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)

Colon cancer cells in culture synthesize and secrete mucin glycoproteins, which carry a number of cancer-associated antigens. However, the structures and mechanisms of biosynthetic processing are not well understood. Mucins synthesized and secreted by LS174T human colon cancer cells were compared to those in LS174T xenografts in athymic mice. Mucins radiolabeled with glucosamine or sulfate were purified by gel filtration and cesium chloride density gradient centrifugation. The mucins were of high molecular weight and were resistant to chondroitinase ABC, hyaluronidase and HNO2 treatment. They were, however, susceptible to pronase digestion and mild alkaline treatment. Using radiochemical precursors, the cellular mucin was shown to contain fucose, galactose, N-acetylgalactosamine, N-acetylglucosamine, N-acetylneuraminic acid, and sulfate. Oligosaccharides released by beta-elimination had N-acetylgalactosaminitol as the reduced amino sugar and also unreduced galactosamine, indicating that there is N-acetyl-galactosamine O-glycosidically attached to protein core and also peripheral N-acetyl-galactosamine not directly linked to protein. DEAE-cellulose chromatography of mucins showed two major peaks with both intracellular and secreted mucins, but xenograft mucins also had more acidic components. Sulfate-labeled mucins were shifted to less acidic peaks by neuraminidase digestion, which indicates that the same mucin molecules are both sialylated and sulfated. We conclude that the intracellular mucins of cultured colon cancer cells, those secreted into the medium, and those in nude mouse xenografts are chemically similar, but differ in sialic acid and sulfate content. This experimental model system, LS174T cells maintained in culture and as nude mouse xenografts, may be useful for further biosynthetic and structural studies of colon cancer mucin.
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PMID:Comparison of metabolically labeled mucins of LS174T human colon cancer cells in tissue culture and xenograft. 273 49

1. Two polysaccharides were isolated from the interstitial matrix surrounding the photoreceptor cells of cattle retina. They were liberated from this region of the tissue in a soluble form after agitation of whole retinas in 0.9% sodium chloride. One, which comprises two-thirds of the polysaccharides present, is a hyaluronidase-sensitive ;half-sulphated' chondroitin sulphate containing uronic acid, galactosamine and sulphate in the molar proportions 1.27:1.0:0.54. The other is a hyaluronidase-resistant non-sulphated heteropolysaccharide for which the name sialoglycan is proposed. It contains galactose, glucosamine and sialic acid in the molar proportions 2.4:1.0:0.4. Both polysaccharides contain only small amounts of nitrogen in excess of the amount calculated from their amino sugar and sialic acid content. 2. A similar combination of mucopolysaccharides is associated with the pigment epithelial-cell layer but in quantities only one-fifth of those present in the adjacent matrix area. 3. The ease with which they are released into aqueous media is consistent with the assumption that they are present in the extracellular spaces in both of these tissue layers. 4. The retinal residue left after removal of the two soluble polysaccharides is rich in amino sugar- and sialic acid-containing polymers, which appear to be firmly bound to the tissue fragments. 5. About one-third of the sialic acid and one-tenth of the amino sugar could be extracted with chloroform-methanol. The components in this fraction were tentatively identified as gangliosides. 6. Digestion of the chloroform-methanol-insoluble residue with Pronase yielded as the principal product a heteropolysaccharide containing 16.5% of glucosamine, 24.3% of neutral sugar (galactose plus fucose) and 18.1% of sialic acid. This substance has been classified as a sialoglycan of composition similar to (but not identical with) that of the soluble one isolated from the matrix area of the tissue.
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PMID:The acid mucopolysaccharides of cattle retina. 423 42

