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)

Human teratocarcinoma-derived cells of line PA 1, which are capable of differentiating in vitro [Zeuthen, J. et al. (1980) Int J. Cancer, 25, 19-32], incorporate label from radioactive sulfate and/or glucosamine into several large-sized glycosaminoglycans including hyaluronate, chondroitin sulfate/dermatan sulfate co-polymers, heparan sulfate and keratan-sulfate-like molecules. All these polysaccharide fractions were identified by specific degradation methods. The labeled hyaluronate was degraded into a mixture of unsaturated octa-, hexa- and tetra-saccharides by a treatment with Streptomyces hyaluronidase (EC 4.2.2.1). The chondroitin sulfate/dermatan sulfate co-polymers were cleaved with chondroitin AC lyase (EC 4.2.2.5) into unsaturated disaccharides and a series of unsaturated oligosaccharides; the latter were degraded by a treatment with chondroitin ABC lyase (EC 4.2.2.4) into unsaturated disaccharides. Heparan sulfate was degraded with nitrous acid into free inorganic [35S]sulfate and a series of [35S]sulfate-labeled oligosaccharides and/or glycopeptides. The keratan-sulfate-like molecules were hydrolyzed by a treatment with endo-beta-galactosidase from Escherichia freundii into a series of distinct [35S]sulfate-labeled oligosaccharides; small oligosaccharides were liberated also from [3H]galactose-labeled molecules. The smallest one of the liberated oligosaccharides was tentatively identified as a sulfated disaccharide.
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PMID:Cell-associated glycosaminoglycans of human teratocarcinoma-derived cells of line PA 1. 680 34

An enzymatic profile of 20 strains of Pseudomonas maltophilia was undertaken with conventional plate tests, API ZYM, and 4-methylumbelliferyl-conjugated substrates. All strains produced DNase, RNase, arbutinase, esterases and lipases, mucinase, acid and alkaline phosphatases, alkaline pyrophosphate diesterase, phosphoamidase, beta-glucosidase, leucine arylamidase, and acetatase and were hemolytic for horse, sheep, and rabbit blood. The majority of strains produced chitinase, hyaluronidase, albuminase, valine arylamidase, trypsin, alpha- and beta-glucosidases, and N-acetyl-beta-glucosaminidase. API ZYM and 4-methylumbelliferyl-conjugated substrate assays are rapid, simple, specific, and sensitive and may be useful as diagnostic aids in the identification of P. maltophilia and other pseudomonads.
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PMID:Enzymatic profile of Pseudomonas maltophilia. 681 50

Hyaluronidase, also called the spreading factor, may be an important pathogenic factor for the streptococci. Production of hyaluronidase is found in 75% of human clinical isolates of group B streptococci, and we have in our investigation found the same frequency (74%) in 195 bovine isolates. Of the same 195 isolates 17% turned out to be lactose negative, a characteristic usually regarded as being typical of group B streptococci of human origin. These same strains were also mostly hyaluronidase positive. The parameters investigated: hyaluronidase production, lactose and salicin fermentation and phage-typability, can be useful in tracing the origin of the group B. However, bovine and human streptococcal populations do not seem to be completely distinguishable because overlapping exists between the characteristics.
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PMID:Hyaluronidase production, lactose and salicin fermentation and phage-typability in bovine group B Streptococci. 703 59

There cutaneous propionibacteria - Propionibacterium acnes, P. avidum and P. granulosum - were grown in chemostats using semi-synthetic medium with various concentrations of glucose. Biomass rose with increasing glucose concentration up to 0.3-0.4% (w/v) and then remained constant. Propionibacterium granulosum had both a low yield and low mumax when grown in the absence of glucose suggesting that this organism is essentially 'saccharolytic' in its nutrition. In contrast, P. acnes and P. avidum had higher growth yields than P. granulosum and showed their highest mumax values in the absence of glucose. Extracellular lipase, hyaluronidase (hyaluronate lyase) and acid phosphatase activities varied with different glucose concentrations, but in all cases were lowest at the highest glucose concentration tested (0.5%, w/v).
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PMID:Effects of glucose concentration n biomass, maximum specific growth rate and extracellular enzyme production by three species of cutaneous Propionibacteria grown in continuous culture. 734 43

