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:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acrosin and hyaluronidase demonstrated different release patterns following treatment of living spermatozoa with the Ca2+-ionophore A 23187. One hour after the acrosomal reaction about 50% of the acrosin was still associated with the spermatozoal membranes, while hyaluronidase could no longer be detected in the spermatozoal remnants. Strong fixation conditions with acrolein and glutaraldehyde were used to prevent redistribution and leakage of these sperm proteins. Lost antigenicity was restored with sodium-borohydride and pronase E treatment. Immunofluorescent localization showed hyaluronidase to be confined to the anterior portion of the acrosome. Acrosin was localized throughout the entire acrosome including the equatorial segment. By immunoelectron microscopy, hyaluronidase was exclusively found in the acrosomal matrix. The equatorial segment was devoid of hyaluronidase. Acrosin was found in the acrosomal matrix as well as on the outer acrosomal membrane. Furthermore, labeling for acrosin in the equatorial segment was clearly demonstrated. Localization of hyaluronidase was the same for epididymal and ejaculated sperm cells but in approximately 70% of the epididymal spermatozoa acrosin could not be detected in the equatorial segment. In most of these epididymal cells acrosin was confined to the anterior part of the acrosome comparable with hyaluronidase. These observations support the motion that the appearance of acrosin in the equatorial segment is part of the maturation process during passage through the epididymis.
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PMID:Immunocytochemical localization of acrosin and hyaluronidase in epididymal and ejaculated porcine spermatozoa. 392 82

Seven inhibitors of the sperm enzyme hyaluronidase were tested at nonspermicidal concentrations for their vaginal contraceptive activity in rabbits. Five of these compounds are marketed antiinflammatory agents and the other two were synthesized. Most of the agents showed contraceptive activity. Of the antiinflammatory agents, phenylbutazone and oxyphenbutazone were particularly potent. Besides being hyaluronidase inhibitors, these compounds are also cyclooxygenase (prostaglandin synthetase) inhibitors; based on other in vitro data, their primary effect on spermatozoa is probably by the inhibition of that enzyme.
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PMID:Vaginal contraceptive activity of hyaluronidase and cyclooxygenase (prostaglandin synthetase) inhibitors in the rabbit. 392 8

Spermatozoa from different bucks were stained with different fluorochromes, mixed, and inseminated heterospermically. By altering the interval between insemination and luteinizing hormone injection, spermatozoa were allowed to reside in the female tract approximately 5, 10, or 15 h prior to ovulation. The number of functional spermatozoa, from each male of a pair used, that was transported to the site of fertilization was estimated by counting total number of differently stained spermatozoa that surrounded or fertilized each oocyte. Spermatozoa from split ejaculates within a male competed against each other equally, indicating that the staining procedure did not affect fertilization or functional spermatozoal transport rates. Three pairs of males with high initial semen quality (greater than 80% motility) differed in fertility primarily due to functional spermatozoal transport. Spermatozoal survival in the female tract and capacitation time played a role in differences in male fertility when heterospermic insemination occurred at variable times relative to ovulation. Differences in fertilization not accounted for by spermatozoal transport ratio raised the possibility that rate of egg penetration due to acrosomal enzyme differences may be important in determining male fertility. Therefore, total acrosin, hyaluronidase, and arylsulfatase activity in spermatozoa from specific bucks used in fertilization experiments were determined. Although there were trends favoring high fertility when enzyme content was higher, the difference was significant only for arylsulfatase in one buck.
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PMID:Fertility differences among male rabbits determined by heterospermic insemination of fluorochrome-labeled spermatozoa. 393 54

Removal of cumulus may increase the chance of fertilization in patients with sperm antibodies, may facilitate fertilization in vitro with a small number of spermatozoa, and is necessary for microsurgical injection procedures in vitro. The aim of this study was to establish whether removal of the cumulus has any detrimental effects on the fertilization rate and embryo viability. Removal of cumulus cells from the human oocyte with bovine testicular hyaluronidase did not interfere with fertilization, early embryonic development, or pregnancy. This suggests that human spermatozoa can spontaneously undergo capacitation and fertilize oocytes in vitro in a chemically defined medium containing 10% preovulatory human serum. In three patients with low-quality semen, removal of the cumulus and the addition of hypotaurine and epinephrine apparently did not improve the motility nor the fertilizing capacity of the spermatozoa. Delayed fertilization and cleavage arrest was observed in one patient when spermatozoa obtained from the body region of the epididymis was used for insemination.
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PMID:Removal of the cumulus oophorus from the human oocyte for in vitro fertilization. 396 84

In contrast to the rabbit: 1) no hyaluronidase could be detected in fresh or frozen human seminal plasma, all color formation on assay being due to a dialyzable, heat stable factor; 2) almost no hyaluronidase could be extracted from frozen-thawed human testicles; 3) the hyaluronidase from human spermatozoa was rapidly inactivated upon release, either spontaneously or on extraction; and 4) a large decrease in hyaluronidase activity occurred when human spermatozoa were stored under various conditions. Rabbit spermatozoa contained six to 13 times more hyaluronidase than human spermatozoa. These results show that distinct species differences exist in the hyaluronidase associated with spermatozoa. None of the human genital tract sources studied could be used to obtain adequate amounts of hyaluronidase for the further isolation and purification of the enzyme. For both human and rabbit spermatozoa, it was optimal to add the cells directly to the assay system for the quantitation of hyaluronidase on spermatozoa rather than extracting the spermatozoa and testing the extracts. The spermatozoa of both species appear to be capable of digesting hyaluronic acid directly. As had previously been found for acrosin, a higher amount of hyaluronidase was maintained when human spermatozoa were cryopreserved in a zwitter buffer (TESTCY) rather than in glycerol.
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PMID:Release, extraction, and stability of hyaluronidase associated with human spermatozoa. Comparisons with the rabbit. 399 61

