cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor.
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 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 shown 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.
Claesson-Welsh
L
L
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
Eriksson
A
A
Westermark
B
B
Heldin
C H
CH
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D006801:Humans; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D010982:Platelet-Derived Growth Factor / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000235:genetics*; D017479:Receptors, Platelet-Derived Growth Factor; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D014162:Transfection
D010982:Platelet-Derived Growth Factor; D011956:Receptors, Cell Surface; D004247:DNA; D017479:Receptors, Platelet-Derived Growth Factor