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Cell Growth & Differentiation, Vol 6, Issue 2 123-130, Copyright © 1995 by American Association of Cancer Research


ARTICLES

Mechanism of c-SRC activation in human melanocytes: elevated level of protein tyrosine phosphatase activity directed against the carboxy-terminal regulatory tyrosine [published erratum appears in Cell Growth Differ 1995 Apr;6(4):484]

TJ O'Connor, JD Bjorge, HC Cheng, JH Wang and DJ Fujita
MRC Signal Transduction Group, University of Calgary, Alberta, Canada.

Normal human melanocytes, and some human melanoma cell lines, contain c-SRC which is constitutively activated by hypophosphorylation of tyrosine 530. We investigated the possibility that the activation of c-SRC in melanocytes might be attributable to elevated levels of tyrosine 530-directed protein tyrosine phosphatase activity in these cells. We found three times more of this phosphatase activity in cell extracts from melanocytes compared to fibroblasts. The majority of the tyrosine 530-dephosphorylating activity was present in the particulate fraction of cell homogenates, where c-SRC is also located. Treatment of melanocytes with the protein tyrosine phosphatase inhibitor, sodium orthovanadate, caused inactivation of c-SRC. From these results, we conclude that activation of c-SRC in human melanocytes may be attributed to an elevated level of protein tyrosine phosphatase activity directed against tyrosine 530.


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S. Zhu, J. D. Bjorge, and D. J. Fujita
PTP1B Contributes to the Oncogenic Properties of Colon Cancer Cells through Src Activation
Cancer Res., November 1, 2007; 67(21): 10129 - 10137.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1995 by the American Association of Cancer Research.