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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of unilateral orchidectomy on the adult rat epidiymal testosterone metabolizing enzymes, delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase, are investigated. Five weeks following unilateral orchidectomy, it is found that the activity of 3 alpha-hydroxysteroid dehydrogenase per organ is not altered, whereas delta 4-5 alpha-reductase activity decreased by more than 80% on the side of the orchidectomy. Neither accessory sex tissue weights, ventral prostate and seminal vesicles, nor the concentration of circulating testosterone, luteinizing hormone, follicle-stimulating hormone, or prolactin is altered by unilateral orchidectomy. These data indicate that (1) epididymal 3 alpha-hydroxysteroid dehydrogenase activity can be maintained by circulating androgens and that (2) the major factor regulating delta 4-5 alpha-reductase activity is not a substance secreted by the testes into the peripheral circulation. It is suggested that a substance directly secreted into the epididymis by the testis regulates epididymal delta 4-5 alpha-reductase activity.
Can J Physiol Pharmacol 1979 Sep
PMID:Effects of unilateral orchidectomy on rat epididymal delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase. 51 41

Sensitivity to norepinephrine (expressed as pD2) was different between the prostatic and the epididymal half of the rat vas deferens. The epididymal half was more sensitive than the prostatic half; difference in pD2 was 0.826 +/- 0.095 (mean +/- S.E., 13 experiments). Between the two halves, nearly the same difference in pD2, 0.745 +/- 0.125 (6 experiments), was observed in the responses to methoxamine, which is not incorporated into the adrenergic nerve terminals. In the two halves, 3 x 10(-6) M phentolamine produced a smiliar decrease in pD2 of norepinephrine: 1.485 +/- 0.056 and 1.282 +/- 0.080 in the prostatic and epididymal half, respectively (6 experiments). Only in the prostatic half, 10(-5) M propranolol produced a slight increase in pD2 of norepinephrine, 0.344 +/- 0.133 (6 experiments). Sensitivity to K+ was also different between the two halves. These results suggest that the difference in the sensitivity to norepinephrine between the prostatic and the epididymal half is due to postjunctional natures varying along the length of the rat vas deferens.
Arch Int Pharmacodyn Ther 1979 Sep
PMID:Variation of postjunctional natures along the length of the rat vas deferens as a cause of regional difference in the sensitivity to norepinephrine. 52 69

The effects of local heating on testicular and epididymal vascular resistance in sodium pentobarbitone anesthetized rats was measured with a microsphere technique. When exposing the left scrotum to 33 and 37 degrees C for 30 min, no significant effects on blood flows were observed in comparison to those of the right side. Exposure to 41 degrees C caused a significant (p less than 0.05) decrease in vascular resistance of both testes and epididymides. The response was more pronounced at 43 degrees C. The Leydig cell function, as judged from the testosterone concentrations in plasma and testicular tissue after LH stimulation, was significantly (p less than 0.01) depressed at 41 and 43 degrees C. It was concluded that the impaired Leydig cell function was unrelated to testicular blood flow.
Acta Physiol Scand 1978 Sep
PMID:The influence of scrotal warming on testicular blood flow and endocrine function in the rat. 69 55

The lipoprotein lipase activity of rat epididymal adipose tissue falls on starvation and increases on refeeding. Studies with fat cells isolated from this tissue have shown that increases in the activity of the enzyme occur under appropriate incubation conditions in vitro. The present study compares the responses of cells isolated from the adipose tissue of fed and 48-h starved rats. Fat cells from rats starved for 48 h display a lower initial lipoprotein lipase activity than cells from fed rats. When cells from rats in both nutritional states are incubated in a suitable medium at 25 degrees C, there is a progressive increase in the medium lipoprotein lipase activity. The absolute increase in the total activity of the incubation system during incubations of cells from 48-h starved rats is significantly less than during incubations of cells from fed rats. However, when expressed as a percentage of the initial cell activity, the rises in total activity are similar in the two nutritional states. Cycloheximide has no significant effect on the increase in activity of lipoprotein lipase that occurs with cells from 48-h starved rats. However, it does partially block the increase in activity seen with cells from fed rats and in a manner similar to that previously reported for cells from 24-h starved rats. The significance of the results is discussed in relation to previous studies with both intact adipose tissue and isolated fat cells.
Biochim Biophys Acta 1978 Sep 28
PMID:The effect of nutritional state on the lipoprotein lipase activity of isolated fat cells. 69 38

