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- W3156232654 endingPage "318" @default.
- W3156232654 startingPage "299" @default.
- W3156232654 abstract "The fibroblast growth factor 23 (FGF23) hormone is a key regulator of mineral ion homeostasis. Its metabolic activity depends on α-Klotho, an aging suppressor protein. A weak binding affinity for the glycosaminoglycan heparan sulfate enables FGF23 to function as a hormone, while its weak binding affinity for FGF receptors (FGFRs) protects FGF23 against inadvertent off-target signaling. α-Klotho concurrently recruits FGF23 by its unique C-terminal tail and FGFR by its immunoglobulin-like D3 domain and thereby brings FGF23 in close proximity of FGFR to enable stable FGF23–FGFR binding. Shed, soluble α-Klotho is not a hormone with glycosidase activity, as widely claimed, but just like membrane-bound α-Klotho, it is a scaffold protein specialized to recruit FGF23 and FGFR. As such, soluble α-Klotho might promote, rather than counteract, left ventricular hypertrophy in advanced chronic kidney disease (CKD). Inhibiting soluble α-Klotho from FGF23 binding thus warrants consideration as an intervention into excess FGF23 signaling in CKD." @default.
- W3156232654 created "2021-04-26" @default.
- W3156232654 creator A5009036115 @default.
- W3156232654 creator A5031474465 @default.
- W3156232654 creator A5064779039 @default.
- W3156232654 creator A5069612025 @default.
- W3156232654 date "2021-01-01" @default.
- W3156232654 modified "2023-10-14" @default.
- W3156232654 title "Structural basis of FGF23 hormone signaling" @default.
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