TAILIEUCHUNG - Báo cáo khoa học: Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells

The oxidation and inactivation of protein tyrosine phosphatases is one mechanism by which reactive oxygen species influence tyrosine phosphory-lation-dependent signaling events and exert their biological functions. In the present study, we determined the redox status of endogenous protein tyrosine phosphatases in HepG2 and A431 human cancer cells, in which reactive oxygen species are produced constitutively. | ỊFEBS Journal Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells Yi-Wei Lou1 2 Yi-Yun Chen1 2 3 Shu-Fan Hsu1 2 Ren-Kun Chen3 Chih-Lei Lee3 Kay-Hooi Khoo1 2 3 t Nicholas K. Tonks4 t and Tzu-Ching Meng1 2 t 1 Institute of BiologicalChemistry Academia Sinica Taipei Taiwan 2 Institute of BiochemicalSciences College of Life Sciences NationalTaiwan University Taipei Taiwan 3 NationalCore Facility for Proteomics Research Academia Sinica Taipei Taiwan 4 Cold Spring Harbor Laboratory NY USA Keywords cancer cells mass spectrometry protein tyrosine phosphatase PTPIB reactive oxygen species Correspondence . Khoo Institute of BiologicalChemistry Academia Sinica 128 Academia Road Section 2 Taipei 11529 Taiwan Fax 886 2 27889759 Tel 886 2 27855696 E-mail kkhoo@ N. K. Tonks Cold Spring Harbor Laboratory 1 Boungtown Road Cold Spring Harbor NY 11724 USA Fax 1 516 367 6812 Tel 1 516 3678846 E-mail tonks@ . Meng Institute of Biological Chemistry Academia Sinica 128 Academia Road Section 2 Taipei 11529 Taiwan Fax 886 2 27892161 Tel 886 2 27855696 E-mail tcmeng@ These authors contributed equally to this work TThis manuscript is a joint communication of these authors The oxidation and inactivation of protein tyrosine phosphatases is one mechanism by which reactive oxygen species influence tyrosine phosphorylation-dependent signaling events and exert their biological functions. In the present study we determined the redox status of endogenous protein tyrosine phosphatases in HepG2 and A431 human cancer cells in which reactive oxygen species are produced constitutively. We used mass spectrometry to assess the state of oxidation of the catalytic cysteine residue of endogenous PTP1B and show that this residue underwent both reversible and irreversible oxidation to high stoichiometry in response to intrinsic reactive oxygen species production. In addition our data show that the oxidation of PTP1B is specific to the .

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