描述：
FGF acidic, also known as FGF-1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member
of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types,
stimulates the proliferation of all cells of mesodermal origin and many cells of
neuroectodermal, ectodermal, and endodermal origin. Itplays a number of roles in
development, regeneration, and angiogenesis. Bovine FGF acidic shares 53% amino acid
sequence identity with FGF basic and 11% -31% with other bovine FGFs. It shares 92%, 91%,
88%, and 91% aa sequence identity with human, mouse, porcine, and rat FGF acidic,
respectively, and exhibits considerable species crossreactivity. During its nonclassical
secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of
synaptotagmin 1. It is released extracellularly as a disulfidelinked homodimer and is stored
in complex with extracellular heparan sulfate. The ability of heparan sulfate to bind FGF
acidic is determined by its pattern of sulfation, and alterations in this pattern during
embryognesis thereby regulate FGF acidic bioactivity. The association of FGF acidic with
heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors . Ligation
triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF
complexes. Internalized FGF acidic can translocate to the cytosol with the assistance of
Hsp90 and then migrate to the nucleusby means of its two nuclear localization signals. The
phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol
where it is dephosphorylated and degraded. Intracellular FGF acidic functions as a survival
factor by inhibiting p53 activity and proapoptotic signaling.
原厂资料：
FGF acidic, also known as FGF-1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member
of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types,
stimulates the proliferation of all cells of mesodermal origin and many cells of
neuroectodermal, ectodermal, and endodermal origin. Itplays a number of roles in
development, regeneration, and angiogenesis. Bovine FGF acidic shares 53% amino acid
sequence identity with FGF basic and 11% -31% with other bovine FGFs. It shares 92%, 91%,
88%, and 91% aa sequence identity with human, mouse, porcine, and rat FGF acidic,
respectively, and exhibits considerable species crossreactivity. During its nonclassical
secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of
synaptotagmin 1. It is released extracellularly as a disulfidelinked homodimer and is stored
in complex with extracellular heparan sulfate. The ability of heparan sulfate to bind FGF
acidic is determined by its pattern of sulfation, and alterations in this pattern during
embryognesis thereby regulate FGF acidic bioactivity. The association of FGF acidic with
heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors . Ligation
triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF
complexes. Internalized FGF acidic can translocate to the cytosol with the assistance of
Hsp90 and then migrate to the nucleusby means of its two nuclear localization signals. The
phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol
where it is dephosphorylated and degraded. Intracellular FGF acidic functions as a survival
factor by inhibiting p53 activity and proapoptotic signaling.
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