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 binding of hyaluronate to SV-3T3 cells was measured by incubating a suspension of cells (released from the substratum with EDTA) with 3H-labeled hyaluronate and then applying the suspension to glass fiber filters which retained the cells and the bound hyaluronate. The extent of binding was a function of both the concentration of labeled hyaluronate and the cell number. Most of the binding took place within the first 2 min of the incubation and was not influenced by the presence or absence of divalent cations. The binding of labeled hyaluronate to SV-3T3 cells could be prevented by the addition of an excess of unlabeled hyaluronate. High molecular weight preparations of hyaluronate were more effective in preventing binding than low molecular weight preparations. The binding of [3H]hyaluronate was inhibited by high concentrations of oligosaccharide fragments of hyaluronate consisting of six sugars or more, and by chondroitin. The sulfated glycosaminoglycans (chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate, heparin, and heparan sulfate) had little or no effect on the binding. The labeled hyaluronate bound to the cells could be totally removed by incubating the cells with testicular hyaluronidase, streptomyces hyaluronidase, or trypsin, indicating that the hyaluronate-binding sites are located on the cell surface.
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PMID:Binding of hyaluronate to the surface of cultured cells. 47 11

During the first 10 days after peripheral deafferentation of the mouse olfactory bulb stereoselective binding of L-[3H]carnosine declines markedly. The initial phase of this decline is due to a decrease in binding site stereoselectivity, which is then followed by a loss of assayable binding sites. The specificity of inhibition of L-[3H]carnosine binding by various peptides is also altered after denervation. Competitive inhibitors of carnosine binding become less potent after denervation, while analogues which are not competitive inhibitors remain equipotent before and after denervation. Several carnosine analogues that are normally poor inhibitors become more potent after denervation. Treatment of bulb membranes with trypsin, RNase and hyaluronidase, but not DNase or collagenase, resulted in significant alterations in carnosine binding. L-, but not D-carnosine, protected the binding site from trypsin digestion, and induced additional binding in bulb membranes in a dose-and temperature-dependent fashion. Preincubation of membranes with L-carnosine also led to the induction of additional carnosine binding in membranes from cerebral cortex, cerebellum and deafferentated bulbs but not from muscle. Bulbs from newborn mice contain about one-half of the adult levels of binding and no significant sex differences in carnosine binding were detected in bulbs from adult rats. L-[3H]carnosine binding was two-fold higher in the anterior compared to the posterior portion of the bulb, but there were no significant differences in binding of opiate, GABA, alpha-adrenergic, muscarinic cholinergic, benzodiazepine of glutamic acid receptor ligands.
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PMID:L-[3H]Carnosine binding in the olfactory bulb. II. Biochemical and biological studies. 48 25

Sertoli cells have been insolated from the newborn calf testis using a combination of mechanical and enzymatic disruption. Testicular fragments, previously chopped into 1-mm pieces, are digested in an enzyme mixture consisting of hyaluronidase, collagenase, trypsin and DNAse, followed by a second digestion in trypsin and DNAse. Isolation of the resulting cellular fractions by sedimentation with unit gravity produces an aliquot of Sertoli cells which is over 95% pure when examined by light and electron microscopy. Cultures of these cells grow rapidly and produce Mullerian Inhibiting Substance as evidenced by their ability to cause the involution of the Mullerian duct of the female fetal rat when co-cultured in an organ-culture assay system.
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PMID:The secretion of Mullerian inhibiting substance by cultured isolated Sertoli cells of the neonatal calf. 51 48

Footpad adhesion sites pinch off from the rest of the cell surface during EGTA-mediated detachment of normal or virus-transformed murine cells from their tissue culture substrates. In these studies, highly purified trypsin and testicullar hyaluronidase were used to investigate the selective destruction or solubilization of proteins and polysaccharides in this substrate-attached material (SAM). Trypsin-mediated detachment of cells or trypsinization of SAM after EGTA-mediated detachment of cells resulted in the following changes in SAM composition: (a) solubilization of 50-70% of the glycosaminoglycan polysaccharide with loss of only a small fraction of the protein, (b) selective loss of one species of glycosaminoglycan-associated protein in longterm radiolabeled preparations, (c) no selective loss of the LETS glycoprotein or cytoskeletal proteins in longterm radiolabeled preparations, and (d) selective loss of one species of glycosaminoglycan-associated protein, a protion of the LETS glycoprotein, and proteins Cd (mol wt 47,000 and Ce' (mol wt 39,000) in short term radiolabeled preparations. Digestion of SAM with testicular hyaluronidase resulted in: (a) almost complete solubilization of the hyaluronate and chondroitin sulfate moieties from long term radiolabeled SAM with minimal loss of heparan sulfate, (b) solubilization of a small portion of the LETS glycoprotein and the cytoskeletal proteins from longterm radiolabeled SAM, (c) resistance to solubilization of protein and polysaccharide in reattaching cell SAM which contains principally heparan sulfate, and (d) complete solubilization of the LETS glycoprotein in short term radiolabeled preparations with no loss of cytoskeletal proteins. Thus, there appear to be two distinct pools of LETS in SAM, one associated in some unknown fashion with hyaluronate-chondroitin sulfate complexes, and a second associated with some other component in SAM, perhaps heparan sulfate. These data, together with other results, suggest that the cell-substrate adhesion process may be mediated principally by a heparan sulfate--LETS complex and that hyaluronate-chondroitin sulfate complexes may be important in the detachability of cells from the serum-coated substrate by destabilizing LETS matrices at posterior footpad adhesion sites.
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PMID:Two functionally distinct pools of glycosaminoglycan in the substrate adhesion site of murine cells. 56 61

