Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Histochemical localization of the estrogen-induced sulfated glycoproteins was made in the estrogen-treated rabbit uterus. Biochemical studies by a group of Endo et al, affirmed these particular glycoproteins were PAS-positive and metachromatic as stained with TB. No sign of digestion, however, has been detected in a series of tests with alpha-amylase, testicular hyaluronidase, streptomyces hyaluronidase, chondroitinase AC and chondroitinase ABC, and heparinase. The apical portions of the epithelial and glandular cells, obviously expanded by the estrogen treatment, display strong beta-metachromasia with TB (pH 4.0), saliva-resistant PAS-positive reactions, and also alcianophilia with AB (pH 2.5). These reactions are not reduced after the treatment with the enzymes above-mentioned. Meanwhile, in the stromal matrix, the same enzymes give an influence to diminish the reactions to various extent. Our results suggest that the estrogen-induced sulfated glycoprotein is definitely localized in the apical portions of the epithelial and glandular cells. The identity is emphasized between the substance that is elucidated in the histochemical sections and the sulfated glycoproteins that have been specified solely by means of biochemical assays.
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PMID:Histochemical localization of estrogen induced sulfated glycoprotein in rabbit uterus. 5 8

Acidic glycoconjugates (glycosaminoglycans and glycoprotein) were obtained, from myometrium of ovariectomized rabbit under estrogenic condition, by pronase digestion, fractionation with cetylpyridinium chloride and Dowex I column chromatography, in succession. Composition of acidic glycoconjugates was determined enzymatically, employing Streptomyces hyaluronidase, chondroitinase AC II, chondroitinase ABC and crude heparinase. Each glycoconjugate was distributed in 3 approximately 8 fractions obtained by Dowex I column chromatography, indicating its charge and/or molecular heterogeneity. Acidic glycoconjugates consisted of hyaluronic acid (13.4%), chondroitin sulfates A plus C (39.4%), dermatan sulfate (24.6%), heparan sulfate (18.7%) and acidic glycoprotein (most probably sialoglycoprotein) (3.9%). Composition of acidic glycoconjugates in myometrium differed remarkably from that in whole uterus. Myometrium was abundant in chondroitin sulfate isomers (chondroitin sulfates A plus C plus dermatan sulfate), but lacked sulfated glycoprotein. The present results suggested that myometrium and endometrium of uterus may play quite different roles in reproduction.
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PMID:Composition of acidic glycoconjugates (glycosaminoglycans and glycoprotein) in myometrium of rabbit uterus under estrogenic condition. 71 60

Mammalian spermatozoa attain their fertilization capacity only after reaching the female genital tract. This process takes place in several stages. First there is a degradation of inhibitors (decapacitation factor and acrosin inhibitor) in the vagina, cervix and uterus. Concurrent with or subsequent to this process the actual capacitation in the uterus and tubes occurs. Capacitation is characterized by an increase in metabolism, alteration of motility and activation of lytic enzymes of the spermatozoa. The acrosome reaction takes place only on direct contact with the ovum. This reaction is accompanied by morphological changes in the spermatozoon and enables the proteolytic enzymes (corona-penetrating enzyme, acrosin and hyaluronidase) to leave the sperm head. With the help of these enzymes, the spermatozoon is able to break down the various egg envelopes, to penetrate the ovum and initiate fertilization.
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PMID:[The capacitation of spermatozoa]. 91 93

To women with chronic inflammatory diseases of uterus adnexes is applied intrauterine electrophoresis and intrauterine hydrotubation with streptomycin (1 gram) and hyaluronidase ferment (400--600 U. Hylaze "Dessau") and experimental studies are carried out. The new method for application of the antibiotic in inner genitals tissue, i.e., intrauterine Electrophoresis with streptomycin finds application in treatment practice under the observation of the relevant indications and conditions.
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PMID:[Therapy of adnexa inflammation]. 121 49

