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Science 7 July 1989:
Vol. 245. no. 4913, pp. 57 - 60
DOI: 10.1126/science.2544996
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Articles

Science, Vol 245, Issue 4913, 57-60
Copyright © 1989 by American Association for the Advancement of Science

articles

Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor

PL Lee, DE Johnson, LS Cousens, VA Fried, and LT Williams

Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.

Basic fibroblast growth factor (bFGF) participates in many processes including early developmental events, angiogenesis, wound healing, and maintenance of neuronal cell viability. A 130-kilodalton protein was isolated on the basis of its ability to specifically bind to bFGF. A complementary DNA clone was isolated with an oligonucleotide probe corresponding to determined amino acid sequences of tryptic peptide fragments of the purified protein. The putative bFGF receptor encoded by this complementary DNA is a transmembrane protein that contains three extracellular immunoglobulin-like domains, an unusual acidic region, and an intracellular tyrosine kinase domain. These domains are arranged in a pattern that is different from that of any growth factor receptor described.


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