CG&D
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
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by O'Connor, T. J.
Right arrow Articles by Fujita, D. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Connor, T. J.
Right arrow Articles by Fujita, D. J.

Cell Growth & Differentiation, Vol 3, Issue 7 435-442, Copyright © 1992 by American Association of Cancer Research

ARTICLES

pp60c-src in human melanocytes and melanoma cells exhibits elevated specific activity and reduced tyrosine 530 phosphorylation compared to human fibroblast pp60c-src

TJ O'Connor, E Neufeld, J Bechberger and DJ Fujita
Department of Medical Biochemistry, University of Calgary, Health Sciences Center, Alberta, Canada.

Elevated levels of pp60c-src tyrosine kinase activity have been implicated in both tumorigenesis and cell differentiation. We have found a 2- to 4-fold elevation in pp60c-src specific activity in certain human melanoma cell lines compared to human foreskin fibroblasts. This activation of pp60c-src did not appear to be related to melanoma tumor progression, because when normal human epidermal melanocytes were examined, it was found that they contained pp60c-src having a 7-fold elevation in specific activity compared to pp60c-src from human fibroblasts. It was determined that pp60c-src from melanocytes was not the neuronal form, pp60c-src+. Melanocyte pp60c-src exhibited a reduced level of phosphorylation on its carboxyl-terminal regulatory site, tyrosine 530, which might be responsible for its elevated specific activity. These results suggest that, in melanocytes, regulation of tyrosine 530 phosphorylation-dephosphorylation favors activation of pp60c-src. This activation may be involved in the growth, differentiation, or function of human melanocytes.


This article has been cited by other articles:


Home page
 Cancer Res.Home page
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 page
 Cancer Res.Home page
M. von Willebrand, E. Zacksenhaus, E. Cheng, P. Glazer, and R. Halaban
The Tyrphostin AG1024 Accelerates the Degradation of Phosphorylated Forms of Retinoblastoma Protein (pRb) and Restores pRb Tumor Suppressive Function in Melanoma Cells
Cancer Res., March 15, 2003; 63(6): 1420 - 1429.
[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 © 1992 by the American Association of Cancer Research.