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Epac2-Dependent Rap1 Activation and the Control of Islet Insulin Secretion by Glucagon-Like Peptide-1
Open accessAbstract
Glucagon-like peptide-1 (GLP-1) binds its Class II G protein-coupled receptor to stimulate cyclic adenosine monophosphate (cAMP) production and to potentiate the glucose metabolism-dependent secretion of insulin from pancreatic β cells located within the islets of Langerhans. Prior clinical studies demonstrate that this cAMP-mediated action of GLP-1 to potentiate glucose-stimulated insulin secretion (GSIS) is of major therapeutic importance when evaluating the abilities of GLP-1 receptor (GLP-1R) agonists to lower levels of blood glucose in type 2 diabetic subjects. Surprisingly, recent in vitro studies of human or rodent islets of Langerhans provide evidence for the existence of a noncanonical mechanism of β cell cAMP signal transduction, one that may explain how GLP-1R agonists potentiate GSIS. What these studies demonstrate is that a cAMP-regulated guanine nucleotide exchange factor designated as Epac2 couples β cell cAMP production to the protein kinase A-independent stimulation of insulin exocytosis. Provided here is an overview of the Epac2 signal transduction system in β cells, with special emphasis on Rap1, a Ras-related GTPase that is an established target of Epac2.
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Metabolism-cAMP coupling involves conversion of ATP into cAMP by adenylate cyclase, which activates protein kinase A and Epac2.
“Metabolism–cAMP coupling refers to the signaling cascade that occurs after the conversion of ATP, which is generated during intracellular glucose metabolism, into cAMP by adenylate cyclase (AC),53 which in turn activates protein kinase A (PKA)54 and cAMP-regulated guanine nucleotide exchange factors, also referred to as exchange protein directly activated by cAMP (Epac) 2.55, 56”
From Pancreatic regulation of glucose homeostasis. (2016) · cites this paper as [56]
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References 96 · Cited by 76
Research works printed but not linked: 1
- Kelly, 2010, Rap1 promotes multiple pancreatic islet cell functions and signals through mTOR complex 1 to enhance proliferation, J. Biol. Chem., Mar 25
Metadata
- Authors
- Leech, C. A., Chepurny, O. G., & Holz, G. G.
- Affiliations
- SUNY Upstate Medical University (US)
- Venue
- Vitamins & Hormones
- Publisher
- Elsevier
- Published
- 2010
- Volume
- 84
- Pages
- 279-302
- ISSN
- 0083-6729 (ISSN-L)
- PMC
- PMC3009389
- OpenAlex
- W1573925283
- Cited by
- 76
- References
- 96
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 3 · 2023: 6 · 2022: 3 · 2021: 8 · 2020: 2 · 2019: 5 · 2018: 5 · 2017: 1 · 2016: 5 · 2015: 5 · 2014: 7 · 2013: 6 · 2012: 7
- FWCI
- 54.60
- Type
- book chapter
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Vitamins and hormones (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-045817, R01DK045817, R01DK069575, DK069575, R01DK052166)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Keywords
- Epac2, Rap1, glucagon-like peptide-1, GLP-1 receptor, glucose-stimulated insulin secretion, pancreatic beta cells, cAMP signaling, guanine nucleotide exchange factor, insulin exocytosis, type 2 diabetes, GLP-1 receptor agonists
- MeSH terms
- Glucagon-Like Peptide-1 Receptor, Animals, Humans, Receptors, Glucagon, Guanine Nucleotide Exchange Factors, rap1 GTP-Binding Proteins, Insulin-Secreting Cells, Glucagon-Like Peptide 1
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