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

• DOI: 10.1073/pnas.86.13.4917
• Publication Date: 2006-05-31T10:58:01Z
• Authors: L Claesson-Welsh; A Eriksson; B Westermark; C H Heldin
• Keywords: Platelet-derived growth factor

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