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)

Proper function of the coronary blood-tissue exchange system may be important in the preservation of myocardium threatened by ischemia. We have undertaken studies aimed at elucidating the functions of this system under baseline and ischemic conditions. The exchange of [14C]sucrose between the coronary capillaries and extravascular space has been studied with the multiple-tracer method. Protein transport has been examined by measuring the deposition of labeled albumin and by collecting cardiac lymph. Results indicate that reduced-flow ischemia decreases functioning capillary surface area but increases permeability to small molecules and protein. Hyaluronidase and adenosine can restore flow after partial occlusion of the coronary artery. However, only hyaluronidase restores capillary surface to its baseline value. Thus, ischemic effects on exchange are not controlled merely by hemodynamic factors. Reduced-flow ischemia in the heart can induce a vascular permeability change in the lung circulation. We conclude that capillary and interstitial transport are altered significantly by ischemia. Preservation of the proper function of these processes may be important in protecting the ischemic myocardium.
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PMID:Tracer exchange in the normal and ischemic coronary circulation. 669 35

Human liver hyaluronidase was purified to homogeneity by (NH4)2SO4 fractionation, chromatography on hydroxyapatite and DEAE-cellulose, and preparative disc polyacrylamide-gel electrophoresis. The enzyme had a pH optimum of 3.8-4.0, a molecular weight (determined by gel filtration) of 76000, and a Km of 0.05 mg/ml for purified human umbilical-cord hyaluronic acid. It generally resembled hyaluronidases studied in other tissues which are believed to be lysosomal, but shared a number of characteristics with a partially purified bovine testicular hyaluronidase. Neither enzyme exhibited inhibition by high concentrations of substrate, but both were competitively inhibited by dermatan sulphate and keratan sulphate. Both enzymes exhibited increased activity in the presence of albumin, probably owing to an increased susceptibility of substrate to enzyme action. The liver enzyme was inhibited by NaCl, but the testicular enzyme exhibited an increase in activity in the presence of the salt which was similar to the effect observed with albumin. The different response toward Cl- ion appeared to be the most significant difference between the two enzymes.
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PMID:Purification and properties of hyaluronidase from human liver. Differences from and similarities to the testicular enzyme. 712 84

The binding of albumin to the glomerular capillary wall was studied using albumin-gold in perfused kidneys, the interaction of [3H]albumin with isolated glomeruli at 37 degrees C and 4 degrees C and the interaction at [3H]albumin with purified basement membrane. The albumin-gold was found to bind predominantly to the basement membrane and this interaction could be dissociated with high concentrations of albumin. There was binding of albumin to isolated rat glomeruli which exhibited temperature dependence. Glomeruli exhibited a binding site at both 37 degrees C and 4 degrees C with an association constant in the range of 1 to 3 x 10(4) M-1 that bound 7 x 10(13) molecules/glomerulus. At 37 degrees C, however, there was anomalous Scatchard binding behaviour at relatively higher concentrations of albumin (30 to 50 mg/ml) which could be due to either glomerular cell uptake or the appearance of multiple binding sites or both. The binding of albumin to isolated glomeruli and the glomerular albumin levels in isolated kidney perfusion could largely be accounted for by the binding of albumin to the glomerular basement membrane. The albumin binding to glomeruli at 37 degrees C was enhanced by Pronase digestion and heparinase digestion, but remained unchanged following trypsin treatment or neuraminidase treatment. Similarly, albumin was shown to bind to purified basement membrane preparations. This binding was also enhanced (approximately 80 times) by heparinase digestion but remained unchanged after digestion with chondroitinase ABC or hyaluronidase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Albumin interaction with the glomerular capillary wall in vitro. 778

