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)

Age-related changes in renal function have been attributed to alterations in the chemical composition of the kidney tissues. Hence, the glycosaminoglycan composition of the renal cortex and medulla at varying age intervals was investigated. Glycosaminoglycans were isolated from the tissues by means of digestion with collagenase and pronase and purified by ethanol precipitation. Subsequent separation of various polyanions was accomplished by ion exchange chromatography on a Dowex 1-X2 column, using sodium chloride buffers of increasing ionic strengths. The glycosaminoglycans in each fraction were identified and quantitated by digestion with specific enzymes, including hyaluronidase, chondroitinase AC and ABC. The enzyme resistant material was separated and further digested with nitrous acid to quantitate the proportion of heparon sulfate. The results indicate that the glycosaminoglycan content of the renal medulla was much higher than the cortex at all the age intervals studied, and age-induced reduction was mainly cortical. There was a significant reduction in the heparan sulfate content of the cortex in aging. Interestingly, the major glycosaminoglycan content of the medulla was hyaluronic acid, which showed a sharp increase during aging, whereas heparan sulfate declined. Chondroitin sulfate was not altered due to age in either tissue. The molecular weight of hyaluronic acid was determined by column chromatography. Results indicate that the size of hyaluronate in the cortex was small and did not vary with age. In the medulla of the younger age group, a considerable amount of large size hyaluronate was observed. As age increased, the size decreased. The results strongly suggest that alteration in the renal glycosaminoglycans may be partly responsible for the age related protinuria and ionic imbalance.
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PMID:Alterations of renal cortex and medullary glycosaminoglycans in aging dog kidney. 662 71

Ruthenium red and toluidine blue O precipitates were described associated with lathyritic elastic fibers in aortas of chickens treated with beta-aminopropionitrile fumarate (I. Pasquali-Ronchetti, C. Fornieri, I. Castellani, G. M. Bressan, and D. Volpin (1981). Alterations of the connective tissue components induced by beta-aminopropionitrile. Exp. Mol. Pathol. 35, 42-56). In this report evidence is given that these precipitates reveal the presence of proteoglycans, as they are completely removed by 5 M guanidine-HCl incubation and by specific enzymatic digestions. In particular, proteoglycans associated with the poorly cross-linked lathyritic elastin can be removed by testicular hyaluronidase, chondroitinase ABC, heparitinase, and nitrous acid treatments, whereas they are rather resistant to streptococcal hyaluronidase and chondroitinase AC. On the contrary, proteoglycans of the matrix or associated with collagen fibers are particularly sensitive to these latter enzymatic treatments. The conclusion is reached that glycosaminoglycans associated with beta-aminopropionitrile-induced lathyritic elastin (i) are different from those of the matrix or associated with collagen, and (ii) include mainly dermatan and heparan sulfates.
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PMID:Elastin fiber-associated glycosaminoglycans in beta-aminopropionitrile-induced lathyrism. 670 93

Chondroitin sulfate lyase (EC 4.2.2.4) was present constitutively at low levels (0.06 to 0.08 U/mg of protein) in cells of Bacteroides thetaiotaomicron which were growing on glucose or other monosaccharides. When these uninduced bacteria were incubated with chondroitin sulfate A (5 mg/ml), chondroitin sulfate lyase specific activity increased more than 10-fold within 90 min. Synthesis of ribonucleic acid and of protein was required for induction, and induction was sensitive to oxygen. The disaccharides which resulted from chondroitinase action did not act as inducers, nor did tetrasaccharides or hexasaccharides obtained by digestion of chondroitin sulfate with bovine testicular hyaluronidase. None of these substances was taken up by uninduced cells; they may not have been able to penetrate the outer membrane. The smallest oligomer capable of acting as an inducer was the outer membrane. The smallest oligomer capable of acting as an inducer was the octassacharide. Oligomers larger than the octassacharide induced chondroitin lyase activity nearly as well as intact chondroitin sulfate.
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PMID:Induction of chondroitin sulfate lyase activity in Bacteroides thetaiotaomicron. 678 77

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

A simple method for the quantitative determination of glycuronic acid-containing glycosaminoglycans (UA-GAG) is described. Sample solutions of glycosaminoglycans were digested with chondroitinase AC, chondroitinase C, chondroitinase B, heparitinases, and Streptomyces hyaluronidase, respectively, and the absorbance was read at 232 nm after digestion. The contents of 4-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-4S), 6-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-6S) plus N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-OS), 4-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)L-idosiduronyl units (D-4S) plus N-acetylgalactosaminyl beta (1 leads to 4)L-idosiduronyl units (D-OS), heparan sulfate, and hyaluronic acid in the sample solutions were calculated from the absorbance with reference to that of the digestion products of known amounts of standard UA-GAG. The analytical data obtained with the mixtures of authentic UA-GAG were in close agreement with the theoretical values. Application of this procedure to the urinary GAG fractions from orthopedic patients gave satisfactory results.
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PMID:A simple method for the quantitation of glycuronic acid-containing glycosaminoglycans with mucopolysaccharidases. 684 97

We aimed to identified cervical ripening at term pregnancy by measuring acid glycosaminoglycans (aGAG) in nonpregnant and immediately postpartum rabbits cervix and body. aGAG was extracted from the uterine tissues by the modified method of K. Anno (1964) and determined by the carbazole method (Bitter, 1962). Components of aGAG were separated by two dimensional electrophoresis (0.1M pyridine-0.47M formic acid in the first and 0.1M calcium acetate buffer in the second) using acetate cellulose strips. aGAG were separated five spots that were identified hyaluronic acid, heparan sulfate, chondroitin sulfate A, dermatan sulfate and chondroitin sulfate C. These results were confirmed by method of hyaluronidase, chondroitinase AC and ABC digestion test.
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PMID:[Studies on acid glycosaminoglycans in rabbit uterine cervix and body (author's transl)]. 706 98