Fibronectin mRNA and protein content were examined during embryonic implantation in the rat uterus. Content of total fibronectin mRNA at day 6 of pregnancy increased relative to the non-pregnant uterus. In contrast, fibronectin protein content of the subepithelial stroma was relatively decreased except in the region directly surrounding the lumen, and this fibronectin immunoreactivity was sensitive to hyaluronidase treatment. These changes are likely to reflect the degradation and subsequent remodeling of the previously stable uterine extracellular matrix in preparation for embryonic implantation. A+, B-, V + fibronectin mRNAs were present in both the non-pregnant and day 6 pregnant uterus with increased content of A+ and V+ fibronectin mRNAs in the latter. A + fibronectin mRNA was distributed throughout the endometrial stroma of the non-pregnant uterus and content of the subepithelial stroma increased by day 4 of pregnancy, coincident with progesterone action on the endometrium. On day 6 of pregnancy, fibronectin mRNAs encoding the V95 and A regions were preferentially localized to the mesometrial zone of the subepithelial stroma. Accumulation of these mRNA splicing variants at the mesometrial zone was dependent upon decidualization, but the embryo was not required. Thus, there are two major changes in uterine fibronectin gene expression as a result of pregnancy: increased fibronectin mRNA content and mesometrial localization. These changes suggest a key function for fibronectin in implantation and imply the operation of a regulatory program of fibronectin gene expression which depends on hormonal sensitization and a nidatory stimulus.
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PMID:Uterine fibronectin mRNA content and localization are modulated during implantation. 129 49

The zona pellucida (ZP), a glycoprotein layer that encloses the mammalian oocyte, is formed during follicular development in the ovary, persists at the time of fertilization within the oviduct, and then surrounds the embryo until implantation in the uterus. Although the structure and chemical properties of the ZP have been extensively studied, the precise site of origin of the ZP remains a matter of controversy. Moreover, the mechanism of synthesis and secretion of the ZP constituents is not fully elucidated. We have recently developed monoclonal antibodies (MAbs) against oviductal ZP of the golden hamster. We have used one of these MAbs (an immunoglobulin G) and the protein A-gold technique to study the localization of the corresponding antigenic sites, and we report here their distribution in the oviduct and within the cumulus oophorus complex of the superovulated hamster. In the oviductal epithelium, immunolabeling was observed in non-ciliated secretory cells in structures involved in protein secretion. In the cumulus masses collected from the oviduct, the sites of immunoreactivity were localized exclusively in the ZP encompassing the oocyte. Gold particles were evenly distributed throughout the entire thickness of the ZP. Treatment of the cumulus masses with hyaluronidase prior to preparation of isolated oocytes for immunocytochemistry did not affect this uniformity. The ZP of the preovulatory oocytes in ovarian follicles was not labeled. Our study provides immunocytochemical evidence for the secretion of an oviductal antigen that becomes intimately associated with the ZP of the oocytes during their passage through the oviduct.
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PMID:Immunocytochemical evidence for the transfer of an oviductal antigen to the zona pellucida of hamster ova after ovulation. 275 89

An inhibitory component that diminishes estrogen receptor (ER) binding to nuclei in vitro is present in cytosol prepared from calf uterus. The inhibitor is heat stable and resistant to enzymatic treatment with trypsin, chymotrypsin, proteinase K, deoxyribonuclease I, or ribonucleases A, T1, and U2. Results of chromatography on DEAE-cellulose and Sephadex G-150 indicate that the factor is a negatively charged macromolecule. Inhibitory activity is sensitive to sequential digestion with chondroitinase ABC, hyaluronidase, and heparinase. Approximately 70% of the inhibitory activity is destroyed by treatment with heparinase alone. Heparitinase destroys only 30% of this activity. Furthermore, the addition of pure hyaluronic acid or chondroitin sulfate to the ER-nuclei binding assay results in little inhibition, whereas addition of heparin inhibits 75% of receptor binding. Overall, these results indicate that glycosaminoglycans, present in bovine uterine cytosol, are capable of inhibiting ER-nuclei interactions. The most potent inhibitory glycosaminoglycan displays heparin-like characteristics.
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PMID:Characterization of a cytosolic inhibitor of calf estrogen receptor binding to nuclei. 330 79

