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)

A high-performance liquid chromatography method for analyzing disaccharides derived from chondroitin sulfate glycosaminoglycans has been developed which employs a Whatman Partisil-10 PAC amino-cyano column and an acetonitrile/methanol/ammonium acetate solvent to resolve disulfated, monosulfated, and unsulfated disaccharides in a chromatographic run of less than 20 min. The single known trisulfated chrondroitin disaccharide can be eluted in an alternate solvent system containing the same mobile phase components in different proportions. Disaccharides were prepared for chromatography from glycosaminoglycans and proteoglycans of known compositions by digestion with chondroitinase ABC, with the exception of king crab cartilage glycosaminoglycan which was incubated sequentially with hyaluronidase and chondroitinase ABC. Disaccharides were extracted from the digestion mixtures in 80% ethanol, dried over nitrogen, resuspended in the HPLC solvent, and chromatographed at a flow rate of 1 ml/min. Unsaturated disaccharides in the column eluate were detected by continuous ultraviolet absorbance monitoring at 232 nm; alternatively, fractions were collected and assayed for uronic acid content or radioactivity. By utilizing the HPLC technique in conjunction with chondroitinase ABC and AC digestion and sulfatase hydrolysis, the epimeric structures of chondroitin sulfates E and H were confirmed. With this technique, rapid and reproducible analyses of chondroitin sulfate disaccharides generated from mouse mast cell proteoglycan and from glycosaminoglycans of squid cranial cartilage, shark skin, hagfish skin, and hagfish notocord were in close agreement with compositions obtained by other techniques.
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PMID:Analysis of polysulfated chondroitin disaccharides by high-performance liquid chromatography. 643 72

Wistar rats aged 7 or 22 months resp. were treated with 50 mg/kg of thioacetamide (TAA) i.p. The TAA-treated animals as well as control groups of the same ages and containing the same number of animals were injected i.p. with 3H-glucosamine (0.2 microCi/g body weight) 2 hours before sacrifice. Previously to sacrifice, the livers had been perfused in narcosis with NaCl (0.9%). Following degradation of the tissue by pronase, specimen of the substances precipitable by ethanol were digested with chondroitinases, streptomyces-hyaluronidase, keratanase, and nitrite. The quantities of substances were estimated photometrically using Alcian blue; radiometry was performed following precipitation with cetylpyridiniumchloride. In aging animals the amount of dermatan-sulphate (DS) and of the total acidic glycosaminoglycans (a.GAG) is increased as compared to the younger animals, although there ist no age related difference in the incorporation of glucosamine. The incorporation per microgram a.GAG (spec. act.) is decreased. Following TAA the amount of DS is increased in both age groups, whereas the total amount of GAG is increased only in the younger animals. The incorporation per mg dry weight is also increased in all GAG types of both age groups which is also the case with the spec. act. (with the exception of HS in the younger animals). The increase of the incorporation per mg dry weight in DS is significantly lower in the older TAA-animals as compared to the younger ones. HS shows the same tendency, but there is no significance. The age related increase of hydroxyproline parallels that of DS.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Age dependence of the early reaction in glycosaminoglycan metabolism of the rat liver on damage following a single dose of thioacetamide]. 647 92

The effect of streptozotocin-induced diabetes on the glycosaminoglycan composition of rat renal cortical tissue was evaluated. Glycosaminoglycans were isolated and purified from the kidney cortex of control and diabetic rats by means of digestion with collagenase, pronase and ethanol precipitation. Subsequent fractionation was performed by ion exchange chromatography on Dowex 1-X2 Cl using various concentrations of sodium chloride solution. The glycosaminoglycan in each fraction was characterized by digestion with hyaluronidase, chondroitinase AC and ABC. The undigested glycosaminoglycans were separated after each enzyme digestion and quantitated. The glycosaminoglycan composition of each fraction was computed from the enzyme digestion profile. The results indicate that in renal cortex of streptozotocin induced diabetic rats there was a significant reduction in the levels of dermatan sulfate, heparan sulfate and hyaluronic acid, while the chondroitin sulfate remained unaffected. In light of this finding, the significance of these anionic polysaccharides in renal functions is discussed.
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PMID:Alterations in the rat renal glycosaminoglycans in streptozotocin-induced diabetes. 660 Sep 34

