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Effect of the different dimeric forms of the platelet‐derived growth factor on cellular responses in mouse Swiss 3T3 fibroblasts
Author(s) -
Sturani E.,
Brambilla R.,
Morello L.,
Cattaneo M.G.,
Zippel R.,
Alberghina L.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81089-0
Subject(s) - platelet derived growth factor receptor , tyrosine phosphorylation , 3t3 cells , platelet derived growth factor , receptor , phosphorylation , growth factor , tyrosine , gene isoform , biology , microbiology and biotechnology , recombinant dna , biochemistry , chemistry , transfection , gene
PDGF consists of two polypeptide chains, A and B, and all three possible dimers have been isolated from different sources. Human PDGF, essentially AB, porcine PDGF (BB) and recombinant PDGF‐AA were tested on Swiss 3T3 fibroblasts for their ability to stimulate mitogenesis, phosphoinositide turnover and tyrosine phosphorylation of the PDGF receptor. When used in saturating amounts, the three isoforms were equally active in inducing mitogenesis. However, PDGF‐AA was less active than AB and BB to induce the phosphorylation of the receptor and the turnover of phosphoinositides (30% and 50%, respectively). These findings suggest that, in Swiss 3T3 fibroblasts, PDGF receptors of the α‐type are present in a slightly lower amount than β‐type. In addition, the two types of receptor appear to have similar physiological functions.