The role of NADPH in the regulation of glucose-6-phosphate and 6-phosphogluconate dehydrogenases in rat adipose tissue
β Scribed by Antonio Ayala; Isabel Fabregat; Alberto Machado
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 371 KB
- Volume
- 105
- Category
- Article
- ISSN
- 0300-8177
No coin nor oath required. For personal study only.
β¦ Synopsis
Previous studies examining the regulation of the synthesis of G6PDH and 6PGDH in rat liver and adipose tissue have focused on the induction of these enzymes by different diets and some hormones. In rat liver these enzymatic activities seem to be regulated by a mechanism involving changes in the NADPH requirements. In this paper we have studied the effect of changes in the flux through different NADPH-consuming pathways on G6PDH and 6PGDH levels in adipose tissue and on the NADPH/NADP ratio. The results show that: I) an increase in the consumption of NADPH, caused by the activation of either fatty acid synthesis or detoxification systems which consume NADPH, is paralleled by an increase in the levels of these enzymes; II) when the increase in consumption of NADPH is prevented, the G6PDH and 6PGDH levels do not change.
π SIMILAR VOLUMES
## Abstract The resistance to oxidative stress is a multifactorial reaction involving the clustering of transcriptionally regulated genes. Because glucoseβ6βphosphate dehydrogenase (G6PD), the principal enzyme responsible for reducing power, is highly expressed in the olfactory bulb (OB), it is of
American buffalos have been studied for their hemoglobin and transferrin types, which show no detectable polymorphism (Braend and Stormont, 1963;Stormont, 1964). This report summarizes new data on erythrocytic glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) in th
The ontogeny of phosphoglueonate dehydrogenase in Japanese quails and chicken-quail hybrids was determined by vertical starch gel eleetrophoresis of pooled early embryos. The enzyme of maternal origin was found to be present at all stages of development. Paternal phosphogluconate dehydrogenase in pu
The activities and kinetics of the enzymes G6PDH (glucose-6-phosphate dehydrogenase) and 6PGDH (6-phosphogluconate dehydrogenase) from the mesophilic cyanobacterium Synechococcus 6307 and the thermophilic cyanobacterium Synechococeus 6716 are studied in relation to temperature. In Synechococcus 6307