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A role for Glucagon-Like Peptide-1 in the regulation of β-cell autophagy

Lookup NU author(s): Dr Catherine ArdenORCiD

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This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (CC BY-NC-ND).

Abstract

© 2017 Elsevier Inc. Autophagy is a highly conserved intracellular recycling pathway that serves to recycle damaged organelles/proteins or superfluous nutrients during times of nutritional stress to provide energy to maintain intracellular homeostasis and sustain core metabolic functions. Under these conditions, autophagy functions as a cell survival mechanism but impairment of this pathway can lead to pro-death stimuli. Due to their role in synthesising and secreting insulin, pancreatic β-cells have a high requirement for robust degradation pathways. Recent research suggests that functional autophagy is required to maintain β-cell survival and function in response to high fat diet suggesting a pro-survival role. However, a role for autophagy has also been implicated in the pathogenesis of type 2 diabetes. Thus, the pro-survival vs pro-death role of autophagy in regulating β-cell mass requires discussion. Emerging evidence suggests that Glucagon-Like Peptide-1 (GLP-1) may exert beneficial effects on glucose homeostasis via autophagy-dependent pathways both in pancreatic β-cells and in other cell types. The aim of the current review is to: i) summarise the literature surrounding β-cell autophagy and its pro-death vs pro-survival role in regulating β-cell mass; ii) review the literature describing the impact of GLP-1 on β-cell autophagy and in other cell types; iii) discuss the potential underlying mechanisms.

Publication metadata

Author(s): Arden C

Publication type: Article

Publication status: Published

Journal: Peptides

Year: 2018

Volume: 100

Pages: 85-93

Print publication date: 01/02/2018

Online publication date: 03/02/2018

Acceptance date: 04/12/2017

Date deposited: 05/03/2018

ISSN (print): 0196-9781

ISSN (electronic): 1873-5169

Publisher: Elsevier Inc.

URL: https://doi.org/10.1016/j.peptides.2017.12.002

DOI: 10.1016/j.peptides.2017.12.002

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