Normal rat liver lysosomes were isolated by the technique of loading with Triton WR-1339. Purity of the preparation was monitored with marker enzymes; a high enrichment in acid hydrolases was obtained in the tritosome fraction. In 0.0145 M NaCl, 4.5% sorbitol, 0.6 mM NaHCO(3), pH 7.2 at 25 degrees C the tritosomes had an electrophoretic mobility of -1.77 +/- 0.02 microm/s/V/cm, a zeta potential of 23.2 mV, a surface charge of 1970 esu/cm(2), and 33,000 electrons per particle surface assuming a tritosome diameter of 5 x 10(-7) m. Treatment of the tritosomes with 50 microg neuraminidase/mg tritosome protein lowered the electrophoretic mobility of the tritosome to -1.23 +/- 0.02 microm/s/V/cm under the same conditions and caused the release of 2.01 microg sialic acid/mg tritosome protein. Treatment of the tritosomes with hyaluronidase did not affect their electrophoretic mobility, while trypsin treatment elevated the net negative electrophoretic mobility of the tritosomes. Tritosome electrophoretic mobilities indicated a homogeneous tritosome population and varied greatly with ionic strength of the suspending media. pH vs. electrophoretic mobility curves indicated the tritosome periphery to contain an acid-dissociable group which likely represents the carboxyl group of N-acetylneuraminic acid; this was not conclusively proven, however, since the tritosomes lysed below a pH of 4 in the present system. Total tritosome carbohydrate (anthrone-positive material as glucose equivalents) was 0.19 mg/mg tritosome protein while total sialic acid was 3.8 microg (11.4 nmol)/mg tritosome protein. A tritosome "membrane" fraction was prepared by osmotic shock, homogenization, and sedimentation. Approximately 25% of the total tritosome protein was present in this fraction. Analysis by gas-liquid chromatography and amino acid analyzer showed the following carbohydrate composition of the tritosome membrane fraction (in microgram per milligram tritosome membrane protein): N-acetylneuraminic acid, 14.8 +/- 3; glucosamine, 24 +/- 3; galactosamine, 10 +/- 2; glucose, 21 +/- 2; galactose, 26 +/- 2; mannose, 31 +/- 5; fucose, 7 +/- 1; xylose, 0; and arabinose, 0. The results indicate that the tritosome periphery is characterized by external terminal sialic acid residues and an extensive complement of glycoconjugates. Essentially all the tritosome N-acetylneuraminic acid is located in the membrane and about 53% of it is neuraminidase susceptible.
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PMID:The lysosome periphery: biochemical and electrokinetic properties of the tritosome surface. 482 95

To elucidate precise chemical nature of urinary keratan sulfate (KS) of Morquio's disease, crude glycosaminoglycans (GAG) were separated from 24-hr urines of 3 patients with Morquio's disease and from pooled urine of a healthy boy, using cetylpyridinium chloride. KS fractions were then separated from the crude GAG after removal of other GAG and acidic glycopeptide by successive digestion with testicular hyaluronidase and chondroitinase ABC, and by nitrous acid treatment, followed by Dowex 1 column chromatography. The distribution of KS in several fractions (1.5 M Fr-5.0 M Fr) obtained by Dowex 1 column chromatography suggested polydispersity of urinary KS. The relative amounts (micrograms/24-hr urine/kg body weight) of the KS fractions excreted into Morquio's urine were 52-63 times as much as that excreted into normal urine. The KS fractions contained galactose, glucosamine and sulfate as the major constituents, together with fairly amounts of galactosamine and sialic acid, and small amounts of mannose, L-fucose and glucose. The KS fractions resembled sulfated glycopeptide with respect to the sugar composition. The contents of sulfate and sialic acid in each KS fraction from Morquio's urine were higher than those in the corresponding one from normal urine, whereas opposite was the case for the ratio of glucosamine to galactosamine. The sulfate contents in the KS fractions from Morquio's urine indicated that the patient excreted over-sulfated KS into urine. The chemical compositions of the KS fractions from Morquio's urine suggest that the sulfatase specific for 6-sulfate linked to sugars with the galactose configuration may act in a early step of the catabolism of oversulfated KS in the normal tissues.
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PMID:Urinary keratan sulfate of Morquio's disease. 645 53

