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 radioautographic distribution of the label of galactose-H(3) was compared with that of glucose-H(3) in a series of secretory cells of the rat. Whereas the glucose label appeared in all mucous cells, the galactose label was incorporated only into certain mucous cells. Whenever either label was incorporated, however, it was located first in the Golgi region and later in the secretion product, mucus. Several lines of evidence, including extraction of glucose label with peracetic acid-beta glucuronidase, indicated that the material synthesized in the Golgi region was glycoprotein in nature. In chondrocytes, both the galactose and the glucose label appeared first in the Golgi region and later in cartilage matrix; extraction of glucose label with hyaluronidase indicated that much of it consisted of mucopolysaccharide. In all secretory cells, the extraction of glycogen by amylase had no effect on Golgi radioactivity. Such extraction did not eliminate the scattered cytoplasmic label also seen after glucose-H(3) injection, but completely eliminated that seen after galactose-H(3). Consequently, the galactose-H(3) label in the Golgi region stood out more clearly, and was detected in many cells: pancreas, liver, epididymis, and intestinal columnar cells. In the latter, label later appeared in the surface coat. Thus, radioautography after injection of galactose-H(3), as after glucose-H(3), indicates that synthesis of complex carbohydrates takes place in the Golgi region of many secretory cells.
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PMID:Radioautographic comparison of the uptake of galactose-H and glucose-H3 in the golgi region of various cells secreting glycoproteins or mucopolysaccharides. 422 8

Hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35) was purified from mouse testes by ion-exchange chromatography, Sephadex G-200 filtration and Con A-agarose affinity chromatography. The final preparation had 94-fold purity and 12.2 units spec. act. of the enzyme (unit of specific activity = mumol N-acetylglucosamine released/h per mg protein at 37 degrees C and pH 4.5). Hyaluronidase is relatively heat stable and loses 10-20% of its activity at 50-55 degrees C for 10 min. Ea for eat denaturation of enzyme is 42-45 kcal between 45 an 63 degrees C. The Michaelis constant of mouse testicular hyaluronidase is 1.1 mg/ml hyaluronic acid. Antibodies to the purified enzyme were produced in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. Antiserum to hyaluronidase inhibited enzyme activity by 25%. Immunologically, mouse testicular hyaluronidase is species specific. Tissue extracts of mouse vital organs, except testes and epididymis did not react with the antisera, though nonspecific precipitation occurred between intestinal extracts and anti-hyaluronidase serum. Hyaluronidase was localized in testis sections by indirect immunofluorescence. A specific dark green fluorescence was localized on cell boundaries extending from spermatogonia to spermatids and appeared on the sperm acrosome. Cytoplasm of spermatogonia and spermatocytes showed light green fluorescence, whereas interstitial tissue was devoid of fluorescence.
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PMID:Isolation, properties, immunological specificity and localization of mouse testicular hyaluronidase. 616 67

Only a very small portion (4-7%) of the hyaluronidase of rat sperm obtained from the caput or cauda epididymis was related during incubation in capacitation medium for up to 24 h at 37 degree C. A portion of the cell-associated hyaluronidase was accessible to external substrates, allowing sperm suspensions to lyse glycosaminoglycans of cumulus clots rapidly, even without capacitation. This process appears to represent the employment of an enzyme bound to the sperm cell, analogous to the use of solid-phase enzymes in current enzyme technology.
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PMID:The role of sperm-bound hyaluronidase in the dispersal of the cumulus oophorus surrounding rat ova. 680 69

Insectivora are of special interest as the most primitive of the eutherian mammals, but essentially nothing is known of their gamete function. In this respect, the Asian musk shrew (Suncus murinus), investigated in the present study, displays many idiosyncrasies. In the epididymis, the giant acrosome undergoes further stabilization, its unusual resilience being especially evident in a "rim" created by a persistent close alignment of the outer acrosomal and overlying plasma membranes. However, until spermatozoa reached a gland on the vas deferens, no post-testicular change was demonstrable in the sperm head surface, the unusual nature of which was indicated by a dorso-ventral differentiation, by an inability to auto-agglutinate or to bind to the homologous zona pellucida, and by an insensitivity to anti-sperm immunoglobulin IgG in fresh serum. At mating, only about 1 x 10(6) spermatozoa are inseminated as far as the anterior vagina with plug formation. Within the small (6 mm) fallopian tube, the isthmus and ampulla are sharply delineated by their contractile activity and epithelial character; there is evidence of some sperm entry into isthmic crypts and a tendency for ipsilateral ovarian control of sperm transport to the tubal ampulla. The cumulus oophorus does not undergo preovulatory mucification and expansion, is characterized by persistent intercellular gap junctions, and is insensitive to hyaluronidase and trypsin. It is unclear how the compact cumulus is penetrated at fertilization. The giant acrosome contains acrosin and an unusually temperature-dependent cumulytic activity; it is intact in motile ampullary spermatozoa but appears to be discharged before reaching the zona pellucida. Since eggs were not penetrated in the presence of ampullary spermatozoa until 4-10 h after ovulation, Suncus spermatozoa spend a long period in the female before they can fertilize. The determinants of sperm function, including capacitation and the acrosome reaction (AR), may depend on a different set of controls in Suncus, perhaps as a legacy of the resilient giant acrosome. This possibility could be examined in other Crociduran and Soricine shrews selected according to acrosome size.
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PMID:Distinctive features of the gametes and reproductive tracts of the Asian musk shrew, Suncus murinus. 819 63

