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

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Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Seven glycosidases (beta-N-acetylglucosaminidase, alpha-fucosidase, beta-galactosidase, acid alpha-glucosidase, beta-glucuronidase, acid and neutral alpha-mannosidase) were analysed in seminal plasma from the first and second successive ejaculates in normal Ayrshire bulls. In comparison to our previous data the results indicate that beta-N-acetylglucosaminidase, beta-galactosidase and beta-glucuronidase are derived mainly from epididymal secretions, while alpha-fucosidase and particularly neutral alpha-mannosidase originate additionally from the spermatozoan cytoplasmic droplets. The seminal vesicles appear to contribute particularly to the seminal plasma acid alpha-glucosidase and acid alpha-mannosidase activities. The seminal plasma enzymes derived from the epididymis and cytoplasmic droplets were suppressed in semen samples with low sperm density or with high numbers of abnormal spermatozoa. The epididymal and seminal vesicle enzymes could be utilized in assessment of the secretory/functional capacity of these glands.
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PMID:Comparison of glycosidase levels in bovine seminal plasma. 311 30

Each epididymis of control and swainsonine-fed rats (5 micrograms/ml drinking water) was divided into 5 segments, and tissue, spermatozoa and sperm-free supernatants were prepared from each segment. When levels of 3 lysosomal glycosidases and total protein were determined, the proximal cauda contained the greatest concentration of glycosidase. The specific-activity profile for beta-glucuronidase and beta-galactosidase was similar in swainsonine-fed and control rats. However, the concentration of alpha-D-mannosidase in tissue of all segments was significantly greater in swainsonine-fed rats than in age-matched controls. Enzyme activity for alpha-D-mannosidase after swainsonine treatment was significantly greater in spermatozoa from the caput, than in spermatozoa from the corpus and the cauda epididymidis. Since the alpha-D-mannosidase activity was optimal at pH 4.5 and studies with highly specific antibody to lysosomal alpha-D-mannosidase immunoprecipitated all of the alpha-D-mannosidase present in detergent extracts of epididymal tissue, spermatozoa, and sperm-free supernatant, the enzyme studied is of lysosomal origin.
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PMID:Effect of swainsonine on rat epididymal glycosidases. 314 32

Daily oral administration of acrylonitrile (10 mg/kg body weight) to mice for a period of 60 days caused a significant decrease in the activity of testicular sorbitol dehydrogenase and acid phosphatase, and an increase in that of lactate dehydrogenase and beta-glucuronidase. Histopathological studies revealed degeneration of the seminiferous tubules. A decrease in the sperm counts of the epididymal spermatozoa was also observed in the animals of the acrylonitrile-exposed group. These observations suggest that acrylonitrile may affect the male reproductive function by causing testicular injury.
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PMID:Testicular effects of acrylonitrile in mice. 338 48

Reproductive tract functions were studied in adult male Wistar rats given 10 ppm thallium as thallium sulfate in the drinking water. After 60 days of treatment, spermatozoa isolated from the cauda epididymides and vas deferens showed reduced motility and immature germ cells were found in the tubular lumen. Histological examination of testes in thallium-treated animals revealed disarrangement of the tubular epithelium and ultrastructural changes in the Sertoli cells with cytoplasmic vacuolation and distension of the smooth endoplasmic reticulum. The activity of testicular beta-glucuronidase was significantly reduced whereas acid phosphatase and sorbitol dehydrogenase activities were unchanged. Plasma testosterone levels were within normal limits. No abnormalities in testicular morphology and biochemistry were seen in animals sacrificed at the end of the first month of thallium exposure. These findings indicate that the male reproductive system is a susceptible target site to toxic effects of thallium under chronic exposure. They also suggest a major involvement of Sertoli cells in the mechanism underlying thallium-induced testicular damage.
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PMID:Thallium-induced testicular toxicity in the rat. 373 19

