Abstract
The biology of autophagy in health and disease conditions has been intensively analyzed for decades. Several potential interventions can induce autophagy in preclinical research; however, none of these interventions are ready for translation to clinical practice yet. The topic of the current review is the molecular regulation of autophagy by glucagon, glucagon-like peptide (GLP)-1 and the GLP-1-degrading enzyme dipeptidyl peptidase-4 (DPP-4). Glucagon is a well-known polypeptide that induces autophagy. In contrast, GLP-1 has been shown to inhibit glucagon secretion; GLP-1 also has been related to the induction of autophagy. DPP-4 inhibitors can induce autophagy in a GLP-1–dependent manner, but other diverse effects could be relevant. Here, we analyze the distinct molecular regulation of autophagy by glucagon, GLP-1, and DPP-4 inhibitors. Additionally, the potential contribution to autophagy by glucagon and GLP-1 after bariatric surgery is discussed.
Highlights
Recent advances with incretin-based drugs have opened new avenues in the management of diabetes
We investigated the potential involvement of autophagy induction by glucagon-like peptide (GLP)-1 and incretin-based dugs
We focused on glucagon, a known polypeptide that regulates glucose levels and a classic molecule that induces autophagy
Summary
Recent advances with incretin-based drugs have opened new avenues in the management of diabetes. Regulation of the Gcg transcription process is not completely known and distinct pattern of mRNA expression has been reported in intestinal endocrine cells and in pancreatic islet α-cells (Jin, 2008; Yi et al, 2008; Chiang et al, 2012; Muller et al, 2017) In addition to such unique transcriptional control in each cell type, posttranslational processing of prohormone plays an important role in the major cell types producing ProG peptides. In addition to glucagon and GLP-1, glucagon-like peptide-2 (GLP-2), oxyntomodulin, glicentin, glicentin-related pancreatic polypeptide (GRPP), and major proglucagon fragment (MPGF) are synthesized from ProG; the specific biological function of some of these fragments has not been identified (Figure 1) Such posttranslational regulation of these ProG peptides in their respective cell types relies on tissue-specific posttranslational modification by prohormone convertases (PCs).
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