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)

Effects of hyaluronidase on myocardial water content and distribution, and on coronary vascular hemodynamics and endothelial cell transport function were assessed in isolated rabbit hearts during 3.5 hours of reperfusion after 30 minutes of global, no-flow ischemia. In nonischemic control hearts, perfusion pressure, left ventricular end-diastolic pressure, maximum +dP/dt, and intravascular clearance of radiolabeled albumin remained constant during 5 hours of continuous perfusion, while the mean-transit time and vascular into extravascular space clearance of radiolabeled albumin increased 1.5X and 2.5X baseline, respectively. During reperfusion after 30 minutes of no flow, perfusion pressure increased 53% and interstitial fluid volume increased 2-fold, while left ventricular end-diastolic pressure and maximum +dP/dt returned to control levels. The rate of intravascular clearance of radiolabeled albumin decreased 38%, and the mean-transit time and vascular-into-extravascular space clearance of albumin increased approximately 3X and 5X baseline, respectively. Hyaluronidase blocked the ischemia-reperfusion-induced increases in total water content and in interstitial fluid volume and reduced the increases in perfusion pressure and mean-transit time of radiolabeled albumin by 40% and 45%, respectively, but did not prevent the increase in albumin vascular-into-extravascular space clearance and the decrease in albumin clearance from the coronary vasculature. These findings indicate that hyaluronidase does not prevent ischemia-reperfusion-induced increases in albumin permeation of the coronary vasculature, and suggest that its protective effect on ischemic myocardium is mediated, instead, by reducing interstitial edema and vascular resistance.
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PMID:Hyaluronidase does not prevent deterioration of vascular functional integrity during reperfusion after no-flow ischemia in isolated rabbit hearts. 400 93

Hyaluronidase release was used as an index of acrosomal membrane damage during cold shock of epididymal boar sperm and ejaculated sperm from intact and vesiculectomized boars. Sperm were also incubated with seminal plasma from intact and vasectomized boars to examine the contributions of male accessory gland secretions. Acrosomal membranes of epididymal sperm were more resistant to cold shock than those of ejaculated sperm. Only 36% of the hyaluronidase released by ejaculated sperm was released by the epididymal sperm in spite of similar hyaluronidase content of the sperm. Preincubation of epididymal sperm in seminal plasma from both intact and vasectomized boars increased resistance to cold shock by 60 to 80%. Initial dilution of epididymal sperm with seminal plasma, rather than Ringer-fructose buffer, was associated with low progressive motility and with retention of cytoplasmic droplets. In contrast, acrosomal membranes of ejaculated sperm from intact and vesiculectomized boars exhibited similar sensitivity to cold shock, releasing hyaluronidase capable of forming .20 and .19 mumol N-acetylglucosamine from hyaluronic acid/10(8) sperm in 8 min. Moreover, seminal plasma from vasectomized boars had no effect on acrosomal sensitivity to cold shock of ejaculated sperm from vesiculectomized boars.
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PMID:Effect of male accessory gland secretions on sensitivity of porcine sperm acrosomes to cold shock, initiation of motility and loss of cytoplasmic droplets. 400 68

The treatment of compartment syndromes in which elevation of intracompartmental pressure occurs is by surgical fasciotomy. This is a relatively simple procedure but may be associated with complications. This study aimed at developing an alternative method to decompress a compartment by use of the enzyme hyaluronidase. Autologous plasma was infused into the anterolateral leg compartments of six dogs to simulate compartment syndromes of 80 mmHg. Pressure decay after pressurization was recorded. The compartment pressures were then again raised to 80 mmHg by subfascial injections of 1500 units hyaluronidase in 2 ml saline injected into one compartment and 2 ml saline only into the control side. Pressure decay was again recorded. On the experimental side, a significantly faster decay rate occurred after hyaluronidase injection than after initial pressurization; 8.0 +/- 1.3 (S.E.M.) versus 3.4 +/- 0.4 (S.E.M.) mmHg/min (p less than .01). Pressure decay after hyaluronidase injection was significantly faster than after the same volume injection on the control side, over both a four-minute period (8.0 +/- 1.3 [S.E.M.] versus 4.1 +/- 0.6 [S.E.M.] mmHg/min [p less than .03]) and a 25-minute period (2.1 +/- 0.3 [S.E.M.] versus 1.3 +/- 0.1 [S.E.M.] mmHg/min [p less than .03]). Hyaluronidase removes hyaluronic acid molecules from the leg compartment fascia and, by facilitating fluid flow from the compartment, causes decompression. Hyaluronidase may then have a place in the prophylaxis and treatment of compartment syndrome, thus avoiding anesthesia and surgery.
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PMID:Decompression of an experimental compartment syndrome in dogs with hyaluronidase. 401 43

The effects of UVA and chlorpromazine on the activity of hyaluronidase were investigated. Hyaluronidase was slightly activated by UVA alone. It was also activated by chlorpromazine, but the activation was enhanced by concomitant UVA irradiation. By pre-irradiation of chlorpromazine, it was found that a stable photoproduct of chlorpromazine was formed that activated hyaluronidase. As activation of hyaluronidase has been described in relation to tissue inflammation, the onset of chlorpromazine-induced photosensitivity may, in part, be related to the hyaluronidase activating effect of chlorpromazine plus UVA.
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PMID:Photoactivation of hyaluronidase by chlorpromazine. 402 15

