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Commentary

FAP finds FGF21 easy to digest

Matthew P. Gillum, Matthew J. Potthoff
Biochemical Journal Apr 26, 2016, 473 (9) 1125-1127; DOI: 10.1042/BCJ20160004
Matthew P. Gillum
Section for Liver Metabolism and Metabolic Imaging, the Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, 2200 Copenhagen, DenmarkDepartment of Biomedical Sciences, the Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, 2200 Copenhagen, Denmark
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  • For correspondence: gillum@sund.ku.dkmatthew-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.
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  • Circulating FGF21 proteolytic processing mediated by fibroblast activation protein

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.

  • dipeptidyl peptidase IV (DPP-IV)
  • fibroblast activation protein (FAP)
  • fibroblast growth factor 21 (FGF21)
  • proteolytic cleavage
  • Abbreviations

    DPP-IV,
    dipeptidyl peptidase IV;
    FAP,
    fibroblast activation protein;
    FGF21,
    fibroblast growth factor 21;
    FGFR1,
    fibroblast growth factor receptor 1;
    GLP-1,
    glucagon-like peptide-1;
    hFGF21,
    human FGF21
    • © 2016 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
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    May 2016

    Volume: 473 Issue: 9

    Biochemical Journal: 473 (9)
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    FAP finds FGF21 easy to digest
    Matthew P. Gillum, Matthew J. Potthoff
    Biochemical Journal May 2016, 473 (9) 1125-1127; DOI: 10.1042/BCJ20160004
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    FAP finds FGF21 easy to digest
    Matthew P. Gillum, Matthew J. Potthoff
    Biochemical Journal May 2016, 473 (9) 1125-1127; DOI: 10.1042/BCJ20160004

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    Keywords

    dipeptidyl peptidase IV (DPP-IV)
    fibroblast activation protein (FAP)
    fibroblast growth factor 21 (FGF21)
    proteolytic cleavage

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