In the present study we investigated the antiinflammatory effect of pentosanpolysulfate (SP 54) in combination with metamizol using different forms of rat paw edema (induced by dextrane, hyaluronidase, trypsin, formaldehyde, carragenine or kaolin). After s. c. application Probaphen, a new drug containing pentosanpolysulfate, metamizol, and lidocaine, proved in our experiments to exert an antiphlogistic effect about 40% stronger than the equivalent amount of SP 54 alone. Since pentosanpolysulfate by itself has no analgetic activity, its combination with metamizol results in a formulation which is not only a more potent antiinflammatory drug but will aslo counteract pains which accompany most edematous reactions. Probaphen may therefore be suggested for the treatment of rheumatoid arthritis and similar inflammatory and edematous processes. First clinical studies and reports on Probaphen fully support our pharmacological results.
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PMID:[Pharmacological studies on the antiphlogistic effect of pentosanpolysulfate in combination with metamizol]. 57 70

Studies have been made on the effect of trypsin, chymotrypsin, pronase, lipases, hyaluronidase and digitonin on electrophysiological properties of the neurons of the snail H. pomatia under external application. Proteases and lipases gradually depolarize the neuronal membrane, decrease the amplitude and prevent the onset of action potentials, initially increase and then decrease the membrane resistance. The decrease in the membrane resistance coincides with the period of maximum inhibition of resting and action potentials in the neurons. The enzymes studied do not affect the membrane capacitance. Changes in electrophysiological characteristics induced by the enzymes are partially reversible provided the preparation is soaked in Ringer's solution for a sufficient time. Digitonin rapidly and irreversibly depolarizes the membrane, decreases its resistance and blocks action potentials. Hyaluronidase does not significantly affect neuronal electrophysiological properties when applied solely, but facilitates the development of changes during subsequent effect of proteases.
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PMID:[Effect of hydrolases and digitonin on the electrophysiological characteristics of the neurons of the snail, Helix pomatia]. 67 79

The chorionic villi of placentas, 10 to 40 weeks of gestation, were examined for A and B blood group antigens with an immunoferritin technique. No specific ferritin attachment was shown on the plasma membrane of the villous trophoblasts. Furthermore, after trophoblast cell-surface mucosubstances (perhaps the barrier of the placental antigenicity, according to some authors) were digested with several enzymes, such as neuraminidase, hyaluronidase, chondroitinase ABC, pepsin, trypsin, and pronase, no ferritin tagging was observed on the plasma membrane of the villous trophoblasts. We have concluded that our failure to detect the A and B blood group antigens was not due to the masking of antigens by mucosubstance coating the trophoblasts, but was due to the intrinsic deficit of those antigens in the plasma membrane of the human trophoblasts.
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PMID:Innumoelectron microscopy of the human chorionic villus in search of blood group A and B antigens. 79 65

An analysis of the cell surface antigens of Streptococcus equi is presented. Following extraction from cell walls, whole cells and hyaluronidase treated cells the immunoprecipitation patterns of the intact and protease treated components were developed with rabbit anti serum against S. equi. It was determined by mouse protection tests that the specificity of protective antibodies was directed toward a trypsin labile antigen. The presence of antigens similar to those designated M and R in Group A streptococci were found in S. equi.
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PMID:The cell surface antigens of Streptococcus equi. 80 79

The oxidation of 3,4-dihydroxyphenylalanine (DOPA) was studied by spectrophotometric methods at pH 6.8. In the presence of L- or D-DOPA, a color development occurred in the presence of the following substances as measured by increase in absorption both at 540 nm and 480 nm: hyaluronic acid, trypsinized human skin and umbilical cord extract, trypsin treated rat tissue from subcutaneous rat leproma, trypsin treated M. lepraemurium isolated from rat lepromata, and trypsinized M. leprae isolated from non-treated lepromatous leprosy cases. Normal human skin and connective tissue extract and nontrypsinized connective tissue of rat leprosy granuloma did not oxidize DOPA. While the trypsin-treated partially purified M. leprae suspension oxidized DOPA at both wave-lengths, the hyaluronidase-treated same suspension of M. leprae failed to oxidize these phenolic compounds. Mushroom tyrosinase oxidized D-DOPA, L-DOPA, epinephrine and norepinephrine at 480 nm. Hyaluronic acid also oxidized epinephrine and norepinephrine at both wave-lengths. Since it is known that M. leprae in the human host is closely associated with the presence of the acid mucopolysaccharides of the skin, and since acid mucopolysaccharides and skin constituents strongly oxidized DOPA, and since the hyaluronidase treated M. leprae failed to oxidize DOPA, it became evident that hyaluronic acid and not M. leprae is responsible for DOPA oxidation, and phenolase activity is not associated with the metabolism of M. leprae. Evidence is presented that DOPA is not a unique characteristic of the human leprosy bacillus. For instance, trypsin-treated murine leprosy bacilli from the rat strongly oxidized DOPA. The reaction of DOPA oxidation, therefore, must be rejected as a test for the identification of M. leprae. The obtained results confirmed the pertinent findings of Skinsnes and his co-workers.
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PMID:Oxidation of 3,4-dihydroxyphenylalanine by connective tissue constituents. Identification of Mycobacterium leprae not related to phenolase activity. 82 25

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4


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