
FAP finds FGF21 easy to digest
Author(s) -
Matthew P. Gillum,
Matthew J. Potthoff
Publication year - 2016
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bcj20160004
Subject(s) - fgf21 , cleavage (geology) , fibroblast growth factor , receptor , hormone , endogeny , fibroblast activation protein, alpha , biology , biochemistry , microbiology and biotechnology , chemistry , genetics , paleontology , fracture (geology) , cancer
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.