Purification and Complementary DNA Cloning of a Receptor for Basic Fibroblast Growth Factor
SciencePublished 7 July 1989
Pauline L. Lee, Daniel E. Johnson, Lawrence S. Cousens, Victor A. Fried, Lewis T. Williams
Citations659
SJR quartileQ1
SJR score10.42
SNIP6.62
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TL;DR
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 that is different from that of any growth factor receptor described.
Abstract
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.
Keywords
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