The uronic acid residues of all known glycosaminoglycuronans reacted with 5-aminofluorescein to yield fluorescent glycosaminoglycuronan derivatives, which showed fluorescence characteristics identical to those of fluorescein or 5-acetamidofluorescein. The fluorescent products could be purified by chromatography on Octyl-Sepharose; three preparations of labeled chondroitin 6-sulfate having different degrees of substitution, and a labeled heparin were obtained. Fluorescent hyaluronic acid containing labeled and unlabeled molecules was digested with testicular hyaluronidase to give fluorescent oligosaccharides. Fluorescent chondroitin 6-sulfate was treated with chondroitinase AC to give a nonfluorescent disaccharide and minor proportion of fluorescent octasaccharide. Fluorescent heparin retained its anticoagulant activity, which was similar to that of the starting heparin; its half-life in circulating rabbit blood was 36 min (by fluorometry) and 45 min (by clotting-time assay).
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PMID:Preparation and properties of fluorescent glycosaminoglycuronans labeled with 5-aminofluorescein. 711 57

During the course of a study of elucidate the role of modification of the common polysaccharide-protein linkage structure, GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, in biosynthetic sorting mechanisms of the different sulfated glycosaminoglycan chains, a novel N-acetylgalactosamine (GalNAc) transferase was discovered in fetal bovine serum. The enzyme catalyzed the transfer of [3H]GalNAc from UDP-[3H]GalNAc to linkage tetrasaccharide and hexasaccharide serines synthesized chemically and to various regular oligosaccharides containing terminal D-glucuronic acid (GlcA), which were prepared from chondroitin and chondroitin sulfate using testicular hyaluronidase digestion. The labeled products obtained with the linkage tetra- and hexasaccharide serines and with the tetrasaccharide (GlcA beta 1-3GalNAc)2 were resistant to digestion with chondroitinase AC-II and beta-N-acetylhexosaminidase but sensitive to alpha-N-acetylgalactosaminidase digestion, indicating that the enzyme is an alpha-N-acetylgalactosaminyltransferase. This finding is in contrast to that of Rohrmann et al. (Rohrmann, K., Niemann, R., and Buddecke, E. (1985) Eur. J. Biochem., 148, 463-469), who reported that a corresponding product was susceptible to digestion with beta-N-acetylhexosaminidase. The presence of a sulfate group at C4 of the penultimate GalNAc or Gal units markedly inhibited the transfer of GalNAc to the terminal GlcA, while a sulfate group at C6 of the GalNAc had little effect on the transfer. Moreover, a slight but significant transfer of [3H]GalNAc was observed to an oligosaccharide containing terminal 2-O-sulfated GlcA as acceptor, whereas no incorporation was detected into oligosaccharides containing terminal unsaturated or 3-O-sulfated GlcA units. These results suggest that this novel serum enzyme is a UDP-GalNAc:chondro-oligosaccharide alpha 1-3- or 1-4-N-acetylgalactosaminyltransferase. The possibility of involvement of this enzyme in glycosaminoglycan biosynthesis is discussed.
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PMID:N-acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans. Identification of UDP-GalNAc:chondro-oligosaccharide alpha-N-acetylgalactosaminyltransferase in fetal bovine serum. 767 97

Acidic glycoconjugates (glycosaminoglycans, sulfated glycopeptide, and sialoglycopeptide) were isolated by precipitation with cetylpyridinium chloride from human pancreatic juice after digestion with pronase. The acidic glycoconjugates were found exclusively in the proteinaceous precipitate that occurred during dialysis against a buffer of low ionic strength. The concentration of the acidic glycoconjugates in normal pancreatic juice was about 2.4 mg/L. The acidic glycoconjugates were characterized by electrophoresis on cellulose acetate membrane and chemical analysis before and after digestion with Streptomyces hyaluronidase, chondroitinase AC, chondroitinase ABC, and heparitinase. It was found that the major acidic glycoconjugates were heparan sulfate (39.3%), sulfated glycopeptide (34.4%), chondroitin sulfate (14.2%), and the minor ones hyaluronic acid (6.4%) and sialoglycopeptide (5.7%).
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PMID:Enzymic determination of acidic glycoconjugates in human pancreatic juice. 811 24

The development of iridocorneal angle and trabecular tissue was investigated histochemically and electron microscopically. Sixty-three human eyes at from 5 to 22 weeks of gestation were used in this study. For identifying glycosaminoglycans, alcian blue staining and enzyme digestion methods with hyaluronidase and chondroitinase AC and ABC were carried out light microscopically. Electron microscopically, specimens were stained with ruthenium red. In the early stage from 8 to 10 weeks, mesenchymal cells between the primordium of the cornea and the iris became elongated and connected with one another. Desmosome-like junctional complexes were observed in these cells. Schlemm's canal and para-canalicular tissue were observed at 20 weeks and the structure of the meshwork became similar that of adults. From findings of enzyme digestion methods, glycosaminoglycans in trabecular tissue seemed to be mainly hyaluronic acid in the early stage, which was replaced by chondroitin sulfate and dermatan sulfate afterwards. Substances positive for ruthenium red, which seemed to be glycosaminoglycans, was observed in intercellular spaces electron microscopically. They decreased according to development. These findings indicated that the beginning of aqueous outflow might be related to the decrease of glycosaminoglycans in trabecular tissue.
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PMID:[Histochemical and electron microscopic study of the formation of trabecular meshwork and changes of glycosaminoglycans]. 831 47


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