FAP finds FGF21 easy to digest

Matthew P Gillum; Matthew J Potthoff

doi:10.1042/BCJ20160004

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Journal article

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FAP finds FGF21 easy to digest

Matthew P Gillum and Matthew J Potthoff

The Biochemical journal, Vol.473(9), pp.1125-1127

05/01/2016

DOI: 10.1042/BCJ20160004

PMID: 27118870

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https://www.ncbi.nlm.nih.gov/pmc/articles/7721556View

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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.

Fibroblast Growth Factors - metabolism

Gelatinases - genetics

Membrane Proteins - genetics

Proteolysis

Humans

Gelatinases - metabolism

Serine Endopeptidases - genetics

Fibroblast Growth Factors - genetics

Protein Domains

Membrane Proteins - metabolism

Serine Endopeptidases - metabolism

Details

Title: Subtitle: FAP finds FGF21 easy to digest
Creators: Matthew P Gillum - Section for Liver Metabolism and Metabolic Imaging, the Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, 2200 Copenhagen, Denmark Department of Biomedical Sciences, the Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, 2200 Copenhagen, Denmark gillum@sund.ku.dk matthew-potthoff@uiowa.edu
Matthew J Potthoff - Department of Pharmacology, University of Iowa Carver College of Medicine, Iowa City, IA 52242, U.S.A. Fraternal Order of Eagles Diabetes Research Center, University of Iowa Carver College of Medicine, Iowa City, IA 52242, U.S.A. gillum@sund.ku.dk matthew-potthoff@uiowa.edu
Resource Type: Journal article
Publication Details: The Biochemical journal, Vol.473(9), pp.1125-1127
DOI: 10.1042/BCJ20160004
PMID: 27118870
NLM abbreviation: Biochem J
ISSN: 0264-6021
eISSN: 1470-8728
Publisher: England
Language: English
Date published: 05/01/2016
Academic Unit: Neurology; Iowa Neuroscience Institute; Neuroscience and Pharmacology
Record Identifier: 9984040223202771

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