FAP finds FGF21 easy to digest

Research

FAP finds FGF21 easy to digest

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FAP finds FGF21 easy to digest. / Gillum, Matthew P; Potthoff, Matthew J.

In: Biochemical Journal, Vol. 473, No. 9, 01.05.2016, p. 1125-7.

Research output: Contribution to journal › Comment/debate › Research › peer-review

Harvard

Gillum, MP & Potthoff, MJ 2016, 'FAP finds FGF21 easy to digest', Biochemical Journal, vol. 473, no. 9, pp. 1125-7. https://doi.org/10.1042/BCJ20160004

APA

Gillum, M. P., & Potthoff, M. J. (2016). FAP finds FGF21 easy to digest. Biochemical Journal, 473(9), 1125-7. https://doi.org/10.1042/BCJ20160004

Vancouver

Gillum MP, Potthoff MJ. FAP finds FGF21 easy to digest. Biochemical Journal. 2016 May 1;473(9):1125-7. https://doi.org/10.1042/BCJ20160004

Author

Gillum, Matthew P ; Potthoff, Matthew J. / FAP finds FGF21 easy to digest. In: Biochemical Journal. 2016 ; Vol. 473, No. 9. pp. 1125-7.

Bibtex

@article{c0ecad1b78d8425fb0670216cd0bb0f5,

title = "FAP finds FGF21 easy to digest",

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.",

keywords = "Journal Article",

author = "Gillum, {Matthew P} and Potthoff, {Matthew J}",

note = "{\textcopyright} 2016 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.",

year = "2016",

month = may,

day = "1",

doi = "10.1042/BCJ20160004",

language = "English",

volume = "473",

pages = "1125--7",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

number = "9",

}

RIS

TY - JOUR

T1 - FAP finds FGF21 easy to digest

AU - Gillum, Matthew P

AU - Potthoff, Matthew J

PY - 2016/5/1

Y1 - 2016/5/1

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1042/BCJ20160004

DO - 10.1042/BCJ20160004

M3 - Comment/debate

C2 - 27118870

VL - 473

SP - 1125

EP - 1127

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 9

ER -

ID: 166944913