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)

We studied the effect of a progestin (R5020) on proteins released by stromal and epithelial endometrial cells in primary culture. Stromal and epithelial cells was isolated by collagenase and hyaluronidase digestion of endometrial tissue. The synthesis of proteins released into the cell culture medium was assayed by [35S]methionine incorporation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, followed by fluorography. The relative proportions of individual proteins secreted by stromal and epithelial cells varied. However, 29K, 128K, and 150K proteins were more abundant in media from epithelial cell cultures, whereas 60K and 70K proteins were more abundant in media from stromal cell cultures. More proteins were secreted by cells obtained in the luteal phase than by those obtained in the proliferative phase. R5020 consistently stimulated the synthesis of a minor protein of 51,000 mol wt secreted by both epithelial and stromal cells. Physiological concentrations of dexamethasone, dihydrotestosterone, or estradiol did not stimulate synthesis of the 51K protein. The effect of R5020 was concentration dependent; maximal synthesis occurred with 10 nM R5020 and 4 days of treatment. This 51K protein is different from the estrogen-regulated 52K protein of breast cancers. These results indicate that cultured endometrial cells can synthesize and release a variety of proteins in vitro. One of them, the 51K protein, is a marker of responsiveness to progestin.
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PMID:A 51K progestin-regulated protein secreted by human endometrial cells in primary culture. 357 30

We have compared the ability of uncapacitated, capacitated acrosome intact, and acrosome-reacted hamster sperm to penetrate the cumulus and corona radiata of fresh hamster oocyte-cumulus complexes (OCC) in vitro. This was done using physiological numbers (1-20) of sperm so that cumulus and corona radiata cells did not disperse during challenge. Uncapacitated sperm did not penetrate to the zona pellucida surface; most (74%) uncapacitated sperm bound to cumulus cells at the periphery of the OCC. Capacitated acrosome-intact sperm penetrated to the zona pellucida surface; a significant percentage of these sperm arrived at the zona pellucida without showing evidence of initiating an acrosome reaction. Most capacitated acrosome-reacted sperm did not enter the extracellular matrix between cumulus and corona radiata cells; those which did penetrated to the zona surface with difficulty, if at all. These results suggest that the changes which occur in the sperm surface during capacitation are more important than the acrosome reaction in enabling hamster sperm to penetrate the cumulus and corona radiata. The effects of gold sodium thiomalate (GST) and polyphloretin phosphate (PPP) (inhibitors of hyaluronidase) on penetration of the OCC by capacitated sperm were also examined. Both synthetic inhibitors blocked sperm penetration to the zona pellucida, but the effective concentrations of inhibitors were far in excess of what was needed to block hyaluronidase activity. Reasons for concluding that the action of these inhibitors is nonspecific are discussed. These data show that hamster sperm with intact acrosomes can penetrate the cumulus and corona radiata cell layers of fresh OCC in vitro and support the hypothesis that the acrosome reaction occurs on the zona pellucida surface.
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PMID:In vitro penetration of hamster oocyte-cumulus complexes using physiological numbers of sperm. 359 10

The use of sodium hyaluronate in cataract surgery and intraocular lens implantation is often followed by a postoperative rise of intraocular pressure. A trial is described in which 10 patients underwent bilateral cataract extraction and Binkhorst intraocular lens implantation with the use of sodium hyaluronate. The enzyme hyaluronidase was instilled into the anterior chamber of the right eye only, to aid removal of sodium hyaluronate, and resulted in a statistically significant lowering of postoperative intraocular pressure in right eyes compared with left. Other uses of the enzyme are discussed.
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PMID:Hyaluronidase and sodium hyaluronate in cataract surgery. 371 4

