical Chemistry, Center for Neurobiology and Immunology Research, Higuchi Biosciences Center, University of Kansas, Lawrence, KS 66047, USA
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/ Helmut Sies
  • Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany and Biologisch-Medizinisches Forschungszentrum, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany
  • Other articles by this author:
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/ Lars-Oliver Klotz
  • Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.175

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.

Keywords: oxidative stress; photosensitization; signal transduction; tyrosine phosphorylation; ultraviolet radiation

About the article

Corresponding author


Received: May 23, 2006

Accepted: July 19, 2006

Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1399–1404, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.175.

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