描述:
Fibroblast growth factor 16 (FGF16) belongs to the large FGF family which has at least 23
members . All FGF family members are heparinbinding growth factors with a core 120 amino
acid (aa) FGF domain that allows for a common tertiary structure. FGFs are expressed during
embryonic development and in restricted adult tissues. They act on cells of mesodermal and
neuroectodermal origin to regulate diverse physiologic functions including angiogenesis, cell
growth, pattern formation, embryonic development, metabolic regulation, cell migration,
neurotrophic effects and tissue repair. Signaling receptors for FGFs are type I transmembrane
receptor tyrosine kinases belonging to the immunoglobulin (Ig) superfamily. Four distinct
but related classes of FGF receptors, FGF R1, 2, 3, and 4, exist. Through alternative splicing,
multiple isoforms for FGF R1, 2 and 3, with distinct ligand recognition profiles, are also
generated.FGF16 was originally identified in rat heart tissue by homology based polymerase
chain reaction. Human FGF16 cDNA predicts a 207 aa precursor protein with one Nlinked
glycosylation site. FGF16 lacks a typical signal peptide, but is efficiently generated by
mechanisms other than the classical protein secretion pathway. Among FGF family members,
FGF16 is most similar to FGF9, sharing 73% aa sequence homology. Human FGF16 shares
99% and 98.6% aa sequence identity with the mouse and rat FGF16, respectively. In rat
embryos, FGF16 message is expressed predominantly in brown adipocytes. In adult animals,
it is localized primarily in heart tissue. FGF16 binds to and activates FGF receptor 4. FGF16
induces proliferation of primary adipocytes and oligodendrocytes in vitro and stimulates
liver weight increase in vivo. The expression pattern of FGF16 and its effect on adipocyte
proliferation suggest a role for this protein on the proliferation of embryonic brown adipose
tissue.
原厂资料:
Fibroblast growth factor 16 (FGF16) belongs to the large FGF family which has at least 23
members . All FGF family members are heparinbinding growth factors with a core 120 amino
acid (aa) FGF domain that allows for a common tertiary structure. FGFs are expressed during
embryonic development and in restricted adult tissues. They act on cells of mesodermal and
neuroectodermal origin to regulate diverse physiologic functions including angiogenesis, cell
growth, pattern formation, embryonic development, metabolic regulation, cell migration,
neurotrophic effects and tissue repair. Signaling receptors for FGFs are type I transmembrane
receptor tyrosine kinases belonging to the immunoglobulin (Ig) superfamily. Four distinct
but related classes of FGF receptors, FGF R1, 2, 3, and 4, exist. Through alternative splicing,
multiple isoforms for FGF R1, 2 and 3, with distinct ligand recognition profiles, are also
generated.FGF16 was originally identified in rat heart tissue by homology based polymerase
chain reaction. Human FGF16 cDNA predicts a 207 aa precursor protein with one Nlinked
glycosylation site. FGF16 lacks a typical signal peptide, but is efficiently generated by
mechanisms other than the classical protein secretion pathway. Among FGF family members,
FGF16 is most similar to FGF9, sharing 73% aa sequence homology. Human FGF16 shares
99% and 98.6% aa sequence identity with the mouse and rat FGF16, respectively. In rat
embryos, FGF16 message is expressed predominantly in brown adipocytes. In adult animals,
it is localized primarily in heart tissue. FGF16 binds to and activates FGF receptor 4. FGF16
induces proliferation of primary adipocytes and oligodendrocytes in vitro and stimulates
liver weight increase in vivo. The expression pattern of FGF16 and its effect on adipocyte
proliferation suggest a role for this protein on the proliferation of embryonic brown adipose
tissue.