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)

Arylsulfatase A was extracted and purified from boar epididymal sperm acrosomes. Acrosomes were extracted by sonication in 50 mM Tris-maleate buffer containing 50 mM MgCl2, pH 6.1, followed by treatment with 50 mM Tris-maleate plus 0.2% Brij-35, pH 6.1. Purification of arylsulfatase A was performed with a three-step procedure consisting of centrifugation (85,000 X g), affinity chromatography with p-aminobenzamidine-Sepharose followed by chromatography on diethyaminoethyl (DEAE) Sephadex. The specific activity of the purified enzyme was 54 mumol/h per mg protein. The purified arylsulfatase did not contain any detectable acrosin or hyaluronidase activities. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis revealed a major band with an estimated molecular weight of 65,000 daltons. Properties of arylsulfatase A, determined by hydrolysis of p-nitrocatechol sulfate, indicated that the enzyme was inhibited 46% by 3.1 microM Ag+ and had a pH optimum of 4.2. Boar acrosomal arylsulfatase A dispersed the cumulus cells of ovulated hamster and rabbit eggs as well as those of follicular pig eggs. No effect of the enzyme on the zona pellucida or the oolemma was observed.
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PMID:Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. 614 55

The presence and composition of arylsulfatases in secretions of various glands of the boar genital tract were studied. Arylsulfatase A was present in seminal plasma but not in extracellular fluids of the testis and epididymis nor in blood serum of boars. On the other hand, arylsulfatase B was present in both seminal plasma and extracellular fluids of the testis but was completely resorbed in the epididymis. The acrosomal arylsulfatase A did not leak out of spermatozoa before ejaculation. We conclude that arylsulfatases A and B present in seminal plasma are secreted by the seminal vesicles, for three reasons: 1) secretions from seminal vesicles contained 2.3-fold higher arylsulfatase activities than did those from seminal plasma, but had an identical composition; 2) cauda epididymal fluids did not contain arylsulfatase; and 3) other accessory glands of the boar genital tract did not secrete arylsulfatase. When intact boar spermatozoa were incubated with arylsulfatase A, complete desulfation of seminolipid was observed. The most important arguments favoring our hypothesis that desulfation of seminolipid does not start before ejaculation are the following: 1) desulfoseminolipid is not detectable in epididymal or freshly ejaculated sperm samples; 2) the acrosomal arylsulfatase A cannot desulfate seminolipid present at the surface of the plasma membrane of intact spermatozoa because of its intracellular localization; 3) extracellular arylsulfatase A is stored in seminal vesicles and thus can interact with spermatozoa during and after ejaculation.
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PMID:Boar seminal vesicles secrete arylsulfatases into seminal plasma: evidence that desulfation of seminolipid occurs only after ejaculation. 809 13

To elucidate the mechanism of sterility induced by gossypol, we studied the relationship between the activities of acrosomal enzymes and their fertilizing capacity in the hamster. The results showed that the ability of spermatozoa to penetrate into bovine cervical mucus, hyperactivated motility (HAM) and fertility in vivo were significantly inhibited when spermatozoa were exposed to gossypol (2.5 microg - 60 microg/mL) for 15 min in vitro. Also, following administration of gossypol (12.5 mg/kg/day) for 6 weeks, sperm motility, HAM and rate of fertilization in vitro by the hamster cauda epididymal spermatozoa were significantly decreased and the extracts of testis delayed dispersion of the cumulus oophorus cells, suggesting that hyaluronidase and other acrosomal enzymes might be inhibited by gossypol. In addition, acrosin and arylsulfatase activities were also markedly inhibited. These data show that the inhibition of acrosin and arylsulfatase activities is the main cause of gossypol-induced infertility. The inhibition was dependent upon gossypol dose and the duration of administration. Thus, the assay of acrosin and arylsulfatase activities may provide a useful tool for monitoring sterility induced by gossypol.
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PMID:Inhibition of hamster sperm acrosomal enzyme by gossypol is closely associated with the decrease in fertilization capacity. 1113 75

In this study, we investigated the subcellular compartmentalization of arylsulfatase-A (AS-A) in the testis and epididymis as well as the surface distribution in rat epididymal sperm. Testicular AS-A was compartmentalized specifically to the area underneath the outer acrosomal membrane of the acrosomal granule and to the dorsal aspect of the sperm acrosome. Epididymal AS-A was synthesized in the endoplasmic reticular (ER) network of principal cells and secreted into epididymal lumen as evident by its reactivity in the apical cytoplasm and vesicles therein underneath stereocilia. In clear cells, AS-A reactivity was found throughout the cytoplasmic machineries involved in endocytosis. Surface distribution of AS-A was initially detectable at the concave ridge as early as in sperm of the initial segment (IS). AS-A was additionally localized to the post-acrosomal region in caput (CP), corpus (CO) and cauda (CD) epididymal sperm. The expression levels of surface AS-A gradually increased during sperm transit from IS to CD epididymidis. These results favored the adsorption of AS-A from epididymal fluid onto the sperm surface, rather than shunting from the acrosome as a consequence of capacitation-associated membrane priming.
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PMID:Rat sperm AS-A: subcellular localization in testis and epididymis and surface distribution in epididymal sperm. 1550 59