Document Detail


Quercetin potentiates insulin secretion and protects INS-1 pancreatic β-cells against oxidative damage via the ERK1/2 pathway.
MedLine Citation:
PMID:  20860660     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND AND PURPOSE: Quercetin lowers plasma glucose, normalizes glucose tolerance tests and preserves pancreatic β-cell integrity in diabetic rats. However, its mechanism of action has never been explored in insulin-secreting β-cells. Using the INS-1 β-cell line, the effects of quercetin were determined on glucose- or glibenclamide-induced insulin secretion and on β-cell dysfunctions induced by hydrogen peroxide (H(2)O(2)). These effects were analysed along with the activation of the extracellular signal-regulated kinase (ERK)1/2 pathway. N-acetyl-L-cysteine (NAC) and resveratrol, two antioxidants also known to exhibit some anti-diabetic properties, were used for comparison.
EXPERIMENTAL APPROACH: Insulin release was quantified by the homogeneous time resolved fluorescence method and ERK1/2 activation tested by Western blot experiments. Cell viability was estimated by the [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide] (MTT) colorimetric assay. KEY RESULTS Quercetin (20 µmol·L(-1)) potentiated both glucose (8.3 mmol·L(-1))- and glibenclamide (0.01 µmol·L(-1))-induced insulin secretion and ERK1/2 phosphorylation. The ERK1/2 (but not the protein kinase A) signalling pathway played a crucial role in the potentiation of glucose-induced insulin secretion by quercetin. In addition, quercetin (20 µmol·L(-1)), protected β-cell function and viability against oxidative damage induced by 50 µmol·L(-1) H(2)O(2) and induced a major phosphorylation of ERK1/2. In the same conditions, resveratrol or NAC were ineffective.
CONCLUSION AND IMPLICATIONS: Quercetin potentiated glucose and glibenclamide-induced insulin secretion and protected β-cells against oxidative damage. Our study suggested that ERK1/2 played a major role in those effects. The potential of quercetin in preventing β-cell dysfunction associated with diabetes deserves further investigation.
Authors:
E Youl; G Bardy; R Magous; G Cros; F Sejalon; A Virsolvy; S Richard; J F Quignard; R Gross; P Petit; D Bataille; C Oiry
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  British journal of pharmacology     Volume:  161     ISSN:  1476-5381     ISO Abbreviation:  Br. J. Pharmacol.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-09-23     Completed Date:  2010-12-02     Revised Date:  2012-05-07    
Medline Journal Info:
Nlm Unique ID:  7502536     Medline TA:  Br J Pharmacol     Country:  England    
Other Details:
Languages:  eng     Pagination:  799-814     Citation Subset:  IM    
Copyright Information:
© 2010 The Authors. British Journal of Pharmacology © 2010 The British Pharmacological Society.
Affiliation:
Université Montpellier I et CNRS UMR 5232, Centre de Pharmacologie et Innovation dans le Diabète (CPID), Montpellier, France.
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MeSH Terms
Descriptor/Qualifier:
Acetylcysteine / pharmacology
Animals
Antioxidants / pharmacology*
Cell Line
Glucose / metabolism
Glyburide / pharmacology
Hydrogen Peroxide / toxicity
Hypoglycemic Agents / pharmacology
Insulin / secretion*
Insulin-Secreting Cells / drug effects*,  metabolism
Male
Mitogen-Activated Protein Kinase 1 / metabolism
Mitogen-Activated Protein Kinase 3 / metabolism
Oxidative Stress / drug effects
Phosphorylation / drug effects
Quercetin / pharmacology*
Rats
Rats, Wistar
Signal Transduction / drug effects
Stilbenes / pharmacology
Chemical
Reg. No./Substance:
0/Antioxidants; 0/Hypoglycemic Agents; 0/Insulin; 0/Stilbenes; 10238-21-8/Glyburide; 117-39-5/Quercetin; 50-99-7/Glucose; 501-36-0/resveratrol; 616-91-1/Acetylcysteine; 7722-84-1/Hydrogen Peroxide; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.24/Mitogen-Activated Protein Kinase 3
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