PH-20, a testis-specific protein first expressed in haploid germ cells, is present on the posterior head plasma membrane and inner acrosomal membrane of mature guinea pig sperm. PH-20 is bifunctional, having a hyaluronidase activity that allows sperm to penetrate the cumulus layer and a separate activity required for binding of acrosome-reacted sperm to the zona pellucida. The immunization of male guinea pigs with PH-20 reproducibly results in infertility with a duration of 6-12 mo or longer. In this study, we analyzed the immunopathology in the reproductive tract of PH-20-immunized males to probe the mechanism(s) responsible for the induced infertility and found two separate effects. Remarkably, in almost all infertile, PH-20-immunized males, the caudae epididymides were empty (contained no sperm) or contained only abnormal sperm. The complete loss of normal sperm in the epididymis apparently results in infertility. A second effect was the induction of experimental autoimmune orchitis (EAO), representing the first report of EAO induced by a purified testis/sperm molecule of known functions. PH-20-induced EAO differed from EAO induced by crude testis antigens in two respects: 1) an absence of epididymitis with abscess and granuloma and 2) the presence of antibody on germ cells within seminiferous tubules and inside the cauda epididymidis. The former suggests that crude testis antigens other than PH-20 are responsible for epididymitis, and the latter suggests a possible role of antibody in EAO pathogenesis and infertility induction. Return to fertility, after 6-12 mo, was accompanied by regression of EAO and reappearance of spermatozoa in the caudae epididymides.
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PMID:Mechanism of infertility in male guinea pigs immunized with sperm PH-20. 916 Jul 11

The gametes of the least shrew, Cryptotis parva, were studied in regard to their maturation and structure, and with particular emphasis on their behavior in the fallopian tube, from the time of ovulation until the appearance of two-cell embryos beginning some 9 h after ovulation. Cryptotis spermatozoa are organized according to the conventional eutherian mold, with the exception of a barbed perforatorium and an unusual plasma membrane density lent by a bristly coat where it overlies the acrosome rim. In the epididymis they undergo a maturation of the capacity for motility and an -S-S-related stabilization of the nucleus and tail organelles, with the cauda housing only approximately 4-5 million spermatozoa. Mating involves penile locking and also the deposition of a modest vaginal plug that covers the cervix. The short (4-5 mm) fallopian tube has three regions-a simple isthmus, a relatively narrow ampulla populated throughout by ciliated crypts, and a crypt-free terminal infundibulum-the fertilization site. Unlike the situation in most mammals, the tubal isthmus was devoid of spermatozoa in mated females before and after ovulation, which occurred approximately 13 h post-hCG and produced a mean of 5.7 ova. However, the ampulla then housed approximately 1500 active cells in groups within the ciliated crypts, sometimes together with leukocytes but with few spermatozoa above in the infundibulum. Within about 1 h after their ovulation from approximately 400-microm follicles, eggs were penetrated while in the infundibulum despite the nonexpanded hyaluronidase-resistant state of the cumulus oophorus. However, on moving down to the ampulla by 2-4 h after ovulation, the dense cumulus around fertilized eggs appeared to proliferate and began to disperse coincidentally with secretion of a hyaluronidase-sensitive matrix in which hundreds of motile spermatozoa often became enmeshed. This cumulus change also occurred around unfertilized eggs, though more slowly, but not around fertilized or unfertilized eggs cultured in vitro. Thus, cumulus matrix production appeared to be stimulated to an important degree by factors in the oviduct, not by preovulatory gonadotropins as in many mammals. Although cumulus-invested eggs were fertilized readily in vitro, cumulus-free eggs of the same age were never fertilized, and spermatozoa bound to the zona pellucida had intact acrosomes. This and related evidence from other shrews makes it seem likely that the soricid cumulus has an essential role in fertilization and may induce the acrosome reaction.
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PMID:Unusual ampullary sperm crypts, and behavior and role of the cumulus oophorus, in the oviduct of the least shrew, Cryptotis parva. 916 Jul 26

Effects of a combination of medoxy-progesterone acetate (MPA) and dihydrotestosterone (DHT) at a dose of 10 mg + 2 mg/kg, injected, in weekly to rats of proven fertility were investigated with respect to their fertility, sperm and organ functions. This hormonal regimen had no effect in body and organ weights except in the testis. A depletion in sperm reserves in testis and epididymis was noted in addition to a loss of their motility in the later. Alterations in cauda epididymal sperm viability and morphology and reduced levels of superoxide dismutase indicated changes in their plasma membrane permeability. Sperm acrosomal enzymes such as acrosin and hyaluronidase were also affected leading to a loss of their function. Consequently the fertility potential of these rats also impaired after 60 days of hormonal regimen. Testicular biochemical machinery revealed its altered metabolism and regressed spermatogenic activity accounting for its loss of weight. Similarly epididymal physiology also exhibited changes leading to impaired sperm maturation. However, toxicity studies showed no significant variations in liver and blood biochemical profiles indicating non-toxic nature of this combination. All these effects seemed to be transient and reversible upon withdrawal of treatment for 60 and 90 days gradually. Thus, this combination with aromatizable androgen is useful for induction of functional sterility.
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PMID:Endocrine approach to male fertility control by steroid hormone combination in rat Rattus norvegicus L. 983 78