The Staphylococcus aureus 8325-4 hyaluronate lyase gene (hysA) was identified after detecting hyaluronate lyase activity expressed by phages from a genomic library. The hysA open reading frame, capable of encoding a protein of 91 980 Da, was identified by Tn5 mutagenesis and nucleotide sequencing. HysA shares 35 and 36% amino acid sequence identity with group B streptococcal hyaluronate lyase and pneumococcal hyaluronidase, respectively. A 94-kDa protein was expressed in Escherichia coli minicells, a result consistent with the coding capacity of hysA. Identification of the S. aureus 8325-4 hyaluronate lyase gene will allow the regulation of this putative virulence determinant to be studied.
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PMID:Cloning, nucleotide sequence determination and expression of the Staphylococcus aureus hyaluronate lyase gene. 755 1

The new cantharanthine-modified vinca alkaloid vinorelbine (Navelbine) was administered intradermally (ID) to dehaired BALB/c mice. Dose-dependent skin lesions were produced over the range 0.01-0.5 mg/mouse, with complete healing after 9-35 days. Local (ID) injections of hydrocortisone and saline were ineffective at blocking vinorelbine-induced skin ulceration. Topical skin heating to 43 degrees C or cooling to 10 degrees C were also ineffective. In contrast, hyaluronidase, 15 Units ID, following vinorelbine significantly reduced skin lesions. These results show that vinorelbine is a vesicant and that inadvertent extravasations may be managed with subcutaneous injection of the spreading factor enzyme, hyaluronidase.
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PMID:Antidote studies of vinorelbine-induced skin ulceration in the mouse. 762 47

Changes in colonic faecal microflora, enzymes of colonic energy metabolism, of cell proliferation and lipid profile in the serum and colon were studied in 48 mice exposed to cycas and fed a Nigeria-type diet. The animals were divided into three diet classes of 16 mice per class, and each class of animals was fed ad libitum either a normal diet, a high-carbohydrate high-fibre (HCF) diet or a high-protein high-fat (HPF) diet. Each diet class was subdivided into two equal groups of 8 animals each. One group was fed a diet type (acted as the diet control) without cycas, and the other group was fed the corresponding diet with cycas. The study period lasted for 3 weeks. The colonic faecal materials were acidified in the HCF-fed mice compared with the other diet-fed mice. Faecal beta-glucuronidase activity was significantly (p < 0.05) increased in the cycas-fed mice compared with the diet controls. Feeding mice with the HPF diet significantly (p < 0.05) increased beta-glucuronidase and mucinase activities. Colonic phosphofructokinase, glucose 6-phosphate dehydrogenase, lactate dehydrogenase and hyaluronidase activities were also significantly (p < 0.05) elevated in the cycas-treated mice. Feeding mice with the HPF diet also significantly (p < 0.05) increased these enzyme activities. Mice fed with the HCF diet significantly (p < 0.05) lowered serum total cholesterol, triglyceride and colonic total lipid. Colonic phosphatidylethanolamine and phosphatidylcholine were significantly (p < 0.05) increased in the HPF-fed mice. This study shows that the HCF diet alters the colonic faecal environment, colonic energy metabolism and hyaluronidase activity in ways which suggest its protective ability against the development of colon cancer in mice.
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PMID:Early biochemical events in mice exposed to cycas and fed a Nigerian-like diet. 787 55

