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A Common PDGF Receptor is Activated by Homodimeric A and B Forms of PDGF

The human platelet-derived growth factor (PDGF) receptor complementary DNA was cloned and expressed by transfection of Chinese hamster ovary (CHO) fibroblasts. The ability of CHO cells expressing the human receptor complementary DNA (CHO-HR5) to interact with different recombinant forms of PDGF (AA...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1988-06, Vol.240 (4858), p.1532-1534
Main Authors: Escobedo, Jaime A., Navankasatussas, Sutip, Cousens, Lawrence S., Coughlin, Shaun R., Bell, Graeme I., Williams, Lewis T.
Format: Article
Language:English
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Summary:The human platelet-derived growth factor (PDGF) receptor complementary DNA was cloned and expressed by transfection of Chinese hamster ovary (CHO) fibroblasts. The ability of CHO cells expressing the human receptor complementary DNA (CHO-HR5) to interact with different recombinant forms of PDGF (AA and BB homodimers) was tested. Both forms of PDGF bind to the transfected receptor, stimulate the receptor tyrosine kinase activity, and elicit a mitogenic response in a manner that was indistinguishable from the responses of Balb/c 3T3 cells. The data indicate that the tyrosine kinase and mitogenic responses of the Balb/c 3T3 cells to AA and BB forms of PDGF can be attributed to a single type of receptor and show that the AA form, like the BB form, is a true mitogen.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2836953