Cumulus cells were isolated by hyaluronidase treatment of whole cumulus masses from superovulated, non-mated mice. The cells, in groups of approximately 200, were incubated for up to 4 h in 50 nl medium M2 at 37 degrees C, and serial 3-nl samples assayed for pyruvate using an ultramicrofluorescence technique. With 5.55 mM glucose, 23.3 mM lactate, or a mixture of the two substrates, the cumulus cells formed pyruvate at rates of 10.2, 9.6, and 8.9 fmol/cell/h, respectively. The concentrations of glucose, pyruvate, and lactate, as measured in 3-nl aliquots of rabbit oviduct fluid were 1.5 mM, 0.3 mM, and 3.7 mM, respectively. When incubated with 1 mM glucose and 3 mM lactate, mouse cumulus cells formed 7.5 fmol pyruvate/cell/h. The mean number of cumulus cells per ovum within a cumulus mass was 2,060. Intact cumulus masses from mated and non-mated superovulated mice, incubated with 1 mM glucose and 3 mM lactate, formed 22.6 and 23.3 pmol pyruvate/ovum/h, respectively. The results suggest that pyruvate production by cumulus cells may be important in supporting the nutrition of unfertilized and fertilized ova, and of spermatozoa, within the oviduct lumen.
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PMID:Production of pyruvate by isolated mouse cumulus cells. 399 81

Hyaluronidase activity was examined in 109 specimens of human semen of various sperm densities, seminal plasma, and spermatozoa sedimented by centrifugation. We used a modification of a method originally devised for estimation of hyaluronidase activity in Clostridia and which was bases on measurements of the area of hyaluronate digestion in agar plates. Enzyme activities in both semen and seminal plasma increased with increase in sperm density. The activity in seminal plasma, which appeared promptly after liquefaction and represented enzyme released from spermatozoa, ranged from 31% to 61% of the activity in semen. Activities of spermatozoa in sediments exhibited lower values than those calculated for sperm of whole semen, possibly due to leakage. Both activities, calculated per million sperm cells, gradually increased with decrease in sperm density. The possibility that with severe oligozoospermia the acrosome may become less prone to enzyme release or that the initial activity per cell may increase is discussed. These phenomena would represent additional characteristics of oligozoospermia.
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PMID:Estimation of hyaluronidase activity of human semen and its relationship with sperm density by means of a simplified method. 612 24

Hyaluronidase activity was examined in 104 oligospermic and normospermic human semen specimens promptly after liquefaction, after repeated cycles of washings with a solution containing 1.3 M sucrose and 0.15 M NaCl, and after freezing and thawing. We assessed enzyme activity by measuring areas of the digestion of substrate (hyaluronate). After washing the oligospermic and normospermic semen specimens twice 34%-43% enzyme activity was still present in the sedimented sperm as compared to the initial values. Following additional washings no enzyme activity could be detected. Freezing and thawing of semen increased enzyme activity by 40%-50%, respectively, after the second cycle whereas further treatment did not increase the enzyme activity rate. It is suggested that two types of hyaluronidase are present in human spermatozoa, differing in membrane-binding properties which would be connected with their localization in the acrosome.
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PMID:Hyaluronidase activity in untreated human semen and following laboratory manipulations. 614 Feb 40

A study was designed to determine whether tetradecyl sodium sulfate (TDSS), a potent inhibitor of both acrosin and hyaluronidase, would have a contraceptive effect in rabbits when a controlled level of TDSS was released from a vaginal delivery system over a 4-week period. The toroidal shaped delivery system was composed of a core of TDSS incorporated in polyurethane surrounded by a rate-limiting membrane of polyurethane. These devices were found to have a sustained in vitro TDSS release rate of equal to or greater than 400 mcg/day for over 30 days and had a complete contraceptive effect in 15 rabbits bred weekly for 4 weeks. No toxic effects were noted at 20 mg/day doses, but slight to moderate vaginal irritation was observed in the 50 and 100 mg/day groups. These results clearly demonstrate that TDSS is a useful intravaginal contraceptive agent when incorporated in a delivery system that continuously releases the compound into the vagina. 175 corpora lutea were found in the ovaries of the study rabbits, indicating that TDSS has no effect on ovulation. It remains unknown whether the TDSS binds to all the spermatozoa at the point of TDSS release in the vagina or whether some TDSS finds its way into the oviduct after release into the vagina and finally binds there to the few spermatozoa that reach this site. The vaginal delivery system shown in this study to be efficacious in rabbits could lead to the development of a similar device for human contraception. The advantages of this system are that it frees users from daily or postcoital administration, is capable of self-insertion, and uses a nonhormonal agent as the active ingredient.
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PMID:An intravaginal contraceptive device for the delivery of an acrosin and hyaluronidase inhibitor. 636 1

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


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