Artículos de revistas
Expression of NADPH oxidase in human pancreatic islets
Fecha
2012Registro en:
LIFE SCIENCES, OXFORD, v. 91, n. 41493, supl. 1, Part 3, pp. 244-249, SEP 17, 2012
0024-3205
10.1016/j.lfs.2012.07.004
Autor
Oliveira, Eduardo Rebelato Lopes de
Guia, Thiago Rennó dos Mares
Graciano, Maria Fernanda Rodrigues
Labriola, Leticia
Britto, Luiz Roberto Giorgetti de
Malpartida, Humberto Miguel Garay
Curi, Rui
Sogayar, Mari Cleide
Carpinelli, Angelo Rafael
Institución
Resumen
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 beta-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 beta-cell function. (C) 2012 Elsevier Inc. All rights reserved.