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)

An experimental model of disc herniation in tail discs of rats is described. Constant result on nucleus hernia and intervertebral narrowing were obtained by an easy manipulation on numerous rats. Intradiscal injection of aprotinin produced a widening of the disc height. Trypsin, collagenase, chymopapain, and hyaluronidase induced a narrowing of disc height; trypsin induced macroscopic necrosis of the soft surrounding tissues; and collagenase had a destructive effect on nucleus pulposus, annulus fibrosus, and even on end-plates. Chymopapain and hyaluronidase acted mainly on nucleus pulposus. Hyaluronidase could be of interest as a nucleolytic drug and needs further studies on optimal dosage and lack of side effects in the surrounding tissues before injecting it into human discs.
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PMID:Experimental model of disc herniations in rats for study of nucleolytic drugs. 244 86

The choice of which neurotransmitters will be produced by a developing neuron is influenced by the microenvironment of the neuron. In this study we show that neuronal contact with membrane-associated molecules promotes expression of peptidergic and cholinergic traits. Treatment of cultured neonatal rat sympathetic neurons with plasma membranes derived from adult rat spinal cord or sympathetic ganglia induced expression of the peptide transmitter substance P and increased levels of the cholinergic biosynthetic enzyme choline acetyltransferase. The transmitter-stimulating activity could be solubilized from spinal cord membranes by the detergent octyl glucoside but not by Triton X-100. The choline acetyltransferase- and substance P-stimulating activity also could be extracted from spinal cord membranes by 4 M sodium chloride, suggesting that the active material is membrane associated rather than an intrinsic structural membrane molecule. Trypsin or heat treatment of the extract destroyed the transmitter-stimulating activity, indicating that the factor contains a protein. Activity also was destroyed by hyaluronidase treatment, suggesting that the active material may contain a glycosaminoglycan. The choline acetyltransferase-stimulating activity in the 4 M NaCl extract was eluted in a single peak from a calibrated Sephadex G-75 column with a retention time slightly less than that of a 25-kDa standard. NaDodSO4/polyacrylamide gel electrophoresis of the active peak revealed a predominant band at 29 kDa. Thus, contact-mediated stimulation of substance P and choline acetyltransferase activity in sympathetic neurons results from neuronal exposure to a 29-kDa membrane-associated factor.
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PMID:Solubilization of a membrane factor that stimulates levels of substance P and choline acetyltransferase in sympathetic neurons. 244 32

In order to analyze the mucoid substance in the epithelial component of synovial sarcoma, electron microscopic and cytochemical studies were made on three of these neoplasms. The mucoid substances in the glandular lumen were intensely stained with ruthenium red (RR), appearing as granular, fibrillar and amorphous structures. RR staining of proteoglycans was diminished after treatment with chondroitinase AC or ABC, and was partially diminished by exposure to streptomyces hyaluronidase. Trypsin treatment did not affect RR staining of proteoglycans in the lumen. On thin sections stained with periodic acid-thiocarbo-hydrazide-silver proteinate (PA-TCH-SP), deposits of reaction product were observed on the mucoid substances within the lumen, and were localized in the Golgi complex, including the rough endoplasmic reticulum, small vesicle and lysosome-like dense body. Trypsin digestion decreased the stain intensity of PA-TCH-SP. These results indicate that the lumen of the gland-like component contains glycoproteins as well as proteoglycans mainly consisting of chondroitin sulfate and hyaluronic acid, and suggest that GERL (Novikoff) is closely related to production, storage and transport of glycoproteins in the cytoplasm of tumor cells.
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PMID:[Ultrastructural cytochemistry of epithelial gland-like component in synovial sarcoma]. 249 43

