描述：
Fibroblast growth factor 23 (FGF-23) is a 30-32 kDa member of the FGF family, within a
subfamily that also includes FGF-19 and FGF-21. FGF proteins contain a 120 amino acid (aa)
core FGF domain that exhibits a β-trefoil structure. FGF-19 subfamily members are highly
diffusible molecules owing to their poor ECM/heparin sulfate binding and plasmastabilizing
intramolecular folds. Mature human FGF-23 contains an atypical (very low affinity) heparin
binding site (aa 134-162), a proteolytic cleavage site (Arg179-Ser180), and multiple Olinked
glycosylation sites with Thr178 being of particular importance.O-linked glycosylation at Thr178
blocks the cleavage of FGF-23, thereby preventing loss of FGF-23 activity. Mature human
FGF-23 shows 72% aa identity to mouse FGF-23 and is active on mouse cells. FGF-23 exerts its
effects through a ternary complex that includes Klotho and an FGF receptor (FGF R4 or the "c"
isoforms of FGF R1 or FGF R3). Klotho has a restricted distribution that limits FGF-23 activity.
FGF-23 is produced by osteocytes and osteoblasts in response to high circulating phosphate
levels, elevated parathyroid hormone, and circulatory volume loading. It functions as an
endocrine phosphatonin by suppressing circulating phosphate levels. FGF-23 interaction with
renal proximal tubular epithelium decreases the renal resorption of phosphate by
downregulating phosphate transportersand by suppressing vitamin D production. It also
decreases the intestinal absorption of phosphate.
原厂资料：
Fibroblast growth factor 23 (FGF-23) is a 30-32 kDa member of the FGF family, within a
subfamily that also includes FGF-19 and FGF-21. FGF proteins contain a 120 amino acid (aa)
core FGF domain that exhibits a β-trefoil structure. FGF-19 subfamily members are highly
diffusible molecules owing to their poor ECM/heparin sulfate binding and plasmastabilizing
intramolecular folds. Mature human FGF-23 contains an atypical (very low affinity) heparin
binding site (aa 134-162), a proteolytic cleavage site (Arg179-Ser180), and multiple Olinked
glycosylation sites with Thr178 being of particular importance.O-linked glycosylation at Thr178
blocks the cleavage of FGF-23, thereby preventing loss of FGF-23 activity. Mature human
FGF-23 shows 72% aa identity to mouse FGF-23 and is active on mouse cells. FGF-23 exerts its
effects through a ternary complex that includes Klotho and an FGF receptor (FGF R4 or the "c"
isoforms of FGF R1 or FGF R3). Klotho has a restricted distribution that limits FGF-23 activity.
FGF-23 is produced by osteocytes and osteoblasts in response to high circulating phosphate
levels, elevated parathyroid hormone, and circulatory volume loading. It functions as an
endocrine phosphatonin by suppressing circulating phosphate levels. FGF-23 interaction with
renal proximal tubular epithelium decreases the renal resorption of phosphate by
downregulating phosphate transportersand by suppressing vitamin D production. It also
decreases the intestinal absorption of phosphate.
京公网安备11010802025653 版权所有：北京逸优科技有限公司