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

An acidic glycoconjugate containing mannose, galactose and phosphate in approximately equimolar amounts was extracted from Leishmania donovani promastigotes and partially characterized. The glycoconjugate could be metabolically labeled with either [3H]mannose or [3H]galactose and was extractable from a delipidated residue fraction with water/ethanol/diethyl ether/pyridine/concentrated NH4OH (15:15:5:1:0.017) at 25 degrees C. The radioactively labeled glycoconjugate was found to possess the following characteristics: 1) comprised 45-60% of the total [3H]mannose label incorporated into macromolecules; 2) was soluble in alkaline solvents and 0.5% Triton X-100; 3) migrated as a broad band upon electrophoresis on sodium dodecyl sulfate-polyacrylamide gels with an approximate molecular weight of 15,000-30,000; 4) bound to DE52 cellulose and was eluted with a salt gradient of 0-0.1 M NaCl; 5) was insensitive to Pronase, hyaluronidase, chondroitinase, endo-beta-N-acetylglucosaminidase H, and endo-beta-galactosidase; and 6) possessed hydrophobic properties. An unusual feature of the glycoconjugate was its lability to mild acid hydrolysis (0.02 N HCl, 15 min, 60 degrees C). As determined by alkaline phosphatase and glycosidase digestion and paper chromatographic analysis, the major fragment generated by mild acid hydrolysis was found to be a phosphorylated galactosyl-beta-mannose disaccharide. All of these characteristics suggest that the glycoconjugate may be a polysaccharide and, possibly, may be important in parasite-host cell interactions.
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PMID:Expression of an unusual acidic glycoconjugate in Leishmania donovani. 670 85

The presence of glycosaminoglycans (GAG) has been histochemically demonstrated in the CNS of various mammalian species. They have been related with some nerve functions as neurotransmitters storage and synaptic transmission. In the present paper, the histochemical properties of nerve cell cytoplasmic GAG were studied in several regions of adult human CNS. Samples of brain cortex, pons, upper medulla, and cerebellar cortex obtained by autopsy from subjects not dying after neurological diseases were fixed by immersion in glutaraldehyde, dehydrated with ethanol, and embedded in paraffin. The sections were stained with Alcian blue solutions adjusted to pH 2.5, 4.0, and 5.7. To the latter solution MgCl2 was added in increasing concentration from 0.05 to 1.2 M. Testicular hyaluronidase, neuraminidase, and ribonuclease were applied on simultaneous sections with their respective controls. The sequence of these reactions allowed us to demonstrate the presence of hyaluronic acid along chondroitin-4- and/or 6-sulphate in the cytoplasm of most nerve cells. The sulphated GAG showed certain variability in the various regions studied related specially with their grade of sulphation.
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PMID:Histochemical demonstration of cytoplasmic glycosaminoglycans in the macroneurons of the human central nervous system. 670 30

Using monoclonal antibodies to H-2Kk antigen, we sought to develop a reproduceable method of in situ localization in embryonic tissue and to determine whether there are specific patterns of H-2 localization in time and space in the developing palatal tissues of B10.A(H-2a) embryonic mice, with and without corticosteroid pretreatment at 12 days gestation. Our procedure employs ethanol-glacial acetic acid fixation, paraplast embedding, and enzymatic predigestion with purified hyaluronidase and neuraminidase. H-2 antigens were detected in palatal mesenchyme as well as basement membranes but not in oral or nasal epithelium. The pattern of distribution in mesenchyme of untreated embryos changed with progressive shelf development vertical leads to horizontal leads to epithelial fusion leads to epithelial seam degeneration leads to mesenchymal confluence. Although the palatal shelves of treated embryos remained vertical, corticosteroid treatment does not appear to alter the detectable spatiotemporal distribution of H-2 antigens in developing palates of embryonic B10.A mice.
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PMID:Localization of H-2Kk in developing mouse palates using monoclonal antibody. 675 48

