Differential binding, biological and biochemical actions of recombinant PDGF AA, AB, and BB molecules on connective tissue cells
✍ Scribed by Gary R. Grotendorst; Atsuyuki Igarashi; Ronald Larson; Yoshinao Soma; Marc Charette
- Book ID
- 102887062
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 986 KB
- Volume
- 149
- Category
- Article
- ISSN
- 0021-9541
No coin nor oath required. For personal study only.
✦ Synopsis
We have compared the biological and biochemical properties of recombinant PDGF AA, AB, and BB using three types of fibroblastic cells: NIH/3T3, human skin fibroblast, and fetal bovine aortic smooth muscle. PDGF binding, receptor autophosphorylation, phosphatidyl inositol hydrolysis, as well as chemotactic and mitogenic responses of the cells were analyzed. PDCF-AB and PDGF-BB showed similar receptor binding, receptor autophosphorylation, and potent biological activity for all three of the cell types tested. In contrast, PDGF-AA was biologically active only for the NIH/3T3 cells in which binding sites for PDGF-AA were abundant, but was inactive for bovine aortic smooth muscle cells and human skin fibroblasts in which binding sites for PDGF-AA were absent. PDGF-AA could not induce any biochemical changes in the human skin fibroblasts or smooth muscle cells. Western blot studies with anti-Type a and p PDGF receptor antibodies indicate that the NIHi3T3 cells contained both PDGF a and p receptors, whereas the human skin fibroblasts and bovine smooth muscle cells contained only detectable levels of p receptors. These results indicate that cells possessing high levels of PDGF p receptors only are capable of responding equally well to either PDGF AB or BB.