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)

The effects of castration and testosterone replacement therapy on the histology and biochemical composition (RNA, DNA, total protein, alkaline phosphatase, acid phosphatase, hyaluronidase, sialic acid, glycogen, phospholipids, and glycerylphosphorylcholine [GPC]) of the epididymis of the rabbit and rhesus monkey were investigated. Castration produced marked ponderal, histologic, and biochemical changes in the epididymis. In the androgen-deficient state the tubular diameter and epithelial cell height were reduced and there was an increase in interbular stroma. The levels of RNA, DNA, phospholipids, and GPC were also reduced in castrated animals. Testosterone treatment restored the histologic features and the levels of various biochemical constituents to a great extent but not to the intact control level. The importance of endocrine and exocrine factors of the testis in relation to epididymal function is discussed.
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PMID:Androgenic control of epididymal function in rhesus monkey and rabbit. 40 58

Cauda epididymal sperm of mature guinea pigs were incubated (37 degrees, 5% CO2 in air). 10% of the total enzyme activity was released into the medium in 4 hr, 30% in 24 hr. Addition of lysolecithin resulted in rapid release of hyaluronidase. Vitamin C (0.54 mM), sodium fluoride (0.02 M), and cholesterol increased the rate of release whereas citrate (20 mM) diminished it. No effect upon hyaluronidase release was noted upon addition of KCN (10(-2)M), progesterone (250 microgram/ml), testosterone (500 microgram/ml), spermine (1.15 mg/ml), inositol (5.6 mM), or chloroquine phosphate (0.54 mM).
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PMID:Hyaluronidase release from guinea pig spermatozoa as affected by reproductive tract secretions and metabolic inhibitors. 73 70

Flutamide, a pure antiandrogen, increases the levels of plasma luteinizing hormone but antagonizes the biological expression of androgen on target organs. Flutamide was administered to rats to study the effect of altered availability of hormones on the functional status of epididymis. The weights of ventral prostate, seminal vesicles and epididymis showed antiandrogenic effects of flutamide. However, increased activity of kidney beta-glucuronidase reflected increased availability of testosterone. The concentrations of protein and DNA along with the activities of acid phosphatase and hyaluronidase decreased in flutamide-treated rats. The activities of acid phosphatase and hyaluronidase in epididymal sperms along with protein concentration increased in flutamide-treated rats. Alteration of epididymal function by treatments affecting lysosomal stability was indicated.
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PMID:Effect of flutamide on the physiological status of epididymis and epididymal sperms. 160

It is the purpose of this study to determine the effects of Zn deficiency on the biochemical composition of testes, epididymis, and seminal vesicle of rabbits. An attempt is made to evaluate previous physiological studies and to correlate them with biochemical changes. 30 mature male Balady rabbits were used in this study. 1 group was fed a Zn-deficient diet, and 2 control groups were pair-fed or fed ad libitum a Zn-sufficient diet, all for a period of 120 d. There was significant reduction in the levels of hyaluronidase, alkaline phosphatase, acid phosphatase, lactic dehydrogenase, sialic acid, protein, and Zn of both testes and epididymis of Zn-deficient rabbits. Reduction in the level of glyceryl-phosphoryl choline in the epididymis of Zn-deficient rabbits was the best indicator of inhibition of epididymal secretory activity. In contrast, the cholesterol and glycogen contents of the testes were elevated. The results also showed in Zn-deficient rabbits significant reduction in androgen-sensitive parameters, namely fructose and citric acid in the seminal vesicle. Zn levels were decreased in the seminal vesicle. The results indicated that Zn deficiency caused inhibition of testicular, epididymal, and seminal vesicle function and, consequently, caused reductions in the biochemical composition of these organs.
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PMID:Response of testes, epididymis, and seminal vesicle of rabbits to zinc deficiency. 178 25

