Abstract
Fibroblast growth factor 21 (FGF21) is an endocrine hormone that regulates carbohydrate and lipid metabolism. In humans, circulating FGF21 is inactivated by proteolytic cleavage of its C-terminus, thereby preventing signalling through a receptor complex. The mechanism for this cleavage event and the factors contributing to the post-translational regulation of FGF21 activity has previously been unknown. In a recent issue of the Biochemical Journal, Zhen et al. have identified fibroblast activation protein (FAP) as the endopeptidase responsible for this site-specific cleavage of human FGF21 (hFGF21), and propose that inhibition of FAP may be a therapeutic strategy to increase endogenous levels of active FGF21.
Originalsprog | Engelsk |
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Tidsskrift | Biochemical Journal |
Vol/bind | 473 |
Udgave nummer | 9 |
Sider (fra-til) | 1125-7 |
Antal sider | 3 |
ISSN | 0264-6021 |
DOI |
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Status | Udgivet - 1 maj 2016 |