Previous studies showed that the flows of albumin and hyaluronidase solutions increased relative to that of saline in isolated segments of rabbit lung interstitium (Lai-Fook et al. J. Appl. Physiol. 67:606-613, 1989). We questioned whether these effects were hydration dependent. In interstitial segments the flows of lactated Ringer, albumin (5 and 10 g/dl), and hyaluronidase (0.02%) solutions were measured at mean interstitial pressures (Pm) between -5 and 15 cmH2O with a constant driving pressure of 5 cmH2O. The albumin-to-Ringer flow ratio increased monotonically from near the viscosity-dependent value (0.75-0.77) at -5 cmH2O Pm to values of 1.6-2.1 at 15 cmH2O Pm. A similar behavior was observed for the flow of the hyaluronidase solution relative to that of Ringer solution. The increased permeability response to albumin was independent of the albumin concentration used. By contrast, the response to hyaluronidase was lower when the interstitium was perfused with the higher concentration albumin solution (10 g/dl) before the flow of hyaluronidase, indicating an inhibitory effect of albumin on the hyaluronidase response. Estimates of interstitial hydration from Pm indicated an increased interstitial permeability (conductivity) to the flows of albumin and hyaluronidase solutions only after interstitial volume had doubled, whereas interstitial permeability was viscosity dependent at normal interstitial hydration.
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PMID:Effect of hydration on lung interstitial permeability response to albumin and hyaluronidase. 817 66

This study demonstrated that semenogelin I and II, the predominant and the major basic human seminal coagulum proteins respectively were shown to be potent activators of sperm hyaluronidase. These proteins stimulated the activity of bovine testicular hyaluronidase, goal cauda sperm hyaluronidase and human ejaculated sperm hyaluronidase. Human seminal plasma protein, which predominantly contains the basic degradation residues of the basic coagulum proteins and albumin (pI 4.7) and which is also basic at the assay pH 3.8, also showed activation of bovine testicular hyaluronidase while acidic pepsin (pI < 1.0) exhibited no such activation. The findings may be utilized as an assay method for comparative evaluation of specific activation units of the purified basic seminal coagulum proteins or their cleavage products and for quantifying the total basic protein (pI > 3.8) units in human seminal plasma. One unit of the coagulum protein was defined as the amount of the activator that increases 1 mIU of hyaluronidase activity by 50%. The specific activity of the 57 kDa and 75-79 kDa coagulum proteins, and that of serum albumin against Sigma bovine testicular hyaluronidase (type IV), were 11,447, 8600 and 6252 units per mg protein respectively. It was speculated that human seminal coagulum proteins may have an activation effect on spermatozoal hyaluronidase activity in vivo.
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PMID:Sperm hyaluronidase activation by purified predominant and major basic human seminal coagulum proteins. 858 73

Guanidinobenzoatase (GB), a serine proteinase with a molecular weight of 71,000, is found both free in the epididymal fluids of the mouse and bound to the sperm surface. Microgram quantities of the enzyme, purified from epididymal fluid, will completely disperse follicle cells from freshly ovulated oocytes after 15 min of incubation. Purified GB exhibits no hyaluronidase activity as determined by the acid albumin assay. The ability of GB to disperse follicle cells is blocked by a proteinase inhibitor endogenous to the male reproductive tract. The inhibitor has no effect on bovine testicular hyaluronidase. Although the function of GB has not been defined, the observations presented here indicate that it may play a role in cumulus matrix penetration during fertilization.
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PMID:Cumulus cell dispersal from murine oocytes by an epididymal guanidinobenzoatase. 929 43

Hyaluronidase, a matrix-degrading enzyme, was assayed in extracts from breast primary tumors and regional metastases using a pool of human sera as a standard. Optimal activities of tumor extracts and serum were found for concentrations of 0.15-0.20 M NaCl in pH 3.8-4.0 buffer. In evaluating contamination by serum due to vascular proliferation, we expressed our results as the ratio of the entire activity (mU/l extract) on serum albumin content of tumors (g/l). Median (interquartile range) activities were 9.02 (6.04-14.34) for primary tumors and 37.36 (24.06-99.63) mU/g albumin for metastases. The difference was significant. Zymographic analysis showed that 3 bands of activity were detected which corresponded to 68, 53 and 49 kDa for tumoral hyaluronidase. The same pattern was observed for cellular extracts of breast cancer cell line CAL51, demonstrating that hyaluronidase detected in tumor extracts had mainly a cellular origin. Our results suggest that hyaluronidase may be involved in the metastatic process.
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PMID:Increased hyaluronidase levels in breast tumor metastases. 935 77