The surface charge of isolated rat dorsal root ganglion neurones was studied by microelectrophoresis technique. The increase of Ca concentration caused greater reduction of the electrophoretic mobility compared to that produced by an equivalent amount of divalent organic cations, dimethonium or hexamethonium. No charge reversal for Ca concentrations up to 80 mM was observed. These data fit the suggestion that two anion groups of the outer membrane surface can bind one Ca ion with apparent binding constant of about 50 M-1. In solutions of low pH the electrophoretic mobility of cells decreased corresponding to titration of acidic groups with apparent pK = 4.2. Trypsin treatment in mild conditions markedly reduced the surface charge; however, neuraminidase and hyaluronidase did not change it. N-bromosuccinimide (a specific reagent for carboxylic groups of proteins) decreased the electrophoretic mobility about 60%. However, no increase of the surface charge after the action of specific reagents for amino groups (2,4,6-trinitrobenzene-sulfonic acid and maleic anhydride) was observed. It was shown that the surface charge depends also on the intracellular metabolism. If 1 mM dibutyryl cAMP or theophilline was added to the culture medium (thus, raising the concentration of cAMP inside the cell) the surface charge increased. This effect developed slowly and reached its maximum on the third day of incubation. Treatment of cells by 5 mM tolbutamide (an inhibitor of some protein kinases) did not change cell mobility. Addition of 5 mM N-ethylmaleimide (an inhibitor of adenylate cyclase) to the culture medium produced some decrease of the surface charge.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Surface charge of mammalian neurones as revealed by microelectrophoresis. 299 79

The pharmacokinetic interaction of an affinity-purified 125I-labeled tetanotoxin fraction with guinea pig brain synaptosomal preparations was investigated. Binding of tetanotoxin was time- and temperature-dependent, was proportional to protein concentration, and was saturable at about 8 X 10(-9) M as estimated by a solid-surface binding assay. Binding was optimal at pH 6.5 under low ionic strength buffer and was almost entirely blocked by gangliosides or antitoxin. In analogy to intact nerve cells, binding of toxin to membranes resulted in a tight association operationally defined as sequestration. Binding and sequestration were abolished after membrane pretreatment with sialidase. The enzyme could not dissociate the membrane-bound toxin formed at 4 or 37 degrees C under low ionic strength conditions, which is in part compatible with internalization as defined in nerve cell cultures. In the latter system the toxin could be removed at 4 degrees C but not at 37 degrees C. Binding was significantly reduced upon pretreatment of guinea pig brain membranes by a variety of hydrolytic enzymes. Trypsin and chymotrypsin inhibited binding between 55% and 68% while bacterial protease abolished it by 91-95%. The effect was species-specific as it was not seen in rat or bovine synaptosomes. Collagenase and hyaluronidase had little or no inhibitory effect when applied to synaptosomes (27% and 9%) but inhibited binding to synaptic vesicles by 56% and 49%, respectively. Phospholipases A2 and C caused 42-43% inhibition of binding in vesicles and less than 22% in synaptosomes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Affinity-purified tetanus neurotoxin interaction with synaptic membranes: properties of a protease-sensitive receptor component. 302 42

Retinal pigment epithelial cells from normal, Long Evans (LE) and retinal dystrophic (RCS) rats can be grown in vitro (Edwards, 1977). An improved technique is described which permits a more rapid isolation of RPE cells, and routinely gives high cell yields (30,000-40,000/eye), excellent cell viability (95%), and high plating efficiencies (95-100%). Whole eyes are treated with hyaluronidase and collagenase followed by trypsin. These enzymes degrade components of the extracellular matrix, releasing sheets of RPE from adherent attachments to the retina and choroid. Trypsin was then used to dissociate the sheets into single cells. RPE cells are grown to confluence in primary culture. This technique permits RPE cell isolation from both normal and retinal dystrophic (RCS) rats, 8-15 days of age. Normal cells isolated by this technique consistently show excellent phagocytosis in vitro.
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PMID:An improved method for isolation and culture of rat retinal pigment epithelial cells. 405 92

Volume and morphological changes of the squid giant axons in response to hyper- and hypoosmotic media were examined. In hyperosmotic media, which were made by adding sucrose or sodium chloride to the artificial seawater, the axons behaved approximately as ideal osmometers. The fraction of the osmotically inactive volume was less than 0.05. In hypoosmotic media down to half the osmolality of the artificial seawater, intact squid axons did not show significant volume increases. However, following a combined treatment with hyaluronidase and collagenase, the volume of the squid axons increased in these hypoosmotic media. A wrinkled pattern appeared on the surface of the axons while they were in hyperosmotic media containing excess NaCl or KCl. Trypsin treatment prevented appearance of this surface pattern. Furthermore, no such patterns appeared in media which were made hyperosmotic by the addition of sucrose or sodium glutamate.
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PMID:Osmotic properties of the squid giant axon and their modifications. 631 79

