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)

Cartilaginous and/or osseous foci were observed in eight aortas from 20 rabbits immunized against heterologous aorta homogenates and sacrificed 11 to 24 months later. They were studied by means of histological and histochemical methods and compared with normal aortas, cartilage and bone. Some of the observed changes seemed to be true markers of these transformations. Chondroid metaplasia was characterized by 1) generalized increase in alcianophilic hyaluronidase sensitive substances. 2) Appearance of Dermatan and/or Keratan sulfates round some isolated cells. 3) Advent of G6 Pase and Alk. Phase activities in cells adjacent to osseous foci. Osteous metaplasia was characterized by 1) decrease, then disappearance of alcianophilic and PAS positive material, 2) increase in osteoblastic alkaline Pase-activities.
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PMID:Cartilage and bone formation in arterial wall. 1. Morphological and histochemical aspects. 12 Dec 37

Glycosaminoglycan-protein complexes were extracted from bovine duodenal mucosa with distilled water, resulting in solubilization of a fraction of the total proteoglycan of the tissue. The extracted material was purified by anion exchange chromatography on DEAE-Sephadex A-25, and then characterized by chemical analysis and by fractionation on Dowex 1. By using these procedures, two major fractions were identified, which were eluted from Dowex with 1.0-1.25 M NaC1 and with 1.5-1.75 M NaC1 respectively. Analyses showed that both fractions were mainly composed of glucosamine-containing, hyaluronidase-resistant polysaccharides, which were identified by their N-sulphate: D-glucosamine and total sulphate: D-glucosamine ratios as heparan-sulphate in the less acidic fraction, and as heparin in the more acidic fraction. Dermatan sulphate molecules were also present in both preparations, with an approximate ratio 1:3 to the glucosamine-containing polysaccharides. Solubility behaviour of the complexes formed by the isolated polyanionic molecules with cetylpyridinium chloride was strongly modified by papain digestion of the duodenal material. This reduction of molecular size of papain treatment suggests that the molecules extracted with water from duodenal mucosa are complex proteoglycans, perhaps in the native state.
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PMID:Water soluble proteoglycans from bovine duodenal mucosa. 88 4

Dermatan sulphate was degraded by testicular hyaluronidase and an oversulphated fraction was isolated by ion-exchange chromatography. This preparation, which contained fairly long segments derived from the non-reducing terminal portion of the molecule, was subjected to periodate oxidation under acidic conditions. The oxidized iduronic acid residues were cleaved by reduction-hydrolysis (Smith-degradation) (Fransson & Carlstedt, 1974) or by alkaline elimination. The oligosaccharides so obtained contained both GlcUA (glucuronic acid) and IdUA-SO(4) (sulphated iduronic acid) residues. Copolymeric oligosaccharides obtained after alkaline elimination were cleaved by chondroitinase-AC into disaccharide and higher oligosaccharides. Since the corresponding oligosaccharides obtained by Smith-degradation were unaffected by this enzyme, it was concluded that the carbohydrate sequences were GalNAc-(IdUA-GalNAc)(n)-GlcUA-GalNAc. The iduronic acid-containing sequences were resistant to digestion with chondroitinase-ABC. It was demonstrated that the presence of unsulphated N-acetylgalactosamine residues in these sequences could be responsible for the observed effect. This information was obtained in an indirect way. Chemically desulphated dermatan sulphate was found to be a poor substrate for the chondroitinase-ABC enzyme. Moreover, digestion with chondroitinase-ABC of chondroitinase-AC-degraded dermatan sulphate released periodate-resistant iduronic acid-containing oligosaccharides. It is concluded that copolymeric sequences of the following structure are present in pig skin dermatan sulphate: [Formula: see text] N-acetylgalactosamine moieties surrounding IdUA-SO(4) residues are unsulphated to a large extent.
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PMID:The copolymeric structure of pig skin dermatan sulphate. Isolation and characterization of L-idurono-sulphate-containing oligosaccharides from copolymeric chains. 437 44

Dermatan sulfate-chondroitin sulfate copolymers with a high content of dermatan sulfate are stored in cultured human skin fibroblasts from patients affected with mucopolysaccharidosis VI (Maroteaux-Lamy disease). Characterization of the storage material provided evidence that hyaluronidase-like enzymes are not present in these fibroblasts. This is based on the following observations: (i) dermatan sulfate chains stored intracellularly show no reduction of molecular size as compared with intact chains isolated from the extra-cellular space; (ii) the stored dermatan sulfate chains lack reducible end groups generated by endoglycosidases; (iii) homogenates of human skin fibroblasts do not degrade hyaluronate and (iv) the stored dermatan sulfate chains are degraded by testes hyaluronidase.
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PMID:Characterization of dermatan sulfate in mucopolysaccharidosis VI. Evidence for the absence of hyaluronidase-like enzymes in human skin fibroblasts. 677 Sep 9

Crude glycosaminoglycans were prepared from acetone powder of diabetic, toxemic, and normal term placentas. Glycosaminoglycan composition was determined by electrophoresis and densitometric scanning with and without treatment with testicular hyaluronidase and chondroitinase ABC. The identity of individual glycosaminoglycans was confirmed by the nature of their hexosamine. Glycosaminoglycan content was found to be significantly increased in diabetic placentas and increased to a lesser degree in the toxemic placentas. The amount of hyaluronic acid was elevated in both abnormal tissues, and heparan sulfate was slightly higher in diabetes, while unchanged in toxemia. Dermatan sulfate was markedly reduced in the abnormal placentas while chondroitin 4/6 sulfate was unaltered. An attempt was made to correlate the histopathologic changes reported to occur in these conditions with the alterations in the glycosaminoglycans patterns of placentas.
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PMID:Glycosaminoglycan patterns in diabetic and toxemic term placentas. 677 11

