描述：
FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show
35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the
family, lack signal peptides and are apparently secreted by mechanisms other than the
classical protein secretion pathway. FGF basic has been isolated from a number of sources,
including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor
contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating
that disulfide bonds are not required for this activity. A variety of forms of FGF basic are
produced as a result of N-terminal extensions. These extensions affect localization of FGF
basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin
or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity
FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and
show a similar range of biological activities. FGF basic stimulates the proliferation of all cells
of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin.
FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates
embryonic development and differentiation. These observed in vitro functions of FGF basic
suggest FGF basic may play a role in vivo in the modulation of such normal processes as
angiogenesis, wound healing and tissue repair, embryonic development and differentiation,
and neuronal function and neural degeneration. Additionally, FGF basic may participate in the
production of a variety of pathological conditions resulting from excessive cell proliferation and
excessive angiogenesis.
原厂资料：
FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show
35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the
family, lack signal peptides and are apparently secreted by mechanisms other than the
classical protein secretion pathway. FGF basic has been isolated from a number of sources,
including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor
contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating
that disulfide bonds are not required for this activity. A variety of forms of FGF basic are
produced as a result of N-terminal extensions. These extensions affect localization of FGF
basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin
or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity
FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and
show a similar range of biological activities. FGF basic stimulates the proliferation of all cells
of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin.
FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates
embryonic development and differentiation. These observed in vitro functions of FGF basic
suggest FGF basic may play a role in vivo in the modulation of such normal processes as
angiogenesis, wound healing and tissue repair, embryonic development and differentiation,
and neuronal function and neural degeneration. Additionally, FGF basic may participate in the
production of a variety of pathological conditions resulting from excessive cell proliferation and
excessive angiogenesis.
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