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Vol. 10, Issue 5, 1429-1444, May 1999
*Department of Cell Biology and the Human basic fibroblast growth factor (FGF-2) occurs in four
isoforms: a low molecular weight (LMW FGF-2, 18 kDa) and three high
molecular weight (HMW FGF-2, 22, 22.5, and 24 kDa) forms. LMW FGF-2 is
primarily cytoplasmic and functions in an autocrine manner, whereas HMW
FGF-2s are nuclear and exert activities through an intracrine, perhaps
nuclear, pathway. Selective overexpression of HMW FGF-2 forms in
fibroblasts promotes growth in low serum, whereas overexpression of LMW
FGF-2 does not. The HMW FGF-2 forms have two functional domains: an
amino-terminal extension and a common 18-kDa amino acid sequence. To
investigate the role of these regions in the intracrine signaling of
HMW FGF-2, we produced stable transfectants of NIH 3T3 fibroblasts
overexpressing either individual HMW FGF-2 forms or artificially
nuclear-targeted LMW FGF-2. All of these forms of FGF-2 localize to the
nucleus/nucleolus and induce growth in low serum. The nuclear forms of
FGF-2 trigger a mitogenic stimulus under serum starvation conditions
and do not specifically protect the cells from apoptosis. These data indicate the existence of a specific role for nuclear FGF-2 and suggest
that LMW FGF-2 represents the biological messenger in both the
autocrine/paracrine and intracrine FGF-2 pathways.
Kaplan Cancer
Center and the Raymond and Beverly Sackler Foundation
Laboratory, New York University Medical Center, New York, New York
10016; and §CIBLEX Corporation, San Diego, California
92121
Corresponding author. E-mail address:
aresem01{at}mcrcr.med.nyu.edu.
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