The acidic glycosaminoglycans (AGAG) of the human coronary arterial tree (the main left and right branches and their distal portions) were analyzed by enzymatic methods employing chondroitinases, hyaluronidase and heparitinase. The AGAG content of human coronary arteries was highest in the left branch, intermediate in the right branch and lowest in the distal portions. Some compositional differences in AGAG were found in these three parts. The amount of AGAG in the coronary arterial tree decreased with increasing severity of atherosclerosis. The main AGAG were heparan sulfate (HS) and chondroitin 6-sulfate (C-6S), constituting 33-38% and 24-36% of the total AGAG, respectively. Dermatan sulfate (DS) and chondroitin 4-sulfate (C-4S) each comprised 1/5-1/10 of the total AGAG. Hyaluronic acid (HA) and oversulfated DS comprised smaller proportions of the total AGAG. A small amount of heparin was occasionally detected in the coronary arterial tree, particularly in the distal portions. The lipid content of the main branches was increased in mildly atherosclerotic parts but diminished in severely affected parts. The water content was relatively higher in the main branches and decreased with severity of atherosclerosis. A possible function of these AGAG in atherosclerosis is discussed with respect to the compositional changes.
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PMID:Acidic glycosaminoglycan, lipid and water contents in human coronary arterial branches. 715 90

Non-pregnant and pregnant rats of known gestational age were killed at intervals and their uterine cervices were excised and digested with papain. Glycosaminoglycans thus extracted were separated by cellulose acetate electrophoresis and stained with Alcian Blue. Glycosaminoglycans were identified by comparison with standards and by serial degradation with chondroitin ABC lyase, butyl nitrite and leech hyaluronidase. Dermatan sulphate, hyaluronic acid and heparan sulphate were identified and quantitative determined by densitometry. The overall concentration of glycosaminoglycans changed little during pregnancy. A 3-fold total increase in uronic acid paralleled the increase in cervical weight. Hyaluronate content, however, increased 17-fold, and rose from 6% of total glycosaminoglycans in the non-pregnant state to 33% at term. Furthermore, the ratio of hyaluronate to hydroxyproline increased 10-fold. These changes are consistent with an accumulation of hyaluronate in the interstices between collagen fibres, resulting in the softening of this tissue that is seen in late pregnancy.
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PMID:Pregnancy-related changes in rat cervical glycosaminoglycans. 730 89

Dermatan sulfate (DS) widespread as a component of extracellular matrix proteoglycans, is characterized by great bio-reactivity and remarkable structural heterogeneity due to distinct degrees of sulfation and glucuronosyl epimerization and different polymerization degrees. However, DS metabolism under various biological conditions is poorly known. Dupuytren's contracture is a benign fibromatosis leading to complex remodeling of the palmar fascia structure and properties. However, it remains unclear whether the disease affects the structure of DS, which is the major tissue glycosaminoglycan. Thus the aim of the study was to examine the structure of the total DS in Dupuytren's fascia. DS chains were extracted from 5 samples of normal fascia and 7 specimens of Dupuytren's tissue by papain digestion followed by fractionation with cetylpyridinium chloride. Then, DS structure analysis was performed comprising the evaluation of its molecular masses and sensitivity to hyaluronidase and chondroitinase B. Dupuytren's contracture is associated with significant remodeling of DS chain structure revealed by (1) a distinct profile of chain molecular masses characterized by the appearance of long size components as well as the increase in the content of small size chains; (2) a different glucuronosyl epimerization pattern connected with the enhanced content of glucuronate disaccharide blocks; (3) chain oversulfation. These structural alterations in total DS may modify the GAG interactions especially affecting collagen fibrillogenesis and growth factor availability. Thus, Dupuytren's contracture associated DS remodeling may promote the phenomena typical for advanced disease: apoptosis and reduction in cell number as well as the appearance of dense pseudotendinous collagen matrix.
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PMID:Dermatan sulfate remodeling associated with advanced Dupuytren's contracture. 1806 4

Dermatan sulfate oligosaccharides having reducing end 2,5-anhydro-d-talose were prepared by partial N-deacetylation of dermatan sulfate polysaccharide with hydrazine followed by deamination with nitrous acid, and the effect of these oligosaccharides on the activity of bovine testicular hyaluronidase was investigated. Hydrolysis activity and transglycosylation activity of this enzyme were assessed in an independent reaction system by analyzing the products by HPLC. Dermatan sulfate oligosaccharides inhibited hyaluronan hydrolysis by bovine testicular hyaluronidase. Kinetic analysis of the hydrolysis reaction revealed that the inhibition mode by dermatan sulfate oligosaccharides was as competitive as that previously shown by chondroitin sulfate oligosaccharides. Transglycosylation of hyaluronan by bovine testicular hyaluronidase, as a reverse reaction of hydrolysis of hyaluronan, was also inhibited. These inhibitory effects were dependent on the dose and sulfation degree of dermatan sulfate.
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PMID:Dermatan sulfate oligosaccharides having reducing end 2, 5-anhydro-d-talose inhibit bovine testicular hyaluronidase activity. 3139 13