Trypsin treatment of viable cells from 24 spontaneous murine mammary carcinomas resulted in a mild but reproducible diminution in their capability to colonise the lung after i.v. reinoculation but did not alter the distribution of deposits formed. The effects were similar on tumours of high and of low colonisation potentials. Neuraminidase and hyaluronidase did not exert any effect on metastatic colonisation potential, although all 3 enzymes were shown to be active and specific in cleaving their purified substrates, under the conditions in which they were used on the cells. Trypsin and neuraminidase were also shown to release characteristic components from the surfaces of living tumour cells, although hyaluronidase did not release detectable quantities of N-acetyl glucosamine indicating that there is little hyaluronic acid-related mucopolysaccharide on the surface of these mammary tumour cells. The results provide direct evidence suggesting that surface protein composition exerts an effect on the metastatic colonisation capability of mammary tumour cells.
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PMID:Effect of enzymic removal of cell surface constituents on metastatic colonisation potential of mouse mammary tumour cells. 662 55

More than half of the extranuclear receptor content of resting cells is associated with cytoplasmic structures. Subfractionation of microsomes reveals a preponderance of "basic" (low electrophoretic mobility) receptor in rough endoplasmic reticulum. Surfynol-dithiothreitol extracts of smooth membranes are rich in "acidic" (high electrophoretic mobility) receptor. Trypsin increases the yields up to seven-fold, and this increase is correlated (r = 0.993) with the acidic receptor content and 5'-nucleotidase activity of these microsomal preparations. Acidic microsomal "cytosolic" and nuclear receptor can be degraded to the "basic" variety of streptomyces hyaluronidase. All forms give rise to a tryptic fragment with unchanged affinity for oestradiol and dimerization ability. Basic receptor isolated after enzymatic conversion of acidic receptor is microheterogenous on isoelectric focusing, but gives rise to only one precipitation arc versus the IgG fraction of a polyclonal antiserum. The precipitation arc can be recharged with labelled oestradiol and autoradiographed. Non-immune IgG's from (unspecific) soluble complexes with oestrogen receptors, but not with their tryptic fragments. The polyclonal antioestrogen receptor IgG fraction precipitates the oestradiol-tagged tryptic receptor fragment from all subcellular sources of all homologous (porcine) and heterologous (human, ovine, bovine, goat, rabbit, guinea pig, rat) target tissues tested. Organ specificity can therefore be excluded and a high degree of phylogenetic conservation of the oestrogen receptor's protein moiety is implied. The presence, in the immune IgG fraction, of steroid releasing antibodies, which apparently distort the binding site, should spur the search for monoclonal antibodies with similar properties.
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PMID:Subcellular distribution, properties and interrelationship of oestrogen receptors in endometrium and other target tissues. 663 34

Ovulated opossum oocytes are surrounded by a zona pellucida, but not by cumulus cells. Opossum sperm carry at least four acrosomal hydrolases (hyaluronidase, acrosin, N-acetylhexosaminidase, and arylsulfatase); the functions of these enzymes in opossum fertilization are uncertain. To identify possible substrates for these hydrolases, the ultrastructure of opossum oocytes was examined after fixation in the presence of ruthenium red which stabilizes extracellular matrices. This oocyte is unusual in having a wide perivitelline space containing a highly structured extracellular matrix (ECM). The ECM is comprised of granules and filaments, and it resembles matrices known to contain hyaluronic acid in other systems. Hydrolases, known to be present in opossum acrosomes, were tested for their effect on the ultrastructure of the zona pellucida and matrix of the perivitelline space. Trypsin dissolved the zona pellucida and decreased the size of the granules in the perivitelline space. Streptomyces hyaluronidase, which specifically attacks hyaluronic acid, removed only matrix filaments. Arylsulfatase, N-acetylhexosaminidase, and beta-glucuronidase did not affect the zona pellucida or ECM in our assay. These observations are consistent with the ideas that (1) opossum sperm must penetrate two oocyte investments, the zona pellucida and ECM of the perivitelline space; (2) the ECM contains hyaluronic acid (filaments) and protein (granules); (3) opossum sperm acrosin may function in penetration of the zona pellucida and ECM; and (4) opossum sperm hyaluronidase may function in penetration of the ECM by degrading hyaluronic acid (filaments). Dissolution of the granules and filaments from oocyte microvilli is probably necessary to permit close apposition and fusion of the sperm and oocyte membranes. The evolutionary significance of these results is discussed.
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PMID:Ultrastructure of opossum oocyte investing coats and their sensitivity to trypsin and hyaluronidase. 671 16


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