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(Received for publication, September 19, 1996, and in revised form, November 15, 1996)
From the Departments of FGF-8 is a member of the family of fibroblast
growth factors and is expressed during vertebrate embryo development.
Eight potential FGF-8 isoforms are generated by alternative splicing in
mice, several of which are expressed during embryogenesis in epithelial
locations. The significance of the multiple isoforms is currently
unknown. In this report, we investigate the expression patterns and the
specificity of the FGF-8 isoforms for known fibroblast growth factor
(FGF) receptors. RNAs for seven of the eight potential isoforms are
present at multiple sites of embryonic Fgf8 expression. None of the FGF-8 isoforms exhibited activity when assayed with BaF3
cells expressing the "b" splice forms of FGF receptors 1-3, which
are mostly expressed in epithelial tissues. Mesenchymally expressed
"c" splice forms of FGF receptors 2 and 3 and FGF receptor 4 were
activated by several FGF-8 isoforms. These findings are consistent with
the hypothesis that the multiple FGF-8 isoforms are functionally
redundant and function to signal in paracrine (epithelial to
mesenchymal) contexts.
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3733-3738
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
and
Molecular Biology and
Pharmacology, 
Pathology, and § Pediatrics, Washington
University School of Medicine, St. Louis, Missouri 63110 and the
** Division of Congenital Defects, Department of Pediatrics, University
of Washington School of Medicine, Seattle, Washington 98195
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