The enzyme, hyaluronidase, detected in crude venom was active over a pH range of 4-9 and was stable to at least a 72 hr storage at 4 degrees C. Preparative electrofocusing indicated a pI value for this enzyme between 9.5 and 10.2. Hyaluronidase partially purified by gel-filtration chromatography was evaluated as a spreading factor for dermonecrosis provoked by the nematocyst venom on depilated rats. The spread of dermonecrosis increased regardless of the presence or absence of hyaluronidase. Hemolytic activity of crude venom was assayed on erythrocyte suspensions from various sources. Pig and rat erythrocytes were the most sensitive to the hemolysin of the erythrocytes tested. The pH optima for the hemolysin was 8.3. Trypsinized rat erythrocytes were more susceptible to hemolysis induced by venom than non-trypsinized cells. The monovalent and divalent cations KCl, BaCl2, CaCl2, and MgCl2 were inhibitory to hemolytic activity induced by crude venom. The hemolysin partially purified by gel-filtration chromatography tested for stability after overnight storage at 4 degrees C and -70 degrees C indicated a 50% and 75% loss of activity, respectively, in comparison to the hemolytic activity recovered directly after gel-filtration chromatography.
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PMID:Characteristics of hyaluronidase and hemolytic activity in fishing tentacle nematocyst venom of Chrysaora quinquecirrha. 790 65

DG42 is one of the main mRNAs expressed during gastrulation in embryos of Xenopus laevis. Here we demonstrate that cells expressing this mRNA synthesize hyaluronan. The cloned DG42 cDNA was expressed in rabbit kidney (RK13) and human osteosarcoma (tk-) cells using a vaccinia virus system. Lysates prepared from infected cells were incubated in the presence of UDP-N-acetylglucosamine and UDP-[14C]glucuronic acid. This yielded a glycosaminoglycan with a molecular mass of about 200,000 Da. Formation of this product was only observed in the presence of both substrates. The glycosaminoglycan could be digested with testicular hyaluronidase and with Streptomyces hyaluronate lyase but not with Serratia chitinase. Hyaluronan synthase activity could also be detected in homogenates of early Xenopus embryos, and the activity was found to correlate with the expression of DG42 mRNA at different stages of development. Synthesis of hyaluronan is thus an early event after midblastula transition, indicating its importance for the ensuing cell movements in the developing embryo. Our results are at variance with a recent report (Semino, C. E. & Robbins, P. W. (1995) Proc. Natl. Acad. Sci. USA 92, 3498-3501) that DG42 codes for an enzyme that catalyzes the synthesis of chitin-like oligosaccharides.
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PMID:Cells expressing the DG42 gene from early Xenopus embryos synthesize hyaluronan. 864 40

Hyaluronic acid was treated exhaustively with a hyaluronate lyase (hyaluronidase, EC 4.2.2.1) from Streptomyces hyalurolyticus to obtain a tetrasaccharide and a hexasaccharide product in a molar ratio of 1 to 1.2. The tetrasaccharide product was fluorescently labeled at the reducing end by reductive amination with 7-amino 1,3-naphthalene disulfonic acid (AGA) and the structure of the conjugate was determined spectroscopically. Partial treatments of hyaluronic acid with hyaluronate lyase afforded complex mixtures of oligosaccharides that were similarly fluorescently labeled. These labeled oligosaccharide mixtures were analyzed using high-resolution capillary electrophoresis. The resulting electropherograms showed the content of each hyaluronic acid derived oligosaccharide, having a degree of polymerization (dp) from 4 to 50, throughout the enzymatic reaction. Computer simulation studies gave comparable kinetic profiles suggesting that hyaluronate lyase exhibits a random endolytic action pattern. Interestingly, oligosaccharides of certain size (dp) were under-represented in these oligosaccharide mixtures suggesting that linkages at spacings of 10 to 12 saccharide units are somewhat resistant to this enzyme. The cause of this resistance might be the result of secondary or higher order structural features present in the hyaluronic acid polymer.
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PMID:Exploration of the action pattern of Streptomyces hyaluronate lyase using high-resolution capillary electrophoresis. 904 98


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