Premium
Glucose‐6‐phosphate dehydrogenase and NADPH‐consuming enzymes in the rat olfactory bulb
Author(s) -
Biagiotti Enrica,
Ferri Paola,
Dringen Ralf,
Del Grande Paolo,
Ninfali Paolino
Publication year - 2005
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20448
Subject(s) - olfactory bulb , bulb , biochemistry , biology , glucose 6 phosphate dehydrogenase , enzyme , nadph dehydrogenase , microbiology and biotechnology , oxidoreductase , dehydrogenase , chemistry , endocrinology , nitric oxide synthase , botany , central nervous system
The resistance to oxidative stress is a multifactorial reaction involving the clustering of transcriptionally regulated genes. Because glucose‐6‐phosphate dehydrogenase (G6PD), the principal enzyme responsible for reducing power, is highly expressed in the olfactory bulb (OB), it is of interest to verify whether other enzymes utilizing NADPH are also highly expressed. The level and localization of G6PD‐ and NADPH‐consuming enzymes, such as NADPH‐cytochrome P450 oxidoreductase (P450R), glutathione reductase (GR), and NADPH‐diaphorase (NADPH‐d), were analyzed in the rat olfactory bulb (OB) by quantitative histochemistry and immunohistochemistry. The highest concentration of G6PD, P450R, and GR was observed in the olfactory nerve layer (ONL), suggesting a correlation in the expression of these enzymes at the gene level. Correlation in staining intensity between G6PD and NADPH‐d activities occurred only in part of the ONL, some glomeruli, and scattered periglomerular cells. This peculiar distribution of NADPH‐d could reflect a spatial patterning of the nose to bulb projections. Taken together, these results indicate that G6PD expression in the ONL could be related to the importance of generating a substantial supply of NADPH to sustain the detoxifying systems represented by GR and P450R reactions and, only in discrete zones, by NADPH‐d activity. © 2005 Wiley‐Liss, Inc.