We have previously reported the occurrence and partial characterisation of an alpha-D-mannosidase activity on plasma membranes of rat, mouse, hamster and human spermatozoa. A soluble isoform of the rat sperm surface mannosidase was purified and polyclonal antibody raised. Since several reports have suggested that mannosyl residues on the rat, mouse and human zona pellucida may be involved in sperm-zona binding, studies were undertaken to examine the receptor-like role of mannose-binding molecules on rat spermatozoa. Sprague-Dawley rats (25-30-days old) were superovulated and eggs collected from the oviduct were treated with 0.3% hyaluronidase to remove the cumulus cells. Spermatozoa, collected from the cauda epididymis were capacitated for 5 h at 37 degrees C in 5% CO2 in air. The sperm-zona binding assay was performed in the presence of increasing concentrations of several sugars as well as preimmune and immune (anti-mannosidase or anti-mannose binding protein) IgG. Data from these studies show that: (1) significantly fewer sperm bound per egg in the presence of competitive inhibitors of mannosidase; (2) among the sugars examined, D-mannose was the most potent inhibitor causing 70% reduction in the number of sperm bound per egg; (3) anti-mannosidase or anti-mannose binding protein (but not preimmune) IgG showed a dose-dependent reduction in the number of sperm bound per egg; (4) anti-mannosidase IgG (but not anti-mannose binding protein IgG) showed a dose-dependent inhibition of sperm surface mannosidase activity; (5) the competitive inhibitors of mannosidase or the immune IgG had no effect on sperm motility or the sperm acrosome reaction. These result suggest that mannose-binding molecule(s) such as alpha-D-mannosidase or mannose-binding protein on the spermatozoa may recognise mannosyl residues on zona pellucida, and play a receptor-like role in sperm-egg interaction in the rat.
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PMID:Mannose-binding molecules of rat spermatozoa and sperm-egg interaction. 1071 52

Rat sperm 2B1 antigen (the orthologue of guinea pig sperm PH20) is a plasma membrane-bound glycoprotein that is endoproteolytically cleaved during passage through the epididymis and subsequently migrates from the tail to the acrosomal domain during capacitation. Unlike guinea pig PH20, however, sperm surface 2B1 is insensitive to phosphatidylinositol phospholipase C, nor is it known how endoproteolytic cleavage affects its hyaluronidase activity. In this investigation we have expressed 2B1 cDNA in Chinese hamster ovary cells; we have shown that it contains an internal sequence motif for attachment of a glycosyl phosphatidylinositol (GPI) anchor and that cleavage from a single- into a two-chain molecule causes a significant shift in the optimum pH for hyaluronidase activity. Functionally, these results suggest that 1) 2B1 glycoprotein on rat spermatozoa is attached to the plasma membrane via a GPI anchor and that this is an important factor in its ability to migrate from the tail to the acrosomal domain during capacitation; and 2) endoproteolytic cleavage of 2B1 serves to optimize its hyaluronidase activity immediately before fertilization, thereby facilitating penetration of spermatozoa through the cumulus oophorus.
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PMID:Rat sperm 2B1 glycoprotein (PH20) contains a C-terminal sequence motif for attachment of a glycosyl phosphatidylinositol anchor. Effects of endoproteolytic cleavage on hyaluronidase activity. 1081 70

The gene for the sperm adhesion molecule 1 (PH-20), SPAM1, has been known to be testis-specific and exclusively haploid expressed. We show that in mice, the 2 common isoforms of the protein (Spam1) observed in sperm are also present in the caput, corpus, and cauda epididymides. Both qualitative and quantitative variation of expression of the protein were observed in epididymis with the highest expression detected in the corpus. The endogenous production of enzymatically active (via hyaluronidase) Spam1 by epididymal cells is supported by the detection of steady-state Spam1 epididymal messenger RNA in both wild type and germ cell-deficient mice. In situ transcript hybridization shows the transcript to be localized to the principal cells of the epithelium. The protein was similarly immunolocalized to these cells, predominantly in vesicles near the apical region. The results suggest a mechanism for transportation of Spam1 from the epididymal epithelium to sperm during their transit and storage in the cauda. None of the current categories of spermatogenic-expressed genes shows the dual transcription pattern (haploid testicular/diploid epididymal) observed for Spam1. The work also confirms and extends the finding that Spam1 is expressed in the kidney.
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PMID:Mouse Spam1 (PH-20): evidence for its expression in the epididymis and for a new category of spermatogenic-expressed genes. 1110 8


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