Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distribution of (newly found) NAD-dependent aldehyde dehydrogenase (ALDH) was determined in the rat testis and epididymis as a function of age. There were changes in specific activity of testicular ALDH as a function of age. Epididymal ALDH, which is found evenly distributed between the caput and cauda epididymis, increased initially from the 20th day after birth to th 50th day and remained little altered thereafter in both the caudet and the caput portion of the epididymis. Testicular and epididymal ALDH were found species-dependent with the hamster testis and the rat epididymis showing greater specific activities from the rest of the species studied, respectively. Determinations of testicular ALDH in various mouse strains indicate that it is strain-dependent. Intake of 25% (v/v) ethanol solution as the sole drinking fluid for 10 consecutive days inhibited testicular ALDH in the three mouse strains studied. Administration of disulfiram, 15 mg/kg/day for 60 consecutive days, exerted inhibitory action on testicular and epididymal ALDH in the rat. Intraperitoneal injection of pyrazol, 100 mg/kg once daily for 7 days, resulted in inhibition of epididymal but not of testicular ALDH. It is suggested that testicular and epididymal ALDH may play a role in the toxic action of ethanol-derived acetaldehyde on the gonad.
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PMID:Testicular and epididymal aldehyde dehydrogenase in rodents: modulation by ethanol and disulfiram. 700 7

The subcellular distribution of the enzymes primarily involved in the metabolism of ethanol and acetaldehyde were made in the rat testis and in the epididymis. The enzymes measured were alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). They were NAD-dependent, temperature sensitive and displaying maximal activity in the presence of pyrophosphate buffer at pH 9.8. Both enzymes were readily measurable in the 10% (w/v) testicular and epididymal homogenates. The ADH activity was mainly localized in the nuclear and in the cytosolic fractions of the testis compared to the absence of measurable ADH activity in the epididymis. Testicular ALDH was measurable in all subcellular preparations, i.e. in the nuclear, in the mitochondrial, in the cytosolic and in the microsomal fractions. Maximal testicular ALDH activity was determined in both the nuclear and the cytosolic components compared to a lower microsomal ALDH activity. Determination of Km shows that cytosolic ALDH possesses the lowest apparent Km as contrasted with a high value for the mitochondrial ALDH. Testicular cytosolic ADH but not ALDH was noncompetitively inhibited by 3-methoxytyramine, histamine and d-amphetamine in vitro.
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PMID:Subcellular fractionation of alcohol and aldehyde dehydrogenase in the rat testicles. 703 79

Male rats were maintained on water or on 10% ethanol drinking fluid. They were pairfed for 30 d prior to exposure to simulated high altitude (approximately 6000 m) and for 78 d, during which they were exposed to simulated high altitude on alternate days. Corresponding controls were maintained at ambient pressure. The high-altitude animals showed loss in liver and epididymis weights compared to respective water controls as contrasted with increased spleen weight in ethanol-drinking rats exposed to high altitude. Hepatic mitochondrial aldehyde dehydrogenase (ALDH) was decreased, compared to controls, by hypobarometric pressure in water-drinking animals. Ethanol intake negated this effect. The kinetics of this inhibition show changes in Vmax without concomitant changes in the apparent Km. Hepatic alcohol dehydrogenase did not change by either treatment. Testicular and epididymal ALDH showed, statistically, no significant changes in specific activity as a function of exposure to high altitude. However, combined ethanol drinking and altitude exposure increased epididymal ALDH compared to water-drinking rats subjected to the same experimental conditions. The changes in liver and testicular weight and in the enzyme involved in the biotransformation of ethanol-derived acetaldehyde suggest the contribution of endocrinological and biochemical factors to hypoxia and to ethanol-evoked adverse responses studied.
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PMID:Ethanol and hypobarometric simulated high altitude: a gonadal-hepatic toxicity study in the male rat. 714 78