FGF19 as a postprandial, insulin-independent activator of hepatic protein and glycogen synthesis

Serkan Kir, Sara A. Beddow, Varman T. Samuel, Paul Miller, Stephen F. Previs, Kelly Suino-Powell, H. Eric Xu, Gerald I. Shulman, Steven A. Kliewer, David J. Mangelsdorf

Research output: Contribution to journalArticle

320 Scopus citations

Abstract

Fibroblast growth factor (FGF) 19 is an enterokine synthesized and released when bile acids are taken up into the ileum. We show that FGF19 stimulates hepatic protein and glycogen synthesis but does not induce lipogenesis. The effects of FGF19 are independent of the activity of either insulin or the protein kinase Akt and, instead, are mediated through a mitogen-activated protein kinase signaling pathway that activates components of the protein translation machinery and stimulates glycogen synthase activity. Mice lacking FGF15 (the mouse FGF19 ortholog) fail to properly maintain blood concentrations of glucose and normal postprandial amounts of liver glycogen. FGF19 treatment restored the loss of glycogen in diabetic animals lacking insulin. Thus, FGF19 activates a physiologically important, insulin-independent endocrine pathway that regulates hepatic protein and glycogen metabolism.

Original languageEnglish (US)
Pages (from-to)1621-1624
Number of pages4
JournalScience
Volume331
Issue number6024
DOIs
StatePublished - Mar 25 2011

ASJC Scopus subject areas

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    Kir, S., Beddow, S. A., Samuel, V. T., Miller, P., Previs, S. F., Suino-Powell, K., Xu, H. E., Shulman, G. I., Kliewer, S. A., & Mangelsdorf, D. J. (2011). FGF19 as a postprandial, insulin-independent activator of hepatic protein and glycogen synthesis. Science, 331(6024), 1621-1624. https://doi.org/10.1126/science.1198363