Journal
BRAIN RESEARCH
Volume 1040, Issue 1-2, Pages 178-186Publisher
ELSEVIER
DOI: 10.1016/j.brainres.2005.01.066
Keywords
p47(Phox); gp91(Phox); immunohistochemistry; rat; NADPH oxidase; brain
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NADPH oxidase is multi-component enzyme, which comprises the cytosolic proteins p40(Phox), p47(Phox), and p67(Phox) and the two membrane proteins, gp9(Phox) and p22(Phox), and which is well characterized in phagocytic cells. NADPH oxidase is a primary source of reactive oxygen species (ROS), and recent studies indicate that free radicals and ROS might be causative factors of several brain degenerative diseases and dysfunctions. However, though previous studies have shown the presence of NADPH oxidase subunits in cell culture and mouse brain, they have not provided detailed high power resolution data. Therefore, we investigated the distributions of the p47(Phox) and gp91(Phox) subunits in rat brain using immunohistochemical approach. Cortex, hippocampus, and Purkinje cells of cerebellum were prominently stained by p47(Phox) and gp91(Phox) antibodies. As compared with the distributions of p47(Phox), gp91(Phox) in mouse, some differences in the rat brain were observed in the hippocampus, thalamus, amygdala, reticular nucleus, and basal ganglia. Additionally, at the cellular level, most p47(Phox) immunoreactivity was largely confined to cell bodies and proximal portions of the dendritic tree. Taken together, the widespread observed distributions of p47(Phox) and gp91(Phox) subunits indicate that they are probably needed to maintain normal brain function. (c) 2005 Elsevier B.V. All rights reserved.
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