描述：
FGF-9 (fibroblast growth factor-9), also called HBGF-9 (heparinbinding growth factor-9)
and GAF (glia-activating factor), is an approximately 26 kDa secreted glycoprotein of the
FGF family. FGFs exhibit heparindependent regulation of cell proliferation, differentiation,
and function, and are characterized by a core heparinbinding FGF domain of approximately
120 amino acids (aa) that exhibits a βtrefoil structure. FGF-9, -16 and -20 form a subfamily
that shares 65-71% aa sequence identity, binds FGF R3 (IIIb), and are efficiently secreted
despite having an uncleavable, bipartite signal sequence. Secreted human FGF-9 is a 205-
207 aa protein that lacks the Nterminal 13 aa and shares 98% sequence identity with mouse,
rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc
splice forms of FGF R1, R2 and R3 are variably reported. An unusual constitutive dimerization
of FGF-9 buries receptor interaction sites which lowers its activity, and increases heparin
affinity which inhibits diffusion. A spontaneous mouse mutant, Eks, interferes with
dimerization, resulting monomeric, diffusible FGF-9 that causes elbow and knee synostoses
(joint fusions) due to FGF-9 misexpression in developing joints. In humans, FGF-9 mutations
that lower receptor binding cause multiple synostoses syndrome (SYNS). Expression in
brain and kidney are reported in the adult rat. In the mouse embryo the location and timing
of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature,
digestive tract, and testes. Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia,
and causes rhizomelia, or shortening of the proximal skeleton. Altered FGF-9 expression or
function is reported in human colon, endometrial, and ovarian cancers, correlating with
progression, invasiveness, and survival.
原厂资料：
FGF-9 (fibroblast growth factor-9), also called HBGF-9 (heparinbinding growth factor-9)
and GAF (glia-activating factor), is an approximately 26 kDa secreted glycoprotein of the
FGF family. FGFs exhibit heparindependent regulation of cell proliferation, differentiation,
and function, and are characterized by a core heparinbinding FGF domain of approximately
120 amino acids (aa) that exhibits a βtrefoil structure. FGF-9, -16 and -20 form a subfamily
that shares 65-71% aa sequence identity, binds FGF R3 (IIIb), and are efficiently secreted
despite having an uncleavable, bipartite signal sequence. Secreted human FGF-9 is a 205-
207 aa protein that lacks the Nterminal 13 aa and shares 98% sequence identity with mouse,
rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc
splice forms of FGF R1, R2 and R3 are variably reported. An unusual constitutive dimerization
of FGF-9 buries receptor interaction sites which lowers its activity, and increases heparin
affinity which inhibits diffusion. A spontaneous mouse mutant, Eks, interferes with
dimerization, resulting monomeric, diffusible FGF-9 that causes elbow and knee synostoses
(joint fusions) due to FGF-9 misexpression in developing joints. In humans, FGF-9 mutations
that lower receptor binding cause multiple synostoses syndrome (SYNS). Expression in
brain and kidney are reported in the adult rat. In the mouse embryo the location and timing
of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature,
digestive tract, and testes. Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia,
and causes rhizomelia, or shortening of the proximal skeleton. Altered FGF-9 expression or
function is reported in human colon, endometrial, and ovarian cancers, correlating with
progression, invasiveness, and survival.
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