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
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Epstein, R. J.
Right arrow Articles by Stiles, C. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Epstein, R. J.
Right arrow Articles by Stiles, C. D.

Cell Growth & Differentiation, Vol 3, Issue 3 157-164, Copyright © 1992 by American Association of Cancer Research


ARTICLES

Extracellular calcium mimics the actions of platelet-derived growth factor on mouse fibroblasts

RJ Epstein, BJ Druker, JC Irminger, SD Jones, TM Roberts and CD Stiles
Department of Medicine, Harvard Medical School, Boston, Massachusetts.

Microprecipitates of calcium phosphate (CaPO4) can substitute for platelet-derived growth factor (PDGF) to stimulate the growth of cultured 3T3 cells. In two-part complementation assays, CaPO4 behaves as a PDGF-like "competence factor"--that is, the mitogenic response to CaPO4 is enhanced synergistically by "progression factors" contained in platelet-poor plasma. In studies described here, we show that early cytoplasmic and intranuclear events in the mitogenic response to CaPO4 are equivalent to those induced by PDGF. However, no net increase in tyrosine kinase activity of either the PDGF-alpha or PDGF-beta receptor is seen following exposure to CaPO4. Our data suggest that calcium acts within the cell, regulating events which normally proceed from activation of PDGF receptors. Alternatively, microprecipitates of CaPO4 could act externally by activating a growth factor receptor which escapes detection with available reagents.


This article has been cited by other articles:


Home page
J Biol ChemHome page
X. Ouyang, T. Gulliford, H. Zhang, G. C. Huang, and R. Epstein
Human Cancer Cells Exhibit Protein Kinase C-dependent c-erbB-2 Transmodulation That Correlates with Phosphatase Sensitivity and Kinase Activity
J. Biol. Chem., September 6, 1996; 271(36): 21786 - 21792.
[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.