A glioma-derived PDGF A chain homodimer has different functional activities from a PDGF AB heterodimer purified from human platelets.

Glioma-derived growth factor I (GDGF-I) is structurally similar to a platelet-derived growth factor (PDGF) A chain homodimer, whereas PDGF purified from human platelets is a heterodimer of one A and one B chain. Binding experiments revealed that GDGF-I and PDGF bound to a common receptor on human fibroblasts, but also suggested the presence of a second receptor type recognizing only PDGF. In contrast to PDGF, GDGF-I had only a limited mitogenic activity, a low ability to stimulate receptor autophosphorylation and actin reorganization, and no chemotactic activity. GDGF-I did, however, cause transmodulation of EGF receptors, suggesting that it, like PDGF, activates protein kinase C in fibroblasts. These data indicate that different PDGF-like growth factors have different functional activities, which are possibly mediated via different receptors.