Using cultured cells from bovine and rat aortas, we have examined the possibility that endothelial cells might regulate the growth of vascular smooth muscle cells. Conditioned medium from confluent bovine aortic endothelial cells inhibited the proliferation of growth-arrested smooth muscle cells. Conditioned medium from exponential endothelial cells, and from exponential or confluent smooth muscle cells and fibroblasts, did not inhibit smooth muscle cell growth. Conditioned medium from confluent endothelial cells did not inhibit the growth of endothelial cells or fibroblasts. In addition to the apparent specificity of both the producer and target cell, the inhibitory activity was heat stable and not affected by proteases. It was sensitive flavobacterium heparinase but not to hyaluronidase or chondroitin sulfate ABC lyase. It thus appears to be a heparinlike substance. Two other lines of evidence support this conclusion. First, a crude isolate of glycosaminoglycans (TCA-soluble, ethanol-precipitable material) from endothelial cell-conditioned medium reconstituted in 20 percent serum inhibited smooth muscle cell growth; glycosaminoglycans isolated from unconditioned medium (i.e., 0.4 percent serum) had no effect on smooth muscle cell growth. No inhibition was seen if the glycosaminoglycan preparation was treated with heparinase. Second, exogenous heparin, heparin sulfate, chondroitin sulfate B (dermatan sulfate), chondroitin sulfate ABC, and hyaluronic acid were added to 20 percent serum and tested for their ability to inhibit smooth muscle cell growth. Heparin inhibited growth at concentrations as low as 10 ng/ml. Other glycosaminoglycans had no effect at doses up to 10 mug/ml. Anticoagulant and non- anticoagulant heparin were equally effective at inhibiting smooth muscle cell growth, as they were in vivo following endothelial injury (Clowes and Karnovsk. Nature (Lond.). 265:625-626, 1977; Guyton et al. Circ. Res. 46:625-634, 1980), and in vitro following exposure of smooth muscle cells to platelet extract (Hoover et al. Circ. Res. 47:578-583, 1980). We suggest that vascular endothelial cells may secrete a heparinlike substance in vivo which may regulate the growth of underlying smooth muscle cells.
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PMID:Cultured endothelial cells produce a heparinlike inhibitor of smooth muscle cell growth. 728 12

The biosynthesis of glycosaminoglycans (GAG) by cultivated rat glomerular epithelial and mesangial cells was studied by incorporation of [35S]sulfate or [14C]glucosamine for 48 h. After dialysis, the incubation medium was subjected to digestion with papain. Labeled GAG were isolated from the digests by precipitation with cetylpyridinium chloride and ethanol. Results of cellulose acetate electrophoresis of the isolated 'epithelial' GAG fraction revealed the presence of two [14C] spots and one [35S] spot. The [35S] spot was identified as heparan sulfate, because it comigrated with the heparan sulfate standard and it was insensitive to testicular hyaluronidase. One [14C] spot comigrated with the [35S] spot and with the heparan sulfate standard. This GAG fraction did not contain galactosamine. The second [14C] spot was identified as hyaluronic acid, since it comigrated with the hyaluronic acid standard and since it was sensitive to testicular hyaluronidase. Results of cellulose acetate electrophoresis of the isolated 'mesangial' GAG fraction revealed the presence of one [14C] spot only. No [35S] spot was detectable. The [14C] spot comigrated with the hyaluronic acid standard and was sensitive to hyaluronidase. The data therefore suggest that the glomerular epithelial cells synthesize and secret both sulfated GAG (heparan sulfate) and nonsulfated GAG (hyaluronic acid) into the culture medium, whereas the glomerular mesangial cells synthesize and secrete nonsulfated GAG (hyaluronic acid) only into the culture medium.
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PMID:Tissue culture of normal rat glomeruli: glycosaminoglycan biosynthesis by homogeneous epithelial and mesangial cell populations. 732 11

The defatted rabbit skin was extracted with 0.5 M LaCl3, and the extract was dialyzed exhaustively against distilled water. The precipitate formed during dialysis was dissolved in 28 mM EDTA (ethylenediamine tetraacetate) (pH 7.0). Fr A was obtained from the solution by precipitation with ethanol in the presence of sodium acetate. The results of gel filtration on Sepharose 4B, electrophoresis on cellulose acetate membrane before and after digestion with Streptomyces hyaluronidase, and analytical data indicated that Fr. A was hyaluronic acid with high molecular weight. The present observation together with previous findings suggest that the binding status of proteoglycans in the skin differs significantly from that in cartilages.
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PMID:Extraction of hyaluronic acid from rabbit skin with lanthanum chloride. 746 13


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