The biochemical distribution of beta-glucuronidase activity was studied in different reproductive organs, seminal plasma and spermatozoa of the bull. The highest specific activity was found in the epididymis, where the activity seemed to be mostly in nonsecretory and only partly in secretory form. A molecular weight of 340 X 10(3) to 360 X 10(3) was recorded for beta-glucuronidase in the bull seminal plasma and different reproductive organs with gel filtration on Sepharose 6B. In chromatofocusing four activity areas (CF-1 to CF-4) were usually obtained for beta-glucuronidase in the bull seminal plasma. The major peak CF-2 (also in the different reproductive organs) had a pI value of 5.6-5.3 and the two minor activity areas CF-1 and CF-3 had pI values of 6.0-5.8 and 5.2-4.5, respectively. Peak CF-4 eluted with a NaCl gradient after the Polybuffer elution and possibly represents an enzyme form incompletely detached from negatively charged cellular material. Isoelectric focusing on polyacrylamide gel confirmed the heterogeneity of beta-glucuronidase, since several activity bands were detected in the secretion of the different parts of the epididymis. beta-Glucuronidase activities CF-1, CF-2 and CF-3 had similar pH activity profiles (pH optimum around pH 3.0-4.0) and response to thermal inactivation at 50 degrees C. The multiple beta-glucuronidase activities of the bull seminal plasma are proposed to derive mainly from the secretion of the cauda epididymidis.
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PMID:beta-Glucuronidase in the bull seminal plasma and reproductive organs. 375 85

The role of hyaluronidase, beta-glucuronidase and beta-N-acetylglucosaminidase in the penetration by mouse spermatozoa through the layers surrounding the oocyte was investigated by in vitro techniques. Myocrisin, fenoprofen, phosphorulated hesperidin and PS53 (a hydroquinone-sulfonic acid-formaldehyde polymer) inhibited fertilization when incubated with capacitated spermatozoa before the treated spermatozoa were mixed with intact oocytes but not when the inhibitor-treated, capacitated spermatozoa were added to oocytes free of follicle cells. The antifertility activity did not appear to be due to an effect on sperm motility or on the oocytes. These 4 compounds are known hyaluronidase inhibitors and, of the acrosomal enzymes tested, only share inhibition of hyaluronidase. Kinetic studies indicated that myocrisin is a reversible inhibitor of mouse sperm hyaluronidase whereas the other three are irreversible inhibitors. Adding saccharolactone, a beta-glucuronidase inhibitor, or N-acetylglucosaminolactone and N-acetylgalactosaminolactone, beta-N-acetylglucosaminidase inhibitors, to capacitated spermatozoa under the same conditions as the hyaluronidase inhibitors did not decrease fertilization. This was the case even though the beta-glucuronidase or beta-N-acetylglucosaminidase activities of the spermatozoa were completely inhibited, at least at the time that the inhibitor-treated, capacitated spermatozoa were mixed with the oocytes. The hyaluronidase activity of mouse spermatozoa remained unaltered during the incubation period required for capacitation; however, prolonged incubation caused a significant decrease in hyaluronidase. Untreated mouse spermatozoa caused hydrolysis of hyaluronic acid more effectively than did sperm extracts obtained by detergent extraction. These results are consistent with the theory of an essential role of hyaluronidase in mouse fertilization. At least in this species, the enzyme appears to be specifically involved in sperm penetration through the follicle cell layer. The data do not support an essential role for beta-glucuronidase and beta-N-acetylglucosaminidase in the penetration by mouse spermatozoa through the oocyte's investments. In contrast to some other species, sperm capacitation in mice does not result in a loss of hyaluronidase although part of the enzyme activity is lost on prolonged incubation. Mouse spermatozoa appear to be able to digest substrate (hyaluronic acid) even though hyaluronidase is not released.
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PMID:Effect of hyaluronidase, beta-glucuronidase and beta-N-acetylglucosaminidase inhibitors on sperm penetration of the mouse oocyte. 376 57

