Platelet Derived Growth Factor

PDGF is a major mitogen for fibroblasts, smooth muscle cells, and other cells. It was originally identified as a component of whole-blood serum (40-60 ng/mL) that was subsequently isolated from human platelets.

PDGF consists of two structurally similar polypeptide chains (A and B), which combine to form homo- and heterodimers. The three-dimensional structure of PDGF-BB has been shown to have similarity to NGF, TGFb, and vascular endothelial growth factor (VEGF)s, which have homologous amino acid sequences.

The PDGF isoforms promote a response by binding to two structurally similar binding sites of a protein tyrosine kinase receptor, designated a and b (91). Binding of PDGF can result in mitosis, chemotaxis, actin reorganization, or prevention of apoptosis in certain cell lines.

In serum both forms of PDGF bind to a2-macroglobulin. PDGF synergizes with EGF and IGF-1 in stimulating normal Balb/C 3T3 fibroblasts to proliferate

(91). Its action is restricted to mesenchymal and neuroectoderm cells, which have specific PDGF receptors exhibiting tyrosine kinase activity (88).

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