Identification of a cysteine-rich receptor for fibroblast growth factors.

Abstract:

:The fibroblast growth factor (FGF) family consists of seven members whose activities are thought to be mediated by multiple receptors. Here we describe the cDNA cloning, expression, and characterization of a cysteine-rich FGF receptor (CFR) that is distinct from previously identified FGF receptors. The deduced amino acid sequence for CFR suggests that it is an integral membrane protein containing a large extracellular domain comprising 16 cysteine-rich repeated units and an intracellular domain of 13 amino acids. No reported sequences exhibit significant homologies to either the repeated extracellular motif or to the entire CFR amino acid sequence. Several CFR transcripts are present in embryonic chick tissue, suggesting that CFR undergoes alternate mRNA splicing or that related genes are present. Chinese hamster ovary cells transfected with the CFR cDNA express a 150-kDa polypeptide that binds FGF-1, FGF-2, and FGF-4 but does not bind several non-FGF family members. The high degree of evolutionary conservation among vertebrate CFRs and its ability to bind three different FGFs with high affinity suggest that this unique receptor plays an important role in FGF biology.

journal_name

Mol Cell Biol

authors

Burrus LW,Zuber ME,Lueddecke BA,Olwin BB

doi

10.1128/mcb.12.12.5600

subject

Has Abstract

pub_date

1992-12-01 00:00:00

pages

5600-9

issue

12

eissn

0270-7306

issn

1098-5549

journal_volume

12

pub_type

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