In this work the alterations of some acrosomal enzymes and gamma-GT were studied in diseases of the male genital tract. Thirty-two patients with vascular diseases, seven with inflammatory diseases and twenty-four controls were investigated. In all patients the sperm morphology was studied and the following enzymes were assayed: beta-glucuronidase, beta-galactosidase, beta-glucosidase and gamma-GT. In all patients with vascular and inflammatory diseases we found severe hypokinesis and decreased number of spermatozoa. The activity of all four enzymes in both pathological groups was decreased in comparison with the controls, and this decrease was significant for all enzymes in males with vascular diseases and for beta-galactosidase and beta-glucosidase in cases with inflammatory diseases. Our data show that the decrease of spermatozoal count was accompanied by a decreased enzyme activity. The role of decreased sperm plasma enzyme activity, the decreased production of spermatozoa and quantitative changes in structure and acrosome enzyme content are discussed.
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PMID:Enzymes and cytomorphological sperm alterations in some diseases of the male reproductive system. 613 94

The effect of in vitro capacitation (events that occur before the acrosome reaction) on the acrosomal enzymes of human spermatozoa was determined. Capacitation of human spermatozoa was assessed by their ability to penetrate denuded hamster oocytes. The activities of a number of enzymes commonly associated with the sperm acrosome, including nonzymogen acrosin, proacrosin, inhibitor-bound acrosin, hyaluronidase, acid phosphatase, beta-glucuronidase, beta-glucosidase, beta-N-acetylglucosaminidase, beta-galactosidase and beta-N-acetylgalactosaminidase were assessed. With the exception of acid phosphatase, no alteration in enzyme activity occurred after 4 h of incubating the spermatozoa under capacitation conditions although gamete fusion took place. The acid phosphatase levels decreased twofold, presumably due to the loss of seminal (prostatic acid phosphatase that loosely adheres to spermatozoa. After 8 h of capacitation, a large decrease in sperm enzyme levels took place only in the case of hyaluronidase, although small decreases were also noted in total acrosin, proacrosin and inhibited acrosin. No new electrophoretically migrating forms of acrosin were observed. Decreases in total acrosin and proacrosin, but not in inhibited acrosin, also occurred when spermatozoa were incubated under noncapacitating conditions for 8 h, indicating that capacitation may specifically cause the release of some acrosin inhibitor from human spermatozoa. It is concluded that, with the possible exception of hyaluronidase, the in vitro capacitation of human spermatozoa does not cause a major change in its acrosomal enzyme content so that these hydrolases are fully present before the acrosome reaction takes place during gamete fusion. Serum albumin appears to protect against the loss of some of these enzymes since the activity of several glycosidases was significantly reduced when the spermatozoa were incubated for 8 h in human serum albumin-free medium.
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PMID:Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. 640 71

Studied was the effect of beta-glucuronidase, hydrocortisone, and mercaptoethanol in bull semen on the activity of the alkaline phosphatase and the viability and fertilizing capacity of spermatozoa. It was found that the beta-glucuronidase enzyme in conc. of 270 UI per cu. cm of semen enhanced the activity of one of the forms of AP in agar electrophoresis (AP-1) with the simultaneous enhancement of the thermal resistance of spermatozoa at 46 degrees C and their fertilizing capacity by 9.6 per cent at first insemination. At minimum concentration hydrocortisone (1 X 10(-6) M) lowered the heat resistance of spermatozoa at 39 degrees C. Mercaptoethanol was found to lower by 3 per cent the activity of semen alkaline phosphatase. It is suggested to use the beta-glucuronidase enzyme in the practice of artificial insemination out of all other biologically active agents studied.
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PMID:[Effect of biologically active substances on the alkaline phosphatase activity, viability and fertility of bull spermatozoa]. 688 16

In vitro experiments were carried put to test the effect of beta-glucuronidase, ensaprost-phi, and carbocholin-proserin on a total of 725 samples of deeply-frozen bull semen in 8 nutrient media. Studied were the motility, thermal resistance, and oxygen consumption of spermatozoa. The first two indices showed highest values with the use of medium No 2 consisting of 2.8 per cent solution of sodium citrate and 4 gamma ensaprost-phi, and the consumption of oxygen was highest in medium No 1, consisting of 2.8 per cent solution of sodium citrate and 50 U beta-glucuronidase. Biologic experiments with 2106 cows were also carried out. The conception rate was 9.03 per cent higher that that of the control animals at first insemination.
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PMID:[Effect of various drugs and enzymes on the quality of deeply frozen bull sperm]. 695 72


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