Acetone-ether preparations of epididymal fat pads from fasted or fed rats contained two enzymes catalyzing the hydrolysis of long-chain monoacylglycerols. The enzymes were identified as monoacylglycerol lipase (Tornqvist, H. and Belfrage, P., (1976) J. Biol Chem. 251, 813--819) and lipoprotein lipase by their apparent pI values after electrofocusing in non-ionic detergent, selective inhibition properties, substrate specificity and positional specificity. It was estimated that monoacylglycerol lipase accounted for about 90% of the total monoacylglycerol-hydrolyzing activity in acetone-ether preparations from fasted and 70% from fed rats. Its enzyme activity did not change with the nutritional state in contrast to that of lipoprotein lipase. The latter enzyme hydrolyzed 2-monoacylglycerols at a much lower rate than the 1(3)-isomers. Monoacylglycerol lipase was located almost entirely in the adipocytes, thus most of the enzyme activity towards monoacylglycerols in the adipose tissue was found in this site. Fractionated sucrose homogenates of rat epididymal fat pads also contained a third enzyme with monoacylglycerol-hydrolyzing activity, identified as hormone-sensitive lipase by its pI, selective inhibition properties and substrate specificity. It was estimated that hormone-sensitive lipase accounted for less than 20% of the total activity against monoacylglycerols in these tissue preparations from fasted rats. Over-all quantitative estimations emphasized the dominant role of monoacylglycerol lipase over the other two enzymes in the hydrolysis of monoacylglycerols.
Biochim Biophys Acta 1978 Sep 28
PMID:Enzymes catalyzing the hydrolysis of long-chain monoacyglycerols in rat adipose tissue. 69 45

Spermatozoa do not achieve full maturation and fertilizing capacity until passage through the epididymis. During this time they also gain motility, although spermatozoa do not move until after ejaculation. The organic fraction of human seminal plasma contains phosphate esters, particularly glycerylphosphorylcholine (GPC), phosphorylcholine (PCh), and inorganic phosphate (Pi). GPC is found in relatively high concentrations in the semen of many male animals, including man. GPC is synthesized by the epithelial cells of the epididymis, apparently under androgenic control. Consequently, it has been suggested that GPC might be a useful indicator of epididymal function. We have measured GPC, Pi, and PCh in fresh and frozen semen samples, using phosphorus nuclear magnetic resonance (31P NMR). All samples were assayed for phosphate esters. It was found that PCh was totally hydrolized to Pi. The average ratio of GPC to total phosphate (TP = GPC + Pi) remained constant at a value of about 0.1 for sperm counts over 20 million/ml. The ratio for azoospermic specimens was 0.02 or less; the same results were obtained from vasectomy specimens. This finding indicates that most of the GPC comes from the epididymis. There was a significant correlation between motility, progression, and the GPC ratio. Poor motility and progression in the specimens were accompanied by low GPC ratios regardless of the sperm counts.
Fertil Steril 1978 Sep
PMID:The role of phosphate esters in male fertility. 71 Jun 5

The influence of insulin and thyroxine on the cellularity of adipose tissue in the rat epididymal fat pad has been studied. Incorporation of (3H) thymidine into the DNA of fat cells and stroma was measured together with fat cell size and number in rats pre-treated with either one of these hormones. There was an increase in fat pad weight in insulin treated rats which was due to 'lipid filling' of existing adipocytes and not increased proliferation of new fat cells. Thyroxine treated rats showed a decrease in fat pad weight caused by a decrease in size of individual fat cells. Cell number remained unaffected by either treatment.
Horm Metab Res 1978 Sep
PMID:Adipose tissue cellularity: effect on insulin and thyroxine. 71 Nov 31

