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cAMP-PKA dependent ERK1/2 activation is necessary for vanillic acid potentiated glucose-stimulated insulin secretion in pancreatic β-cells.

IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore

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Relation http://ir.cftri.com/14118/
https://doi.org/10.1016/j.jff.2019.02.047
 
Title cAMP-PKA dependent ERK1/2 activation is necessary for vanillic acid potentiated glucose-stimulated insulin secretion in pancreatic β-cells.
 
Creator Mahendra, V. P.
Devendra, J. Haware
Ravi, Kumar
 
Subject 10 Plants
04 Diabetes Mellitus
 
Description Vanillic acid (VA), a dietary phenolic compound is generally studied for its anti-oxidative and anti-inflammatory effects. However, the effect of VA on insulin secretion and its mechanism of action has never been explored. In this study, we report that VA augments glucose-stimulated insulin secretion (GSIS) in both insulin-secreting cellline INS-1 and isolated rat pancreatic islets. Potentiation of GSIS is accompanied by a concurrent increase in 3′,5′-cyclic adenosine monophosphate (cAMP) and activation of protein kinase A (PKA) in INS-1 and rat islets. The activated cAMP-PKA pathway, in turn, phosphorylates extracellular signal-regulated kinases 1/2 (ERK1/2) in INS-1 cells. Pharmacological intervention with PKA and ERK1/2 inhibitors revealed that VA potentiated GSIS is primarily dependent on PKA mediated ERK1/2 activity. These findings demonstrated that VA directly acts on insulin-secreting pancreatic β-cells to exert its insulinotropic effect thereby providing a novel role of VA in the regulation of insulin secretion.
 
Publisher Elsevier
 
Date 2019
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/14118/1/Journal%20of%20Functional%20Foods%2056%20%282019%29%20110%E2%80%93118.pdf
Mahendra, V. P. and Devendra, J. Haware and Ravi, Kumar (2019) cAMP-PKA dependent ERK1/2 activation is necessary for vanillic acid potentiated glucose-stimulated insulin secretion in pancreatic β-cells. Journal of Functional Foods, 56. pp. 110-118. ISSN 1756-4646