ArticleInternational journal of molecular sciences2025
A Novel Recombinant Human FGF21 Analog with High Glycosylation Has a Prolonged Half-Life and Affects Glycemic and Body Weight Control.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Fibroblast growth factor 21 (FGF21), a hormone-like protein, plays a crucial role in enhancing glucose and lipid metabolism, offering promising therapeutic avenues for conditions such as nonalcoholic steatohepatitis and severe hypertriglyceridemia. Despite its potential, this protein's limited stability and brief half-life pose significant challenges for its use in clinical settings. In this study, we created an FGF21 analog (named FGF21-164) that is a mutant of FGF21 and fused it with the tandem repeat sequence of human CD164. FGF21-164, characterized by extensive glycosylation and sialylation, exhibits enhanced pharmacokinetic properties, particularly in terms of its significantly longer half-life compared to its native form. The in vitro efficacy of FGF21-164 was evaluated using 3T3-L1-induced adipocytes. The protein demonstrated a dose-dependent increase in glucose uptake and effectively decreased lipid droplet accumulation surrounding the adipocytes. The in vivo activity of FGF21-164 was evaluated in
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