1. Enzyme activities (units/g wet wt.) were determined in the caput and cauda epididymidis and in epididymal spermatozoa of the rat. 2. The activity of most enzymes in the cauda was between 50 and 100% of that in the caput, except that ATP citrate lyase was barely detectable in the cauda. 3. Spermatozoa, unlike epididymal tissue, contained sorbitol dehydrogenase but lacked ATP citrate lyase. NADP+-malate dehydrogenase, mitochondrial glycerol 3-phosphate dehydrogenase, succinate dehydrogenase, carnitine acetyltransferase and citrate synthase were 5 to 400 times as active in spermatozoa as in epididymal tissue. 4. 2-Oxoglutarate dehydrogenase was the least active member of the tricarboxylic acid cycle in all tissues and most closely matched the measured flux through the cycle. 5. The concentrations of hydroxyacyl-CoA dehydrogenase and carnitine palmitoyltransferase were equivalent to the more active enzymes of the tricarboxylic acid cycle, indicating the capacity for extensive lipid oxidation, and the presence of 3-hydroxybutyrate dehydrogenase suggests that these tissues can also oxidize ketone bodies. 6. Transfer of reducing equivalents from cytoplasm to mitochondrion is unlikely to occur by means of the glycerol phosphate cycle because mitochondrial glycerol 3-phosphate dehydrogenase is relatively inactive in epididymal tissue, whereas the cytoplasmic enzyme has little activity in spermatozoa, but transfer may be accomplished by the malate-aspartate shuttle. 7. Transfer of acetyl units from mitochondrion to cytoplasm could be effected by the pyruvate-malate cycle in the caput of androgen-maintained rats, but not in the other tissues because of the low activity of ATP citrate lyase. Acetyl unit transfer could take place via acetylcarnitine, mediated by carnitine acetyltransferase. 8. Castration resulted in a decrease in the concentration of nearly all enzymes, although subsequent administration of testosterone restored concentrations to values similar to those in animals maintained by endogenous androgen. The extent to which enzyme concentration was changed by an alteration in androgen status was highly variable, but was most marked in the case of pyruvate carboxylase.
Biochem J 1978 Sep 15
PMID:Activity and androgenic control of enzymes associated with the tricarboxylic acid cycle, lipid oxidation and mitochondrial shuttles in the epididymis and epididymal spermatozoa of the rat. 72 83

The factors regulating the physiology of the epididymis and the induction of functional sterility by alteration of epididymal function are discussed. The threshold requirement of androgens to maintain the structural and functional integrity of the epididymis in the rat, hamster and monkey is much higher than that needed by the accessory glands. Further, the cauda epididymidis has a higher threshold requirement of androgens than the caput epididymidis and may reflect the differences in the availability and metabolism of androgens to these two segments. An inverse relationship exists between the levels of sialic acid (sialoproteins) in the epididymal luminal plasma and that bound to the spermatozoa in the cauda epididymidis. Androgen deprivation and consequent alteration of the secretory activity of the epididymis either by castration or by treatment with antiserum to LH or by the antiandrogen, cyproterone acetate, caused concurrent decrease in the levels of sialic acid in the luminal plasma and in the spermatozoa of the different regions of the epididymis. These changing patterns of sialic acid in the spermatozoa and luminal plasma may be associated with changes in the surface charge of the spermatozoa and the stabilization of the acrosome and its membranes during sperm maturation.
J Reprod Fertil Suppl 1976 Sep
PMID:Physiology of the epididymis and induction of functional sterility in the male. 82 28

MODIFICATIONS IN RABBIT SPERM PLASMA MEMBRANES DURING EPIDIDYMAL PASSAGE AND AFTER EJACULATION WERE INVESTIGATED BY USED OF THREE LECTINS: concanavalin A (Con A); Ricinus communis I (RCA(I)); and wheat germ agglutinin (WGA). During sperm passage from caput to cauda epididymis, agglutination by WGA drastically decreased, and agglutination by RCA(I) slightly decreased, although agglutination by Con A remained approximately unchanged. After ejaculation, spermatozoa were agglutinated to a similar degree or slightly less by Con A, WGA, and RCA(I), compared to cauda epididymal spermatozoa. Ultrastructural examination of sperm lectin-binding sites with ferritin- lectin conjugates revealed differences in the densities of lectin receptors in various sperm regions, and changes in the same regions during epididymal passage and after ejaculation. Ferritin-RCA(I) showed abrupt changes in lectin site densities between acrosomal and postacrosomal regions of sperm heads. The relative amounts of ferritin-RCA(I) bound to heads of caput epididymal or ejaculated spermatozoa. Tail regions were labeled by ferritin RCA(I) almost equally on caput and cauda epididymal spermatozoa, but the middle-piece region of ejaculated spermatozoa was slightly more densely labeled than the principal-piece region, and these two regions on ejaculated spermatozoa were labeled less than on caput and cuada epididymal spermatozoa. Ferritin-WGA densely labeled the acrosomal region of caput epididymal spermatozoa, although labeling of cauda epidiymal spermatozoa was relatively sparse except in the apical area of the acrosomal region. Ejaculated spermatozoa bound only a few molecules of ferritin-WGA, even at the highest conjugate concentrations used. Caput epididymal, but not cauda epididymal or ejaculated spermatozoa, bound ferritin-WGA in the tail regions. Dramatic differences in labeling densities during epididymal passage and after ejaculation were not found with ferritin-Con A.
J Cell Biol 1977 Sep
PMID:Lectin-binding sites on the plasma membranes of rabbit spermatozoa. Changes in surface receptors during epididymal Maturation and after ejaculation. 90 74


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