Hyaluronidase is a protein whose enzymatic activity is successfully employed in extravasation therapy. Taking into account that several proteins (e.g. gelatin and albumin) have been employed as natural polymers for the preparation of microspheres, this work approaches a comprehensive investigation on hyaluronidase injectable microparticles. The goals are either to obtain a sustained release preparation of hyaluronidase or to use the enzyme as drug carrier. Microspheres have been prepared using a water-in-oil emulsification technique, and they have been crosslinked either by thermal or chemical means. Results show that hyaluronidase microspheres with good morphological characteristics can be obtained by this preparation method. Manufacturing variables influence the enzymatic activity of the microspheres, which can be highly preserved under mild experimental conditions. Moreover, the suitability of this enzyme as a microparticulate drug carrier has been shown by the successful encapsulation of hydrocortisone sodium succinate.
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PMID:Hyaluronidase-injectable microparticles intended for the treatment of extravasation. 946 10

Mastitis caused by environmental pathogens is a major problem that affects many well-managed dairy herds. Among the environmental pathogens, Streptococcus dysgalactiae is isolated frequently from intramammary infections during lactation and during the nonlactating period. In spite of its high prevalence, little is known about factors that contribute to the virulence of S. dysgalactiae. During the last decade, several cell-associated and extracellular factors of S. dysgalactiae have been identified; yet, the relative importance of these factors in the transmission and pathogenesis of mastitis caused by S. dysgalactiae has not been defined. Streptococcus dysgalactiae can interact with several plasma and extracellular host-derived proteins such as immunoglobulin G, albumin, fibronectin, fibrinogen, collagen, vitronectin, plasminogen, and alpha 2-macroglobulin. These interactions are mediated by bacterial surface proteins. This organism also produces hyaluronidase and fibrinolysin which may be involved in promoting dissemination of the organism into host tissue. Streptococcus dysgalactiae adheres to and is internalized by bovine mammary epithelial cells in vitro. Involvement of host cell kinases, intact microfilaments and de novo eukaryotic protein synthesis are required for internalization of S. dysgalactiae into bovine mammary epithelial cells; a process that appeared to occur by a receptor-mediated endocytosis mechanism. However, de novo bacterial protein synthesis was not required for epithelial cell internalization. Furthermore, S. dysgalactiae survived within mammary epithelial cells for extended periods of time without losing viability or damaging the eukaryotic cell. Further research on characterization of host-pathogen interactions that take place during the early stages of mammary gland infection will enhance our understanding of pathogenesis of intramammary infection which may contribute to development of methods to minimize production losses due to mastitis.
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PMID:Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis. 964 69

The present study was conducted to investigate the effects of hyaluronidase on elastase-induced lung injury in rats. Male Wistar rats were divided into 4 groups: 1) Control group, single tracheal instillation of 0.3 ml saline; 2) PPE group, single tracheal instillation of 120 micrograms porcine pancreatic elastase (PPE); 3) HD group, intravenous injection of 240 mg/kg hyaluronidase (HD); and 4) HE + PPE group, intravenous injection of HD before single tracheal instillation of PPE. Cellular component and protein concentration in bronchoalveolar lavage fluid (BALF), myeloperoxidase (MPO) activity and hyaluronan content in lungs were examined 24 hours after treatment. After 8 weeks of treatment, hyaluronan content in the lungs and physiological parameters such as total lung capacity (TLC), functional residual capacity (FRC) and static compliance (Cst) were examined. The number of BALF nucleated cells in the HD + PPE group 6 h after treatment, and lung MPO activity in the HD group after 1 h and 3 h. were both higher than the corresponding measurements in the PPE group. After 6 h of treatment, the number of BALF nucleated cells in the HD + PPE group was significantly higher than in the HD group. The BALF albumin concentrations in the HD + PPE and HD groups were also significantly higher than in the control group. After 8 weeks of treatment, the measurements of TLC and Cst indicated greater emphysematous changes in the HD + PPE group. These results suggest that decreased interstitial HA accelerates acute inflammation and emphysematous changes in elastase-induced lung injury.
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PMID:[Effect of hyaluronidase on porcine pancreatic elastase-induced lung injury]. 980 7


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