Calcium in the Action of Growth Factors

Publisher Website
Google Scholar
Abstract
The proliferation of cells in vivo and in culture is regulated by polypeptide growth factors, such as epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). Binding of growth factors to their specific cell-surface receptors initiates a cascade of biochemical events in the cell which ultimately leads to DNA synthesis and cell division. Immediate consequences of receptor activation include tyrosine-specific protein phosphorylations, a sustained increase in cytoplasmic pH and a transient rise in cytoplasmic free Ca2+. The PDGF-induced Ca2+ signal is due to Ca2+ release from intracellular stores, whereas EGF seems to activate a voltage-independent Ca2+ channel in the plasma membrane. Monoclonal antibodies to the EGF receptor that stimulate the tyrosine-specific protein kinase fail to raise [Ca2+]i and are not mitogenic for quiescent cells. These results suggest that activation of the EGF receptor tyrosine kinase is not sufficient for the induction of a Ca2+ signal, and that the rise in [Ca2+]i is indispensable for cell proliferation.

This publication has 44 references indexed in Scilit: