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)

The presence of hyaluronoglucosidase (EC 3.2.1.35; hyaluronidase), beta-N-acetylglucosaminidase (EC 3.2.1.30), exo-1,4-beta-xylosidase (EC 3.2.1.37), and arylsulfatase (EC 3.1.6.1) in dentinogenically active odontoblasts isolated from the rat incisor has been demonstrated by means of biochemical methods. The possible function of these enzymes in relation to the calcification process is discussed.
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PMID:Acid hydrolases in the odontoblast-predentin region of dentinogenically active teeth. 0 47

Buffalo sperm acrosome resembles its counterpart in other species, being rich in hydrolytic enzymes. Of the enzyme activities estimated, acid phosphatase, beta-N-acetylglucosaminidase and hyaluronidase were low compared to those of ram semen. However, the aryl sulphatase activity was high. GOT activity estimated in sperm preparation may not be of acrosomal origin.
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PMID:Acrosomal hydrolases in buffalo spermatozoa. 0 85

Some important enzymes concerned with the biosynthesis of the precursors of glycosaminoglycans (gg), degradation of gg and biological sulphation have been studied in rats fed an atherogenic diet. L-Glutamine-D-fructose-6-phosphate amino-transferase and glucosamine-6-phosphate-N-acetylase--2 enzymes concerned with the biosynthesis of hexosamine precursors of gg--decreased in the liver in rats fed the atherogenic diet. UDPG pyrophosphorylase, UDPG dehydrogenase and UDPG glucuronic acid-5'-epimerase, which are concerned with the biosynthesis of the uronic precursors of gg, also decreased in the liver in the diet-fed rats. The activities of some of the enzymes concerned with degradation of gg-hyaluronidase, beta-glucuronidase beta-hexosaminidase, cathepsin and aryl sulphatase--increased both in the liver and aorta. The hepatic concentration of PAPS significantly decreased in the diet-fed rats. The sulphate-activating system, which includes ATP sulphurylase, APS kinase and sulphotransferase, also decreased. Thus the overall picture is one of decreased synthesis of gg and their increased degradation in the atheromatous rats.
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PMID:Metabolism of glycosaminoglycans in atheromatous rats. Enzymes concerned with synthesis, degradation and sulphation of glycosaminoglycans. 12 76

The effect of low and high doses of ascorbic acid on glycosaminoglycan and lipid metabolism was studied in guinea pigs fed both normal and atherogenic diets. The high dose of ascorbic acid (25 mg/100 g body weight/day) decreased the cholesterol level in the liver and aorta but not in the serum in animals fed the normal diet in comparison with those fed the low dose of ascorbic acid (0.1 mg/100 g body weight/day). In animals fed the atherogenic diet, cholesterol decreased in the serum and liver, but not in the aorta. Serum triglycerides were not affected by the dose of ascorbic acid in the group on the normal diet, but in the animals receiving the atherogenic diet, the high dose of ascorbic acid caused serum triglycerides to decrease when compared with the low dose. Hepatic and aortic triglycerides decreased in groups on normal and atherogenic diets receiving the high dose of ascorbic acid. Lipoprotein lipase activity was not affected in the aorta by the dose of ascorbic acid either in the normal or atherogenic diet group. It was increased in the liver and heart in both the groups receiving the low dose of ascorbic acid but decreased in the high dose group. The concentration of all the glycosaminoglycans significantly increased in the aorta of animals on normal diet receiving the high dose of ascorbic acid when compared with the low dose group. In the group on the atherogenic diet, hyaluronic acid was not affected, but all the sulphated glycosaminoglycans increased in the animals receiving the high dose when compared with those receiving the low dose. In the liver all the sulphated glycosaminoglycans increased while hyaluronic acid decreased in both the normal and atherogenic diet groups receiving the high rather than the low dose of ascorbic acid. L-Glutamine:D-fructose-6-phosphate aminotransferase and UDPG dehydrogenase, two key enzymes in the biosynthesis of precursors of glycosaminoglycans, were studied in relation to the dose of ascorbic acid. Hepatic aminotransferase activity was higher both in the normal and atherogenic diet groups when receiving the high rather than the low dose of ascorbic acid. UDPG dehydrogenase was not affected by the dose of ascorbic acid. The activities of the degrading enzymes -- hyaluronidase, beta-glucuronidase, beta-hexosaminidase and aryl sulphatase -- significantly increased both in the normal and atherogenic diet groups when receiving the low rather than the high dose of ascorbic acid. The concentration of PAPS, sulphate activity and sulphotransferase activity were all increased in both the normal and atherogenic diet groups receiving the high dose of ascorbic acid.
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PMID:Ascorbic acid and glycosaminoglycan and lipid metabolism in guinea pigs fed normal and atherogenic diets. 12 67

Bovine testicular hyaluronidase (endo-beta-N-acetyl hexosaminidase) has a significant corrective effect on cultured Hurler fibroblasts. Nonspecificity of this effect is indicated by its equally strong corrective effect on Hunter fibroblasts. Although all specimens of hyaluronidase also possessed iduronidase activity, a separate corrective effect could be attributed to the endo-N-acetyl hexosaminidase activity of at least one hyaluronidase (Wyeth M-151) for four reasons: (i) its very low content of iduronidase activity; (ii) a decrease in intracellular macromolecular mucopolysaccharides (believed to be largely dermatan sulfate) with a corresponding increase in intracellular and extracellular oligosaccharides; (iii) no measurable increase in iduronidase activity of hyaluronidase-treated cells despite near maximal correction; (iv) direct correlation between Hurler cell correction and hyaluronidase activity when enzymes of different strength were used at less than maximal correction.
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PMID:In vitro correction of Hurler fibroblasts with bovine testicular hyaluronidase. 13 20

A potential enzymic mechanism for the degradation of glycosaminogly cans was characterised using enzymes found in rheumatoid synovial fluid from the knee joint. This mechanism involves a true hyluronidase together with the concerted action of beta-glucuronidase and beta-N-acetylhexosaminidase. The contribution of the exopolysaccharidases to hyaluronate degradation was demonstrated by the use of specific inhibitors, while the distinct identity of a true hyaluronidase was shown by ammonium sulphate and agarose gel column fractionations. Only the hyluronidase fraction was capable of degrading high molecular weight hyaluronate. The exopolysaccharidase activities were shown to be markedly elevated in rheumatoid as compared to osteoarthritic synovial fluid and also normal serum. On the other hand, hyluronidase was similarly active in rheumatoid and osteoarthritic synovial fluids; both these levels were lower than that of normal human serum. Hyaluronidase in synovial fluid may thus be derived by diffusion from serum, since it is of relatively low molecular weight (60 000). The pH requirements of this enzyme system and the strong inhibition of hyaluronidase by synovial fluid make it unlikely that the mechanism operates extracellularly. It is proposed that as a lysosomal mechanism, however, it is an important contributing factor in the chronic erosion process characteristic of rheumatoid arthritis.
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PMID:The characterisation and function of the polysaccharidases of human synovial fluid in rheumatoid and osteoarthritis. 23 48

Glycosidases capable of degrading intercellular matrix components were investigated in a 32P induced rat osteosarcoma. Homogenates of ossifying tumour were shown to readily degrade hyaluronic acid, chondroitin sulphates 4 and 6 but not dermatan sulphate. High levels of the exoglycosidases, beta-glucuronidase and beta-N-acetylglucosaminidase were found in tumour homogenates, and it was demonstrated that these enzymes contribute to the degradation of high molecular weight hyaluronic acid. The levels of these enzymes were compared with activities found in homogenates of neonatal bone and muscle surrounding tumours. Exoglycosidases, but not hyaluronidase, were found to be produced by cultures of osteosarcoma in vitro.
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PMID:Endo- and exoglycosidases in an experimental rat osteosarcoma. 27 64

1. Incubation of rabbit tracheal explants with N-[(3)H]acetyl-d-glucosamine and N-acetyl-d-[1-(14)C]glucosamine led to labelling of a number of soluble macromolecular products separable from the medium, after papain digestion, by ion-exchange chromatography. 2. With N-acetyl-d-[1-(14)C]glucosamine in the incubation medium, a neutral glycoprotein, two acidic glycoprotein fractions, hyaluronic acid and a glycosaminoglycan fraction were obtained and all were radioactively labelled. Similar labelling occurred with N-fluoroacetyl-d-[1-(14)C]glucosamine or N-fluoro[(3)H]acetylglucosamine as precursor. 3. Maximal labelling was obtained at 96h after incubation of cultures. N-Fluoroacetyl-glucosamine under these conditions was incorporated into hyaluronate less efficiently than N-acetylglucosamine. 4. With N-fluoroacetyl-d-[1-(14)C]glucosamine as precursor, a hyaluronate component was separated that on enzymic degradation by glycosidases (hyaluronidase, beta-glucuronidase and N-acetyl-beta-hexosaminidase) yielded a (14)C-labelled oligosaccharide fraction together with N-acetyl-d-[1-(14)C]glucosamine and N-fluoroacetyl-d-[1-(14)C]glucosamine, consistent with some exchange of N-acetyl groups having occurred. 5. The results on enzymic degradation of labelled macromolecules by glycosidases suggest that the presence of incorporated N-fluoroacetyl side chains may render the hyaluronate analogue more resistant to hyaluronidase.
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PMID:Incorporation of N-fluoroacetyl-D-glucosamine into hyaluronate by rabbit tracheal explants in organ culture. 51 60

The activity of four lysosomal enzymes (hyaluronidase, beta-N-acetylglucosaminidase, acid phosphatase, and cathepsin D) was studied in aqueous extracts of the light mitochondrial fraction of regenerating male rat liver. This tissue was chosen as a model for normal cell division in vivo. In the first wave of division, 40 to 50% of the cells divide synchronously. Activities were measured at 0, 9, 18 (end of G1 phase), 24 (S phase), and 30 hr (mitosis) and during regeneration, 4 and 11 days after partial hepatectomy. Activities were related to fresh tissue weight, to cellular DNA, and to protein content of the extracts. At 9 hr, there was an important increase in hyaluronidase and cathespin D activities (these two enzymes act upon macromolecules); beta-N-acetylglucosaminidase and acid phosphatase activities were only slightly increased. At the end of the G1 phase, 40 to 50% of the activity of all four enzymes was lost, which might indicate complete loss of activity in cells undergoing division. This depletion persisted until mitosis was complete. Four days later, there was a slow restoration of enzyme activities; after 11 days, hyaluronidase and cathepsin D exhibited about 80% of their initial activity, whereas beta-N-acetylglucosaminidase and acid phosphatase only regained about 50%. These results show that the lysosomal system perhaps plays some role in cell division.
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PMID:Lysosomal enzyme activities in the regenerating rat liver. 83 61

The effect of orchidectomy in male rabbits and administration of testosterone to orchidectomized animals on the metabolism of glycosaminoglycans (GAG) has been studied. The response of the different GAG fractions in the aorta varies with the nature of the GAG, and in some cases is different in different segments of the aorta. Orchidectomy produced an increase in hyaluronic acid fraction, decrease in heparin sulphate fraction, and no response in the chondroitin sulphate A fraction in the aortic arch, thoracic aorta, and abdominal aorta. Chondroitin sulphate C and chondroitin sulphate B fractions decreased only in the abdominal aorta and were not significantly altered in the other two segments, while heparin fraction decreased only in the thoracic aorta and was not affected in the other segments. Administration of testosterone to the orchidectomized animals counteracted these changes in the aortic GAG fractures. The enzymes concerned with the synthesis of precursors of GAG--L-glutamine:D-fructose-6-phosphate aminotransferase, UDPG dehydrogenase, and UDPG pyrophosphorylase-- all decreased in the orchidectomized animals; testosterone administration increased their activity in the orchidectomized animals. Enzymes concerned with degradation of GAG--beta-glucuronidase, beta-hexosaminidase, aryl sulphatase, cathepsin, and hyaluronidase--increased in the orchidectomized and decreased on administration of testosterone. Concentration of PAPS and activity of sulphate-activating system and sulphotransferase also decreased in the orchidectomized animals, and testosterone administration tended to restore this decrease to normal levels.
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PMID:Sex hormones and metabolism of glycosaminoglycans. I. Effect of orchidectomy and administration of testosterone in rabbits. 99 37


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