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

Plasma membranes of boar sperm from caput, corpus and cauda of the epididymis were purified by differential- and sucrose-density equilibrium centrifugation and were found to yield a single band at a density of 1.13 g/cm3. This fraction was enriched in acid and alkaline phosphatase, 5'-nucleotidase and (Na+ + K+)-ATPase activities, whereas it contained minimal amounts of hyaluronidase and N-acetylglucosaminidase and no succinic acid dehydrogenase activities. The plasma membrane of caput, corpus and cauda sperm had the same phospholipid/protein and cholesterol/phospholipid ratios but yielded different amounts of protein and individual lipid classes. Several changes in the plasma membrane were observed during transit of sperm through the epididymis. Within the phospholipid class a decrease in the percentage of phosphatidylethanolamine, phosphatidylserine and phosphatidylinositol was detected accompanied by an increase in amount of phosphatidylcholine, sphingomyelin and polyphosphoinositides. In the other lipid classes there was a decrease in the amount of free fatty acid and the major glycolipid. The amount of cholesterol decreased, while the amount of desmosterol and cholesterol sulfate increased. There was an increase in the amount of diacylglycerol. In addition, the changes in the fatty acid composition of the total membrane lipid and each phospholipid were determined. The above changes in the lipid composition of the plasma membrane during epididymal maturation may help to explain the decreased resistance to cold shock and changes in membrane fluidity of sperm during transit in the epididymis.
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PMID:Changes in the lipid content of boar sperm plasma membranes during epididymal maturation. 399 37

Hyaluronidase release was used as an index of acrosomal membrane damage during cold shock of epididymal boar sperm and ejaculated sperm from intact and vesiculectomized boars. Sperm were also incubated with seminal plasma from intact and vasectomized boars to examine the contributions of male accessory gland secretions. Acrosomal membranes of epididymal sperm were more resistant to cold shock than those of ejaculated sperm. Only 36% of the hyaluronidase released by ejaculated sperm was released by the epididymal sperm in spite of similar hyaluronidase content of the sperm. Preincubation of epididymal sperm in seminal plasma from both intact and vasectomized boars increased resistance to cold shock by 60 to 80%. Initial dilution of epididymal sperm with seminal plasma, rather than Ringer-fructose buffer, was associated with low progressive motility and with retention of cytoplasmic droplets. In contrast, acrosomal membranes of ejaculated sperm from intact and vesiculectomized boars exhibited similar sensitivity to cold shock, releasing hyaluronidase capable of forming .20 and .19 mumol N-acetylglucosamine from hyaluronic acid/10(8) sperm in 8 min. Moreover, seminal plasma from vasectomized boars had no effect on acrosomal sensitivity to cold shock of ejaculated sperm from vesiculectomized boars.
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PMID:Effect of male accessory gland secretions on sensitivity of porcine sperm acrosomes to cold shock, initiation of motility and loss of cytoplasmic droplets. 400 68

Pig testicular hyaluronidase was prepared, separated and purified. An assay technique for hyaluronidase which takes advantage of colorimetric methods for the detection of Nacetyglucosamine, which is released from hyaluronic acid was employed. Male and female guinea pigs were immunized with crude pig testicular hyaluronidase or guinea pig epididymal sperm and sacrificed at various times up to 8 weeks. The serum was assayed for inhibition of hyaluronidase. Complete inhibition of enzyme activity is observed in antiserum from female guinea pigs at serum dilutions of 1:100. The implications for this infertility inducing antibody for human use require further study.
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PMID:Hyaluronidase and its relationship to contraceptive development. 473 93

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

Sodium aurothiomalate, a low molecular weight inhibitor of hyaluronidase, blocked in-vitro fertilization in hamsters at the level of the zona pellucida: concentrations of 25-250 micrograms inhibitor/ml prevented fertilization of cumulus-intact and cumulus-denuded eggs. Fertilization of zona-free ova was not affected. In-vivo fertilization was also reduced (from 100% controls to 37.5%) by 10 mg inhibitor/ml added to an epididymal sperm suspension before artificial insemination into the uterus. These findings suggest that hyaluronidase may play a role in zona penetration or that sodium aurothiomalate blocks sperm penetration of the zona by inhibiting an enzyme(s) other than hyaluronidase.
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PMID:Inhibition of fertilization in the hamster by sodium aurothiomalate, a hyaluronidase inhibitor. 677 82


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