The major urinary trypsin inhibitor (Mr 44 000), isolated from human urine, contains 35% carbohydrate. In addition to N-acetylglucosamine and neutral sugars (primarily mannose and galactose), the carbohydrate moiety contains hexuronic acid and N-acetylgalactosamine and corresponds to a glycosaminoglycan. This carbohydrate chain is an integral component of the inhibitor: it does not dissociate from the inhibitor when using dissociative conditions such as sodium dodecyl sulfate, guanidinium chloride, or by increasing ionic strength or mixing with cetylpyridinium chloride. This glycosaminoglycan chain is sensitive to chondroitinase ABC or testicular hyaluronidase digestion and corresponds to slightly sulfated chondroitin 4-sulfate or 6-sulfate. After treatment by these enzymes, the urinary inhibitor has a lower molecular mass (Mr 26 000) but still inhibits trypsin.
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PMID:The major human urinary trypsin inhibitor is a proteoglycan. 373 76

The isolating agents, one enzymatic (hyaluronidase) and two chemical (sodium citrate and EDTA) have been used to search for the best technique to prepare suspensions of viable cells from chicken cecum and jejunum. Viability of enterocytes was assessed in terms of cell membrane integrity (trypan blue exclusion test), metabolic activity (oxygen uptake, lactate production and ATP content) and monosaccharide cumulative capacity. Results show that: In both cecum and jejunum, membrane integrity is better in cells harvested with citrate than those isolated with hyaluronidase or EDTA; The best metabolic status was found in cecal cells isolated with citrate and in jejunal cells obtained with hyaluronidase; The capacity to support alpha-methyl-D-glucoside gradients is highest in the cells harvested with citrate. The citrate-containing isolation medium is thus considered to yield epithelial cell suspensions with the best functional conditions.
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PMID:Preparation and properties of isolated epithelial intestinal cells from chicken cecum and jejunum. 379 80

The use of intraocular sodium hyaluronate is complicated by a postoperative rise in intraocular pressure (IOP). The rise in IOP is thought to stem from a "clogging" at the trabecular meshwork by the large molecules of hyaluronate. This study uses serial tonographic measurements in an animal model to document this change in outflow facility. Furthermore, we investigate the ability of the enzyme hyaluronidase to cleave the hyaluronate into smaller molecular weight fragments, in vivo, and thereby eliminate the change in outflow facility. This report demonstrates the potential usefulness of this enzyme and documents the lack of harmful side effects histopathologically.
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PMID:Elimination of sodium hyaluronate-induced decrease in outflow facility with hyaluronidase. 380 83

A murine (BALB/c) skin toxicity model was used to evaluate various possible antagonists to vinca alkaloid-induced skin ulceration. Reproducible dose-response relationships were developed for vinblastine (VBL) and vindesine (VDS). With vincristine (VCR) only about 70% of mice developed dose-dependent ulceration. On an equal weight basis, VCR proved to be significantly more toxic than either VBL or VDS (P less than .05 by Student's t-test). Effective local intradermal antidotes to VBL, VDS, and VCR included hyaluronidase, normal saline, and calcium leucovorin (P less than .05 by the Student's Newman-Keuls multiple range test). Mild, topical skin heating significantly reduced VCR ulceration. In contrast, diphenhydramine and sodium bicarbonate were ineffective as local antidotes. Topical skin cooling, however, significantly increased vinca-induced skin ulcers for VBL, VDS, and VCR (P less than .05). Hydrocortisone, vitamin A topical cream, and isoproterenol increased skin toxicity. [3H]VBL was given intradermally to follow the drug's pharmacokinetic disposition from the skin and adherent panniculus carnosus muscle. [3H]VBL exhibited two phases of elimination: a rapid early phase [half-life (t 1/2) of approximately equal to 30 min] and a prolonged terminal phase (t 1/2 of approximately equal to 17 hr). The application of heat increased the distributive, early phase by 0.5-2.5 hours and did not enhance the terminal elimination of the drug from skin. Intradermal hyaluronidase significantly reduced the area under the ulceration multiplied by the time curve to one-seventh the control value, the peak [3H]VBL skin concentration to one-half the control value and the terminal [3H]VBL t 1/2 in skin to one-third the control level (P less than .05 by Student's t-test). These results show hyaluronidase to be an effective antidote for vinca-induced skin ulceration. Local glucocorticosteroids and topical cooling are definitely contraindicated in the management of inadvertent vinca alkaloid extravasations.
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PMID:Vinca alkaloid skin toxicity: antidote and drug disposition studies in the mouse. 385 72

