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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)
35S- as well as 3H-labeled glycosaminoglycans (GAG) produced by cultivated epithelium and fibroblasts of the rabbit cornea were treated with testicular
hyaluronidase
, leech
hyaluronidase
and chondroitinase-ABC or -AC. The fractionation-patterns of enzyme-treated GAG were compared with blanks not exposed to enzymes. The epithelial GAG revealed to be generally more resistant to the enzymatic degradation than the GAG synthesized by the fibroblasts, but--depending on the enzyme--in the GAG of both cell types the same fractions were attacked. The decline of the radioactivity in the fractions of enzyme-treated GAG allows the conclusions that both cell types produce relatively small amount of keratan sulfate but mainly chondroitin sulfates with a different degree of sulfation. In addition GAG, not present in the normal cornea, are synthesized: hyaluronic acid chiefly by fibroblasts and probably dermatan sulfate. The possible role of the fibroblastic and epithelial GAG in corneal wound repair is discussed.
...
PMID:Biosynthesis of glycosaminoglycans by mammalian corneal epithelium and fibroblasts in vitro. II. Approach to specify the GAG from the two cell types. 12 25
The acidic glycosaminoglycans (AGAG) in normal human kidneys were fractionated on Dowex 1-X2 columns and analysed by electrophoretic separation in three buffers on cellulose acetate membranes and gel filtration on Sephadex G-100 columns, before and after digestion with chondroitinases and streptomyces
hyaluronidase
. Thin-layer chromatography was also performed to separate glucosamine from galactosamine moieties. Enzymatic digestion combined with electrophoretic characterization indicated that heparan sulfates exist as the main AGAG which accounted for two-fifths of the total AGAG. Hyaluronic acid and dermatan sulfates accounted for one-fourth and one-sixth of the total kidney AGAG, respectively. Chondroitin sulfate isomers (4-sulfate and 6-sulfate) consisted of the residual one-sixth of the total AGAG. An oversulfated chondroitin sulfate was detected in a small amount by demonstration of the unsaturated disulfated disaccharide after digestion with chondroitinase-ABC but not with chondroitinase-AC.
...
PMID:Acidic glycosaminoglycans in human kidney tissue. 12 23
Chondroitin sulfate fractions were isolated from different animal cartilages, including whale, cattle, sheep, ray and shark, by Dowex 1 chromatography followed by ethanol fractionation. Although each preparation showed a single spot when electrophoresed on cellulose acetate, both 4- and 6-sulfated disaccharides were present in chondroitinase digests of each. In particular, the main fraction of bovine tracheal chondroitin sulfate (SO4/Ga1N = 1) gave both the disaccharides in nearly equal amounts, and its IR spectrum showed absorption bands at 820 and 850 cm-1. This fraction yielded three types of tetrasaccharides after digestion with testicular
hyaluronidase
. Structural studies on these tetrasaccharides, using P. vulgaris chondro-4-sulfatase followed by chondroitinase, showed that one of them is a hybrid consisting of the 4- and 6-sulfated residues. In the light of these facts, a nomenclature for chondroitin sulfates is discussed.
...
PMID:Microheterogeneity of chondroitin sulfates from various cartilages. 12 31
Periodontal ligaments from unerupted, partially erupted and mature teeth were extracted with 0.15 M NaCl. The major reducible collagen cross-link in each insoluble fraction was dehydrodihydroxylysinonorleucine; the dehydroydroxylysinonorleucine contents were smaller. There was no significant difference in the quantities of these cross-links relative to collagen contents in the three speciments, but one of the precursors, hydroxyallysine, markedly decreased in the older tissue. The amino acid compositions of the trypsin-resistant insoluble fractions were generally characteristic of collagen. Analyses of separated glycopeptides revealed the presence of insoluble non-collagenous glycoproteins and collagen hexoses. The latter were lower in the mature ligament. Hyaluronic acid progressively decreased relative to chondroitin sulphate on eruption and maturation. A
hyaluronidase
-resistant glycosaminoglycan, probably dermatan sulphate, occurred in the NaCl-insoluble fraction of the mature ligament and in appreciable amounts in all NaCl extracts.
...
PMID:Bovine periodontal ligament. An invesitation of the collagen, glycosaminoglycan and insoluble glycoprotein components at different stages of tissue development. 12 33
Uterine slices obtained from the estrogen-treated rabbits were digested with pronase. Glycosaminoglycans and acidic glycopeptides were then isolated by Dowex 1 column chromatography and preparative electrophoresis on cellulose acetate membrane (Separax), in succession. Each subfraction thus obtained was identified by the mobility on Separax electrophoresis and the digestibility with mucopolysaccharidases (Streptomyces
hyaluronidase
, testicular
hyaluronidase
, chondroitinase AC, chondroitinase ABC and heparinase). The resulting data showed that each complex saccharide (hyaluronic acid, heparan sulfate, chondroitin sulfate A, chondroitin sulfate C, dermatan sulfate, sulfated glycopeptide and sialoglycopeptide) was separated into 2-5 fractions, indicating charge and/or molecular heterogeneity of each complex saccharide.
...
