cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor.

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Abstract
The primary structure of the human A-type receptor for platelet-derived growth factor (PDGF) has been etermined. A 6.5-kilobase (kb) transcript was identified through low-stringency hybridization with a probe derived from the b-type PDGF receptor cDNA. The sequence of a cDNA clone corresponding to the 6.5-kb transcript contains an open reading frame that predicts a 1089-amino acid growth factor receptor-like molecule, which displays 44% overall amino acid similarity with the PDGF B-type receptor. The two receptors have a similar domain organization, with five immunoglobulin-like domains extracellularly and an intracellular split protein tyrosine kinase domain. Transfection of the new cDNA into COS cells led to the expression of a protein specifically recognized by an antiserum previously shwn to react with the PDGF A-type receptor. The expressed protein was shown to display high-affinity binding of all three 125I-labeled dimeric forms of PDGF A and B chains in a manner that is characteristic for the PDGF A-type receptor.

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