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

We have isolated and characterized the human cardiac mast cell (CMC) and compared this novel mast cell (MC type with MC obtained from uterus, skin, and lung. Heart tissue was obtained from 14 patients with cardiomyopathy (CMP, heart transplantation). CMC were isolated by enzymatic digestion using collagenase, pronase-E, hyaluronidase, and DNAse. Substantial amounts of CMC (0.5% to 1.5% of isolated cells) were found in the atrial appendages but not in ventricular digests or other sites of the heart (< 0.1%). In situ staining of atrial tissue revealed the presence of CMC in the myocardium (2.16 +/- 0.7 MC/mm2), endocardium (2.24 +/- 0.9 MC/mm2), and epicardium. As assessed by combined toluidine blue/immunofluorescence staining with monoclonal antibodies (MoAbs), isolated CMC expressed surface IgE, the receptor for stem cell factor (c-kit receptor/CD117), the p24 antigen (CD9), the Pgp-1 homing receptor (CD44), the pan leukocyte antigen (CD45), and the ICAM-1 antigen (CD54). CMC were not recognized by MoAbs to lymphocyte function associated antigen 2 (LFA-2; CD2), T-cell receptor (TcR; CD3), T4 antigen (CD4), LFA-1 alpha-chain (CD11a), C3biR alpha-chain (CD11b), CR4 alpha-chain (CD11c), LPS-R related Ag (CD14), 3-FAL/x-hapten (CD15), Fc gamma RIII (CD16), lactosylceramid (CDw17), the B-cell antigen CD19, or CR1 (CD35). In situ expression of leukocyte antigens on CMC was demonstrable by indirect immunoperoxidase staining technique and double-labeling immunohistochemistry. Almost all CMC (90%) reacted with MoAbs against tryptase and chymase and thus were MCTC. Cardiac mast cells were also stained by the heparin-binding dye Berberine sulfate and expressed measurable amounts of histamine (4.6 +/- 1.4 pg per cell). Cross linking of either IgE receptor or SCF receptor (c-kit) on CMC resulted in histamine secretion (non-specific release: < 6% of total histamine, alpha IgE induced: 12% to 52%; SCF-induced release: 9% to 18%), whereas neither substance P (a skin MC agonist) nor the basophil agonist FMLP showed an effect on CMC. Together, the CMC is an MCTC primarily located in the appendage of the atrium. This novel type of MC exhibits surface membrane antigen and functional properties similar to those of lung and uterus MC.
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PMID:The human cardiac mast cell: localization, isolation, phenotype, and functional characterization. 752 50

Monoclonal antibodies were produced against the oviductal secretory substances in 'Shiba' goats and their nature was characterized. In the ampullary region, very strong immunoreactivity with one clone (EE-1) was localized within the cytoplasm of non-ciliated cells ("secretory cells"), whereas very little or no immunoreactivity was observed in the isthmus region. This reactivity pattern was observed in both estrous and luteal phases. Immunohistochemical analysis showed the antigen to be either absent or minimally present in other organs including the alimentary canal, liver, pancreas, lung, kidney, uterus, thyroid gland, heart, spleen and spinal cord, and in oviducts of other species such as hamster, sheep and cow. The immunoglobulin isotype of EE-1 was determined as IgM with a kappa light chain. The positive reactions were eliminated by treating deparaffinized sections with periodic acid or testicular hyaluronidase. Results obtained in this study suggest that ampullary secretory cells in 'Shiba' goat oviduct contain a species- and tissue-specific antigen containing hyaluronic acid or hyaluronidase-sensitive carbohydrates.
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PMID:Production and immunohistochemical characterization of specific antibody to oviductal fluid of miniature 'Shiba' goat. 754 93


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