Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetohexamide reductase activity in microsomes from the kidney of male rats increased markedly at puberty to approach the maximum level at 8 weeks of age; it was not detected until 4 weeks of age. Furthermore, castration suppressed effectively the activity in kidney microsomes at 8 weeks of age. These findings clearly indicate that the activity in kidney microsomes can be regulated by androgens. On the other hand, in cytosol from the kidney of male rats, a higher acetohexamide reductase activity was observed at all weeks of age tested. Castration had no significant effect on the activity in kidney cytosol.
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PMID:Factors affecting acetohexamide reductase activities in microsomes and cytosol from the kidney of male rats: age and castration. 151 59

The influence of testosterone treatment on acetohexamide reductase activities in liver microsomes and cytosol of female rats was examined. Acetohexamide reductase activity in liver microsomes was much lower in female rats than in male rats. Combined testosterone treatment in pubertal and adult periods induced male-specific acetohexamide reductase activity in liver microsomes of female rats. However, testosterone treatment only during puberty or during adulthood was without effect. Testosterone secreted from the testes during puberty appeared to have a significant effect similar to neonatal imprinting in the induction of acetohexamide reductase activity in liver microsomes of female rats. The combined testosterone treatment, or testosterone treatment only during puberty or during adulthood had no effect on acetohexamide reductase activity in liver cytosol of female rats.
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PMID:Combined testosterone treatment in pubertal and adult periods induces male-specific acetohexamide reductase activity in liver microsomes of female rats. 785 Feb 60

The influence of aging on the reductase activity of acetohexamide, an oral antidiabetic drug with a ketone group, was examined in liver microsomes and cytosol of male rats. Acetohexamide reductase activities in liver microsomes of male rats at 26 and 31 months of age were much lower than that in liver microsomes of male rats at 9 weeks of age. Testectomy markedly decreased acetohexamide reductase activity in liver microsomes of the 9-week old rats and the decreased enzyme activity was significantly increased by testosterone administration. These results indicate, at least in part, that aging decreases the enzyme activity by decreasing the secretion of testosterone from the testes. On the other hand, aging (26 months of age) did not affect acetohexamide reductase activity in liver cytosol of male rats, although the enzyme activity at 31 months of age was slightly but significantly lower than that in liver cytosol of male rats at 9 weeks of age. Testectomy or testosterone administration had no effect on the enzyme activity in liver cytosol of 9-week old male rats.
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PMID:Influence of aging on acetohexamide reductase activities in liver microsomes and cytosol of male rats. 787 66

Acetohexamide is an oral antidiabetic agent and is metabolized by the reductive conversion of the acetoxy group to a secondary alcohol metabolite. In vivo, many drugs are metabolized by reductase enzymes; however, the characteristics of the enzymes that reduce carbonyl compounds need to be clarified. We tested whether reductase activity for acetohexamide can be found in human erythrocytes. Enzyme activity was monitored by formation of hydroxyhexamide using HPLC methods. In human erythrocytes, reductase activity (6.10 +/- 1.20 nmol/min/g hemoglobin) (mean +/- SD) was indeed observed, when 0.5 mM acetohexamide was used as a substrate. KM values and Vmax at the physiologically important pH 7.4 were 0.70 +/- 0.13 mM and 9.19 +/- 0.88 nmol/min/g hemoglobin, respectively. Separation of protein by gel filtration gave one major peak fraction with reductase activity whose molecular weight was estimated to be 31,000. Known substrates of carbonyl reductase such as menadione, daunorubicin, and ethacrynic acid inhibited the acetohexamide reduction. The acetohexamide reductase in erythrocyte showed characteristics of carbonyl reductase. Furthermore, acetohexamide reductase activity in erythrocyte was approximately 30% activity of that of human liver (0.17 +/- 0.05 nmol/min/mg cytosolic protein). The pattern of inhibitors in human liver was essentially the same as that in erythrocytes. It is plausible that the activity in erythrocytes may predict the activity in the liver. It was concluded that carbonyl reductase in human erythrocyte plays an important role in acetohexamide metabolism.
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PMID:Carbonyl reductase activity for acetohexamide in human erythrocytes. 807 Mar 12

We examined the alteration of acetohexamide reductase activities in kidney microsomes and cytosol of cadmium (Cd)-treated rats. Acetohexamide reductase activity in kidney microsomes of male rats was markedly decreased by treatment with Cd at a dose of 1.23 mg/kg body weight. However, the decreased enzyme activity was completely restored by repeated treatment with testosterone propionate. Therefore, it is reasonable to assume that the treatment with Cd indirectly affect the androgen-dependent acetohexamide reductase activity in kidney microsomes of male rats, possibly by depressing androgen production. In the case of female rats, unlike male rats, the microsomal enzyme activity was little detectable, and was unaffected by the treatment with Cd. Furthermore, Cd treatment had no significant effect on acetohexamide reductase activity in kidney cytosol of male or female rats.
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PMID:Alteration of acetohexamide reductase activities in kidney microsomes and cytosol of cadmium-treated rats. 963 11

In this review, we describe the physiological, genetic and pathological factors regulating the reductive metabolism of drugs with a ketone group. Acetohexamide (AH) was chosen as a model drug with a ketone group. Species differences of AH reductase activity were observed in liver cytosol and microsomes of animals tested. AH reductase activity in liver microsomes of rats was much higher in males than females. The activity was not detectable until 4 weeks of age after birth in both sexes, but increased markedly at puberty only in males. AH reductase activity in liver microsomes of male rats was decreased by testectomy, and restored by the treatment with testosterone propionate, indicating that the sex-related difference and postnatal development of the activity are regulated by androgens. There was a strain difference of AH reductase activity in liver microsomes of male rats. Of rat strains tested, only Wistar-Imamichi strain was found to lack male-specific microsomal enzyme activity. The inheritance pattern of AH reductase activity in liver microsomes of rats was determined by mating the genetic deficiency Wistar-Imamichi strain with Fischer-344 strain. Streptozotocin-induced diabetes significantly decreased AH reductase activity in liver microsomes of male rats. Furthermore, the physiological role of AH reductase present in liver microsomes of male rats was examined. We propose the possibility that the male-specific microsomal enzyme physiologically functions as a 20 beta-hydroxysteroid dehydrogenase.
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PMID:[Physiological, genetic and pathological factors regulating the reductive metabolism of drugs with a ketone group]. 1059 Jul 11

Acetohexamide, an oral antidiabetic agent, is metabolized by carbonyl reductase to hydroxyhexamide, which has a higher hypoglycemic potency than the parent compound. In the present study, interindividual variability of carbonyl reductase activity in erythrocyte was examined. Enzyme activity in 31 healthy subjects (23.9 plus minus 3.4 years, mean plus minus SD) was monitored by measuring formation of hydroxyhexamide using HPLC methods. Using 0.5 mM acetohexamide as substrate, reductase activity of 6.06 plus minus 0.06 nmol min(minus sign1) gHb(minus sign1) (range: 5.9--6.2) with a coefficient of variation of 15% was observed in erythrocytes. Acetohexamide-reducing activity in erythrocytes showed a normal distribution and the interindividual variability of the reductase activity was found to be small, implying that the large variability reported for the acetohexamide plasma half-life is not caused by the amount of reductase enzyme in erythrocytes.
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PMID:Individual Variability of Carbonyl Reductase Activity for Acetohexaminde in Human Erythorcytes. 1185 Jun 47