The length-tension properties of alveolar wall from normal cats were studied before and after exposure to enzymes naturally found in mammals (elastase, trypsin, collagenase, hyaluronidase). Hyaluronidase effected little change while all the proteolytic enzymes altered the mechanical properties of lung tissue. Collagenase removed the "mechanical stop" and the alveolar walls fractured at low forces. The properties of wall exposed to trypsin resembled those of elastase-treated tissue. Elastase increased the extension necessary to reach a given force and increased the maximum length (L(max)) and resting length (L(o)). Maximum extensibility (lambda(max)), the ratio of L(max) to L(o), fell with both elastase and trypsin digestion. A reduction in lambda(max) simulates the changes in alveolar wall properties seen in the lungs of the aged and in those with an irreversible diffuse obstructive pulmonary syndrome (DOPS(I)). Unlike these states, however, the energy loss in stretching alveolar wall increased with elastolysis. Furthermore, the changes in L(o) necessary to effect a change in lambda(max) of alveolar wall comparable to that seen in DOPS(I) were excessive. The altered tissue properties that occur in man with obstructive pulmonary syndromes could not be produced with these proteolytic enzymes or with hyaluronidase.
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PMID:Simulation of tissue properties in irreversible diffuse obstructive pulmonary syndromes. Enzyme digestion. 435 77

1. Electrophoresis of chondroitin sulphate, before and after partial degradation with testicular hyaluronidase, revealed charge heterogeneity of the degraded but not of the intact polymer. 2. Hyaluronidase-treated chondroitin sulphate was fractionated by gel chromatography. Two subfractions which were essentially monodisperse with regard to molecular weight (values of 8600 and 4800, respectively) were separated further by chromatography on Dowex 1. The resulting subfractions differed considerably with respect to their sulphate/disaccharide molar ratios. 3. Amino acid and neutral-sugar analyses of the Dowex 1 subfractions showed that the less sulphated fragments contained the carbohydrate-protein linkage region, whereas the high-sulphated fragments essentially lacked this constituent. It was concluded that chondroitin sulphate contains relatively less sulphate in the vicinity of the carbohydrate-protein linkage region than in the more peripheral portion of the polysaccharide chain.
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PMID:The distribution of sulphate residues in the chondroitin sulphate chain. 516 40

Hyaluronidase activity was examined in 109 specimens of human semen of various sperm densities, seminal plasma, and spermatozoa sedimented by centrifugation. We used a modification of a method originally devised for estimation of hyaluronidase activity in Clostridia and which was bases on measurements of the area of hyaluronate digestion in agar plates. Enzyme activities in both semen and seminal plasma increased with increase in sperm density. The activity in seminal plasma, which appeared promptly after liquefaction and represented enzyme released from spermatozoa, ranged from 31% to 61% of the activity in semen. Activities of spermatozoa in sediments exhibited lower values than those calculated for sperm of whole semen, possibly due to leakage. Both activities, calculated per million sperm cells, gradually increased with decrease in sperm density. The possibility that with severe oligozoospermia the acrosome may become less prone to enzyme release or that the initial activity per cell may increase is discussed. These phenomena would represent additional characteristics of oligozoospermia.
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PMID:Estimation of hyaluronidase activity of human semen and its relationship with sperm density by means of a simplified method. 612 24

Hyaluronidase activity was examined in 104 oligospermic and normospermic human semen specimens promptly after liquefaction, after repeated cycles of washings with a solution containing 1.3 M sucrose and 0.15 M NaCl, and after freezing and thawing. We assessed enzyme activity by measuring areas of the digestion of substrate (hyaluronate). After washing the oligospermic and normospermic semen specimens twice 34%-43% enzyme activity was still present in the sedimented sperm as compared to the initial values. Following additional washings no enzyme activity could be detected. Freezing and thawing of semen increased enzyme activity by 40%-50%, respectively, after the second cycle whereas further treatment did not increase the enzyme activity rate. It is suggested that two types of hyaluronidase are present in human spermatozoa, differing in membrane-binding properties which would be connected with their localization in the acrosome.
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PMID:Hyaluronidase activity in untreated human semen and following laboratory manipulations. 614 Feb 40

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

Monoclonal antibodies to hyaluronidase-treated chondroitin sulfate proteoglycan (CSPG) were used to study the immunological determinants of chick cartilage proteoglycan. The determinants recognized by the antibodies were studied by a radioimmune inhibition assay utilizing hyaluronidase-treated [35S]CSPG. Hyaluronidase-treated CSPG inhibits the reaction of four clonal antibodies, S54C, S103L, S11D, and P100D, with [35S]CSPG, but to varying degrees. Only the reaction of S103L is inhibited to a considerable extent by undigested CSPG, indicating that hyaluronidase treatment exposes determinants specific for the other three antibodies. These findings are consistent with the earlier conclusion that S103L is specific for a protein determinant (Dorfman et al., 1980). Only the reaction of S54C is not significantly inhibited by chondroitinase ABC-digested CSPG. This result indicates that chondroitinase ABC digestion can also expose determinants recognized by S11D and P100D but that such digestion removes the determinant recognized by S54C. Of the four antibodies tested, only the reaction of S54C with hyaluronidase-treated [35S]CSPG is significantly inhibited by chondroitin-6-SO4 tetra- and hexasaccharide (59 and 43% inhibition, respectively, at a concentration of 1333 microM). The reaction of S54C is inhibited to a lesser extent by chondroitin tetra- and hexasaccharide (28 and 26% inhibition, respectively, at a concentration of 1333 microM). In contrast, chondroitin-4-SO4 oligosaccharides do not inhibit the reactions of any of the clonal antibodies. These result suggest that S54C recognizes a determinant that contains chondroitin-6-SO4 oligosaccharide, attached via the linkage oligosaccharide to core protein.
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PMID:Chondroitin 6-sulfate oligosaccharides as immunological determinants of chick proteoglycans. 616 75


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