Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P56851 (
epididymal
)
11,273
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Cellulose acetate zymograms of
alcohol dehydrogenase
(
ADH
) and sorbitol dehydrogenase (SDH) extracted from male reproductive tissues of inbred mice were examined.
ADH
isozymes were differentially distributed in these tissues of C3H/He mice;
ADH
-B2 was observed in all tissues and testis cellular preparations examined;
ADH
-C2 was localized predominantly in the epididymis but was also present in the seminal vesicles, coagulating gland, and prostate gland. SDH was broadly distributed in these tissues but exhibited highest activities in the seminal vesicles, coagulating glands, and germinal cells of mature testes. Genetic variants for
ADH
-C2 and SDH provided evidence for (1) the identity of a second form of SDH in epididymis with
ADH
-C2; (2) the genetic identity of kidney, seminal vesicle, and testis SDH; and (3) the gentic identity of stomach and
epididymal
ADH
-C2. Developmental changes in testis and
epididymal
ADH
isozymes during maturation were examined.
ADH
-C2 appeared in the mature epididymis whereas
ADH
-B2 exhibited no major changes in activity in testis and epididymis during development.
...
PMID:Genetic variation, cellular distribution and ontogeny of sorbitol dehydrogenase and alcohol dehydrogenase isozymes in male reproductive tissues of the mouse. 72 74
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.
...
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.
...
PMID:Ethanol and hypobarometric simulated high altitude: a gonadal-hepatic toxicity study in the male rat. 714 78