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

To study kinetics and principles of cellular uptake of 13N-ammonia, a marker of coronary perfusion in myocardial scintigraphy, heart muscle cells of adult rats were isolated by perfusion with collagenase and hyaluronidase. Net uptake of 13N, measured by flow dialysis, reached equilibrium within 20 sec in the presence of sodium bicarbonate and carbon dioxide (pH 7.4, 37 degrees C). Total extraction, 80 sec after the reaction start, was 786 +/- 159 mumol/ml cell volume. Cells destroyed by calcium overload were unable to extract 13N-ammonia. Omission of bicarbonate and carbon dioxide reduced total extraction to 36% of control. 13N-Ammonia uptake could also be reduced by 50 muM 4,4' diisothiocyanostilbene 2,2' disulfonic acid, by 100 micrograms/ml 1-methionine sulfoximine, and by preincubation with 5 muM free oleic acid. These results indicate that in addition to metabolic trapping by glutamine synthetase, the extraction of 13N-ammonia by myocardial cells is influenced by cell membrane integrity, intracellular-extracellular pH gradient, and possibly an anion exchange system for bicarbonate. For this reason, the uptake of 13N-ammonia may not always provide a valid measurement of myocardial perfusion.
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PMID:Kinetics of 13N-ammonia uptake in myocardial single cells indicating potential limitations in its applicability as a marker of myocardial blood flow. 396 79

Characterization of muscarinic acetylcholine receptors in acinar cells from rat pancreas and lacrimal and parotid glands was achieved by binding of the reversible muscarinic antagonist [3H]quinuclidinyl benzilate (QNB) and the specific alkylating reagent [3H]propylbenzilylcholine mustard (PrBCM) to intact acini or dispersed acinar cells. Binding studies with [3H]QNB showed that acinar cells from pancreas contain 26,400, from parotid 21,400, and from lacrimal gland 25,700 binding sites/cell. To assess molecular size of the receptor in each gland, acini were prepared by digestion with purified collagenase and singly dispersed acinar cells were prepared by a combination of digestion with crude collagenase, hyaluronidase, and alpha-chymotrypsin and divalent cation chelation using EDTA. Muscarinic receptors on acini or dispersed cells were covalently labeled with 5 nM [3H]PrBCM, solubilized directly in hot sodium dodecyl sulfate buffer, and resolved by polyacrylamide gel electrophoresis. When solubilized acini were electrophoresed, a major labeled peak was observed on gels along with a smaller peak of lower apparent molecular weight. For pancreatic acini, the apparent molecular weights of these peaks were 117,600 and 85,700; for parotid acini, 104,800 and 74,500; and for lacrimal acini, 87,200 and 63,100. Addition of muscarinic antagonists to the labeling medium abolished both peaks. When dispersed acinar cells were labeled, the larger peak was eliminated, and all radioactivity was concentrated in a single peak: 87,600 for pancreas, 78,000 for parotid gland, and 62,800 for lacrimal gland. Digestion of prelabeled acini with the mixture of enzymes used to produce dispersed acinar cells similarly shifted all radioactivity into this second peak. Limited digestion of acini or dispersed cells with 1 mg/ml of papain resulted in the disappearance of these higher molecular weight peaks and the appearance of a broad peak at Mr = 40,000. Cells of nonepithelial origin, IM-9 lymphocytes and NG108 neuroblastoma X glioma hybrids, also were labeled with [3H]PrBCM and electrophoresed.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Muscarinic acetylcholine receptor structure in acinar cells of mammalian exocrine glands. 398 Apr 74


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