Abstract
In cerebellum of the adult rat, glucose-6-phosphate dehydrogenase (G6PD) activity is particularly localized in Purkinje cells, showing lower activity in the molecular and granule cell layers. G6PD is the first and rate-limiting step of the hexose monophosphate shunt (HMS), which has the physiological role of providing NADPH for reductive biosynthesis and detoxifying reactions. In this study, we searched for a possible correlation between G6PD and other NADPH-consuming enzymes, such as NADPH-cytochrome P450 reductase (P450R), glutathione reductase (GR) and NADPH-diaphorase (NADPH-d). This study was performed by means of immunohistochemistry and enzyme histochemistry followed by quantitative densitometric and confocal laser scanning microscopic analyses. Our results demonstrated that G6PD, P450R and GR have a similar distribution pattern characterized by the highest concentration of these enzymes in the somata of Purkinje cells, and by lower concentrations in the molecular and the granule cell layers. Moreover, in Purkinje cells, G6PD colocalized with both P450R and GR. NADPH-d activity showed a different distribution pattern when compared to the other enzymes, revealing the highest activity in the molecular layer and the lowest in Purkinje cells. Our results suggest a coordinated regulative mechanism of G6PD, P450R and GR based on the request of NADPH or on specific transcription factors.
| Original language | English |
|---|---|
| Pages (from-to) | 185-197 |
| Number of pages | 13 |
| Journal | Neuroscience Research |
| Volume | 51 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 2005 |
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Keywords
- Cerebellum
- Glucose-6-phosphate dehydrogenase
- Glutathione reductase
- NADPH-cytochrome P450 reductase
- NADPH-diaphorase
- Purkinje cells
ASJC Scopus subject areas
- Neuroscience(all)
Cite this
NADPH-consuming enzymes correlate with glucose-6-phosphate dehydrogenase in Purkinje cells : An immunohistochemical and enzyme histochemical study of the rat cerebellar cortex. / Ferri, Paola; Biagiotti, Enrica; Ambrogini, Patrizia; Santi, Spartaco; Grande, Paolo Del; Ninfali, Paolino.
In: Neuroscience Research, Vol. 51, No. 2, 02.2005, p. 185-197.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - NADPH-consuming enzymes correlate with glucose-6-phosphate dehydrogenase in Purkinje cells
T2 - An immunohistochemical and enzyme histochemical study of the rat cerebellar cortex
AU - Ferri, Paola
AU - Biagiotti, Enrica
AU - Ambrogini, Patrizia
AU - Santi, Spartaco
AU - Grande, Paolo Del
AU - Ninfali, Paolino
PY - 2005/2
Y1 - 2005/2
N2 - In cerebellum of the adult rat, glucose-6-phosphate dehydrogenase (G6PD) activity is particularly localized in Purkinje cells, showing lower activity in the molecular and granule cell layers. G6PD is the first and rate-limiting step of the hexose monophosphate shunt (HMS), which has the physiological role of providing NADPH for reductive biosynthesis and detoxifying reactions. In this study, we searched for a possible correlation between G6PD and other NADPH-consuming enzymes, such as NADPH-cytochrome P450 reductase (P450R), glutathione reductase (GR) and NADPH-diaphorase (NADPH-d). This study was performed by means of immunohistochemistry and enzyme histochemistry followed by quantitative densitometric and confocal laser scanning microscopic analyses. Our results demonstrated that G6PD, P450R and GR have a similar distribution pattern characterized by the highest concentration of these enzymes in the somata of Purkinje cells, and by lower concentrations in the molecular and the granule cell layers. Moreover, in Purkinje cells, G6PD colocalized with both P450R and GR. NADPH-d activity showed a different distribution pattern when compared to the other enzymes, revealing the highest activity in the molecular layer and the lowest in Purkinje cells. Our results suggest a coordinated regulative mechanism of G6PD, P450R and GR based on the request of NADPH or on specific transcription factors.
AB - In cerebellum of the adult rat, glucose-6-phosphate dehydrogenase (G6PD) activity is particularly localized in Purkinje cells, showing lower activity in the molecular and granule cell layers. G6PD is the first and rate-limiting step of the hexose monophosphate shunt (HMS), which has the physiological role of providing NADPH for reductive biosynthesis and detoxifying reactions. In this study, we searched for a possible correlation between G6PD and other NADPH-consuming enzymes, such as NADPH-cytochrome P450 reductase (P450R), glutathione reductase (GR) and NADPH-diaphorase (NADPH-d). This study was performed by means of immunohistochemistry and enzyme histochemistry followed by quantitative densitometric and confocal laser scanning microscopic analyses. Our results demonstrated that G6PD, P450R and GR have a similar distribution pattern characterized by the highest concentration of these enzymes in the somata of Purkinje cells, and by lower concentrations in the molecular and the granule cell layers. Moreover, in Purkinje cells, G6PD colocalized with both P450R and GR. NADPH-d activity showed a different distribution pattern when compared to the other enzymes, revealing the highest activity in the molecular layer and the lowest in Purkinje cells. Our results suggest a coordinated regulative mechanism of G6PD, P450R and GR based on the request of NADPH or on specific transcription factors.
KW - Cerebellum
KW - Glucose-6-phosphate dehydrogenase
KW - Glutathione reductase
KW - NADPH-cytochrome P450 reductase
KW - NADPH-diaphorase
KW - Purkinje cells
UR - http://www.scopus.com/inward/record.url?scp=12844281138&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=12844281138&partnerID=8YFLogxK
U2 - 10.1016/j.neures.2004.11.002
DO - 10.1016/j.neures.2004.11.002
M3 - Article
C2 - 15681036
AN - SCOPUS:12844281138
VL - 51
SP - 185
EP - 197
JO - Neuroscience Research
JF - Neuroscience Research
SN - 0168-0102
IS - 2
ER -