Literature DB >> 22820165

Expression of NADPH oxidase in human pancreatic islets.

Eduardo Rebelato1, Thiago R Mares-Guia, Maria Fernanda R Graciano, Letícia Labriola, Luiz R G Britto, Humberto M Garay-Malpartida, Rui Curi, Mari C Sogayar, Angelo R Carpinelli.   

Abstract

AIMS: NADPH oxidase (NOX) is a known source of superoxide anions in phagocytic and non-phagocytic cells. In this study, the presence of this enzyme in human pancreatic islets and the importance of NADPH oxidase in human β-cell function were investigated. MAIN METHODS AND KEY
FINDINGS: In isolated human pancreatic islets, the expression of NADPH oxidase components was evidenced by real-time PCR (p22(PHOX), p47(PHOX) and p67(PHOX)), Western blotting (p47(PHOX) and p67(PHOX)) and immunohistochemistry (p47(PHOX), p67(PHOX) and gp91(PHOX)). Immunohistochemistry experiments showed co-localization of p47(PHOX), p67(PHOX) and gp91(PHOX) (isoform 2 of NADPH oxidase-NOX2) with insulin secreting cells. Inhibition of NADPH oxidase activity impaired glucose metabolism and glucose-stimulated insulin secretion. SIGNIFICANCE: These findings demonstrate the presence of the main intrinsic components of NADPH oxidase comprising the NOX2 isoform in human pancreatic islets, whose activity also contributes to human β-cell function.
Copyright © 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID: 22820165     DOI: 10.1016/j.lfs.2012.07.004

Source DB:  PubMed          Journal:  Life Sci        ISSN: 0024-3205            Impact factor:   5.037


  11 in total

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