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Methods Enzymol. 2013;528:189-94. doi: 10.1016/B978-0-12-405881-1.00011-2.

Detection of H2O2-mediated phosphorylation of kinase-inactive PDGFRα.

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1
The Schepens Eye Research Institute, Massachusetts Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts, USA.

Abstract

Platelet-derived growth factor (PDGF) receptor α (PDGFRα) belongs to the 58-member family of receptor tyrosine kinases and contributes to a variety of physiological and pathological settings. Activation of PDGFRα proceeds by at least two mechanisms. The traditional route involves PDGF-dependent dimerization and activation of the receptor's intrinsic kinase activity. The second mechanism proceeds intracellularly and involves reactive oxygen species and Src family kinases, which activate monomeric PDGFRα. Herein we describe an assay to investigate reactive oxygen species-mediated phosphorylation of PDGFRα that is independent of the receptor's intrinsic kinase activity.

KEYWORDS:

H(2)O(2)-regulated kinases; Kinase activity; PDGF receptor; Receptor tyrosine kinases; Tyrosine kinases

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