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An Acetate-Specific GPCR, FFAR2, Regulates Insulin Secretion.

Medha Priyadarshini1, Stephanie R Villa1, Miles Fuller1

  • 1Division of Endocrinology, Metabolism, and Molecular Medicine (M.P., S.R.V., M.F., B.T.L.), Northwestern University, Chicago, Illinois 60611; Kovler Diabetes Center (B.W.), The University of Chicago, Chicago, Illinois 60637; Monash University (C.R.M.), Clayton, Victoria 3800, Australia; Montreal Diabetes Research Center, Centre de Recherche du Centre Hospitalier de l'Université de Montréal, and Department of Medicine (T.A., V.P.), University of Montreal, Quebec, H2X 0A9 Canada; Multispan (H.M.), Hayward, California 94545; Department of Pediatrics and the Herman B Wells Center for Pediatric Research (R.G.M.), Indiana University School of Medicine, Indianapolis, Indiana 4602; Department of Biochemistry and Molecular Biology (R.G.M.), Indiana University School of Medicine, Indianapolis, Indiana 46202; Department of Medicine (R.G.M.), Indiana University School of Medicine, Indianapolis, Indiana 46202; Department of Pharmaceutical Sciences (A.G.), Midwestern University, Downers Grove, Illinois 60515; and Jesse Brown Veterans Affairs Medical Center (B.T.L.), Chicago, Illinois 60612.

Molecular Endocrinology (Baltimore, Md.)
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Summary

Free fatty acid receptor 2 (FFAR2) plays a complex role in glucose-stimulated insulin secretion (GSIS). Its signaling can either enhance or inhibit insulin release, with distinct responses between mouse and human receptors.

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Area of Science:

  • Endocrinology
  • Metabolic Research
  • G protein-coupled receptor signaling

Background:

  • G protein-coupled receptors (GPCRs) regulate glucose-stimulated insulin secretion (GSIS).
  • Free fatty acid receptor 2 (FFAR2), a short-chain fatty acid sensor, is present in pancreatic β-cells and its expression changes with insulin resistance in rodents.
  • The precise role of FFAR2 in GSIS requires further investigation.

Purpose of the Study:

  • To investigate the role of FFAR2 in regulating GSIS.
  • To determine how FFAR2 activation by its ligand acetate and specific agonists affects insulin secretion.
  • To compare the signaling properties of mouse and human FFAR2.

Main Methods:

  • Phenotypic analysis of wild-type and Ffar2(-/-) mice.
  • In vivo glucose homeostasis assessment on normal and high-fat diets.
  • Ex vivo studies of insulin secretion from mouse and human islets.
  • Analysis of FFAR2 signaling pathways (Gαq/11 and Gαi/o).

Main Results:

  • No significant differences in glucose homeostasis between wild-type and Ffar2(-/-) mice.
  • Marginally significant defect in insulin secretion in Ffar2(-/-) mice during hyperglycemic clamps.
  • Diminished GSIS from Ffar2(-/-) islets ex vivo.
  • Acetate potentiated GSIS in a FFAR2-dependent manner.
  • FFAR2 agonists differentially modulated GSIS via Gαq/11 (potentiation) or Gαi/o (inhibition).
  • Significant differences observed in the response of human FFAR2 to acetate and agonists compared to mouse FFAR2.

Conclusions:

  • FFAR2 signaling involves divergent G protein pathways, capable of selectively potentiating or inhibiting GSIS in mouse islets.
  • Significant species-specific differences exist in FFAR2 response to agonists, impacting its potential as a therapeutic target for type 2 diabetes.