描述：
FGF basic (FGF-2, HBGF-2) is one of at least 22 mitogenic proteins of the FGF family, which
show 35 60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal
peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell
surface heparan sulfate proteoglycans (HSPG) are likely. The predicted 18 kDa FGF basic
isoform can be located in both the cytoplasm and the nucleus and is presumed to be the
form secreted. Transcription from alternate start sites produces 21-23 kDa forms found only
in the nucleus. High and low molecular weight human FGF basic targets the expression of
different genes when expressed in NIH-3T3 cells. The 18 kDa rat sequence has 98% amino
acid (aa) identity with mouse, and 96 -97% aa identity with human, bovine and sheep FGF
basic. Autocrine, intracrine and paracrine actions of FGF basic have been identified. Binding
of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation
of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids
with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse
FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF
family members. FGF basic modulates such normal processes as angiogenesis, wound healing
and tissue repair, embryonic development and differentiation, neuronal function and neural
degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and
angiogenesis reminiscent of a variety of pathological conditions.
原厂资料：
FGF basic (FGF-2, HBGF-2) is one of at least 22 mitogenic proteins of the FGF family, which
show 35 60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal
peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell
surface heparan sulfate proteoglycans (HSPG) are likely. The predicted 18 kDa FGF basic
isoform can be located in both the cytoplasm and the nucleus and is presumed to be the
form secreted. Transcription from alternate start sites produces 21-23 kDa forms found only
in the nucleus. High and low molecular weight human FGF basic targets the expression of
different genes when expressed in NIH-3T3 cells. The 18 kDa rat sequence has 98% amino
acid (aa) identity with mouse, and 96 -97% aa identity with human, bovine and sheep FGF
basic. Autocrine, intracrine and paracrine actions of FGF basic have been identified. Binding
of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation
of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids
with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse
FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF
family members. FGF basic modulates such normal processes as angiogenesis, wound healing
and tissue repair, embryonic development and differentiation, neuronal function and neural
degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and
angiogenesis reminiscent of a variety of pathological conditions.
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