PMID:Glycosaminoglycans and acidic glycoproteins in rabbit uterus under estrogenic conditions. 12
Development of the human hand plate (stages 16-17) has been analyzed with emphasis on differentiation of elements within the extracellular matrix and the composition of the mesenchymal cell surface. The epithelial-mesenchymal interface contains a basal lamina and a sublaminar matrix exhibiting: (a) collagen fibrils with characteristic 63-64 nm banding: (b) non-banded filaments, 10-15 nm in diameter; (c) ruthenium red-positive particles, 12-15 nm in diameter; and (d) attenuated threads, 3-5-5-0 nm in diameter which inter-connect particles, fibrils, filaments and the basal lamina. Processes of mesenchymal cells penetrate this matrix network. In addition to staining with ruthenium red, components of basal laminae bind to ferritin-conjugated Concanavalin A, greatest binding being localized on the mesenchymal surface of the lamina. Asymmetry of binding is removed by incubation of exposed laminae with trypsin (5 mug/ml). Regional differences in these staining and binding characteristics within the subepithelial matrix have not been observed in the hand plate. However, precartilaginous extracellular zones deep within the plate are notably unstructured in comparison to the sublaminar region. Ruthenium red-positive materials at mesenchymal cell surfaces display sensitivity to testicular
hyaluronidase
, Pronase and trypsin but resist removal with neuraminidase and EDTA. These features of the substrate in situ may be important in the regulation of mesenchymal cell behavior during limb morphogenesis in man.
...
PMID:Ultrastructural identification of extracellular matrix and cell surface components during limb morphogenesis in man. 12 16
Some hitherto undetected differences in chemical and macromolecular structure between both dermatan sulphates and heparan sulphates excreted in the Hurler and Hunter syndromes are demonstrated. 1. Of Hunter dermatan sulphate, 37-43% is resistant to periodate oxidation, as opposed to 25% of the corresponding Hurler material. It is likely that the resistance is conferred by the presence of sulphate groups on carbon atoms 2 or 3 of the iduronate residues, correlating with the recently established deficiency of a sulphoiduronate sulphatase in Hunter fibroblasts. 2. Two distinct electrophoretic species of dermatan sulphate are found in Hunter urine, but only one in Hurler preparations. 3. Ion-exchange chromatography and gel filtration reveal that Hurler dermatan sulphate is more heterogeneous with respect to molecular weight distribution than the other. The dermatan sulphates were degraded by
hyaluronidase
to a limited extent. 4. Hurler heparan sulphate contains a higher proportion of sulphoamino-glucose than material from Hunter urine. Similar high levels in Sanfilippo patients, representing 65-78% of the total glucosamine suggest a direct correlation with mental deficiency.
...
PMID:Comparative structural studies of urinary glycosaminoglycans in the Hurler and Hunter syndromes. 12 16
7 clinically uninvolved as well as 8 involved (6 moderately, 2 markedly) back or forearm skin specimens from 12 patients with systemic scleroderma were subjected to quantitative evaluation and to qualitative analysis of glycosaminoglycans (GAG) by one-dimensional and two-dimensional cellulose acetate electrophoresis. Skin specimens from the back, clinically uninvolved but histologically demonstrating the initial change, revealed increased amounts of
hyaluronidase
, chondroitinase-resistant GAG of varying electrophoretic mobilities, and one of them was chemically confirmed to be heparan sulfate variant, whereas involved skin specimens showed hardly this increase.
...
PMID:Initial change of glycosaminoglycans in systemic scleroderma. 12 27
Proteoglycans extracted with 4M-guanidinium chloride from pig laryngeal cartilage and bovine nasal septum were purified by density-gradient centrifugation in CsCl under 'associative' followed by 'dissociative' conditions [Hascall & Sajdera (1969) J. Biol. Chem. 244, 2384-2396]. Proteoglycans were then digested exhaustively with testicular
hyaluronidase
, which removed about 80% of the chondroitin sulphate. The
hyaluronidase
was purified until no proteolytic activity was detectable under the conditions used for digestion. The resulting 'core' proteins of both species were fractionated by a sequence of gel-chromatographic procedures which gave four major fractions of decreasing hydrodynamic size. Those that on electrophoresis penetrated 5.6% (w/v) polyacrylamide gels migrated as discrete bands whose mobility increased with decreasing hydrodynamic size. The unfractionated 'core' proteins had the same N-terminal amino acids as the intact proteoglycan, suggesting that no peptide bonds had been cleaved during
hyaluronidase
digestion. Alanine predominated as the N-terminal residue in all the fractions of both species. Fractions were analysed for amino acid, amino sugar, uronic acid and neutral sugar compositions. In pig 'core' proteins, the glutamic acid content increased significantly with hydrodynamic size, but in bovine 'core' proteins this trend was less marked. Significant differences in amino acid composition between fractions suggested that in each species there was more than one variety of proteoglycan. The molar proportions of xylose to serine destroyed on alkaline beta-elimination were equivalent in most fractions, indicating that the serine residues destroyed were attached to the terminal xylose of chondroitin sulphate chains. The ratio of serine residues to threonine residues destroyed on beta-elimination, was similar in all fractions of both species. Since the fractions of smallest hydrodynamic size contained less keratan sulphate than those of larger size, it implies that in the former the keratan sulphate chains were shorter than in the latter.
...
PMID:The nature of the protein moieties of cartilage proteoglycans of pig and ox. 12 55
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.
...
PMID:Ascorbic acid and glycosaminoglycan and lipid metabolism in guinea pigs fed normal and atherogenic diets. 12 67
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