Polysaccharides and other complex carbohydrates were released by proteolysis of the chloroform-methanol insoluble residue of 10 day-old worms and eggs of Hymenolepis diminuta. Gas-liquid chromatographic analysis of alditol acetate derivatives of monosaccharides released from the polysaccharides by hydrolysis revealed that in the 10 day-old worm, glucose was the most abundant sugar, followed by galactose, glucosamine, galactosamine, fucose and possibly rhamnose. Mannose was least abundant and xylose was absent. In the egg, glucose and galactose were equally abundant, followed by the same sugars found in 10 day-old worms, and xylose was present. Uronic acid was detected in both fractions by specific chemical tests. None of the saccharide material from eggs and worms was susceptible to degradation by Streptomyces hyaluronidase, chondroitinase AC, and slightly susceptible to chondroitinase ABC, as shown by electrophoretic analysis on composite 2.2% acrylamide-agarose slab gels and 4.5/12.5% polyacrylamide gels before and after enzymatic treatment. One of the gel-separable bands, however, was degradable by both nitrous acid and Flavobacterium heparinase. Both bands from eggs were degradable by nitrous acid. These results suggest that eggs contain heparin and/or heparan sulfate and perhaps dermatan sulfate and that 10 day-old worms also have these polyglycans but possibly not chondroitin sulfate or hyaluronic acid.
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PMID:Characterization of polysaccharides of the eggs and adults of Hymenolepis diminuta. 653 86

A 6-sulfated tetrasaccharide obtained by digesting chondroitin-6-sulfate with testicular hyaluronidase was used as a substrate for the determination of N-acetylgalactosamine-6-sulfate sulfatase activity. The activity was not detected in liver obtained from the elder sister with clinically classic Morquio syndrome and 4.7% of the control in liver from the younger sister with the same disease.
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PMID:Activities of N-acetylgalactosamine-6-sulfate sulfatase in liver from two sisters with morquio syndrome. 677 85

Isolated rat jejunal villus and crypt cells prepared by differential scraping and hyaluronidase dispersion were used in the presence of 8 mM sodium taurocholate to study the incorporation of sn-[3H]glycerol-2-monooleate, [1-14C]palmitate, [1-14C]acetate, L-[4,5(n)-3H]leucine and D-[1-14C]glucosamine into cellular and medium lipids and proteins, respectively. The villus cells were capable of an apparently normal biosynthesis of triacylglycerols and phospholipids, as well as of proteins and glycoproteins despite an altered dye permeability and increased release of cytosolic and membrane enzymes. About 20-30% of the newly formed triacylglycerols and about 35% of the newly formed phospholipids were secreted into the medium and were recovered as triacylglycerol-rich particles. Labelled proteins and glycoproteins were also recovered from this fraction. The crypt cells synthesized about one-half as much triacylglycerol and phospholipid as did the villus cells, but secreted little or no labelled lipid into the postincubation medium. The release into the medium of triacylglycerols synthesized by the villus cells was blocked by a pretreatment of the isolated cells with the microtubule disruptors, nocodazole, colchicine and colcemid; by the amino sugar, D-galactosamine; by the inhibitors of protein synthesis, puromycin and cycloheximide, and by the inhibitor of the biosynthesis of phosphatidylcholine, chlorocholine. These results indicate that the secretion of labelled lipids, proteins and glycoproteins by the upper villus enterocytes in the presence of sodium taurocholate is not entirely due to cell breakage and spillage of contents. It is concluded that incubations of isolated villus cells of rat jejunum with mixed micellar solutions containing 8 mM taurocholate are compatible with an apparently normal biosynthesis and secretion of triacylglycerol-rich particles.
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PMID:Synthesis and release of lipids and lipoproteins by isolated rat jejunal enterocytes in the presence of sodium taurocholate. 728 26

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

Hyaluronic acid was the only glycosaminoglycan found in detectable amounts in the pulmonary secretions of patients with cystic fibrosis. The compound gave a hexuronate/hexosamines molar ratio of approximately 1. Glucosamine represented over 98% of the total hexosamines, the remainder being galactosamine. No hexoses or sulfate could be detected. It moved as a single spot with the mobility of standard hyaluronic acid on cellulose acetate electrophoresis and this spot disappeared after digestion with testicular hyaluronidase. It was associated with trace amounts of protein, the major amino acids of which are aspartic acid, glutamic acid, glycine, and alanine.
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PMID:Hyaluronic acid. An indicator of pathological conditions of human lungs? 739 Jun 11

Hyaluronic acid was the only glysosaminoglycan detected in the pulmonary secretions of healthy adult rats exposed to inhalation to methylene chloride, but not of control animals. The compound migrated as a single spot with the mobility of standard hyaluronic acid on cellulose acetate electrophoresis and disappeared after digestion with testicular hyaluronidase. Its identification was confirmed by finding hexuronate/hexosamine in a molar ratio of approx. 1. Glucosamine represented over 97% of the total hexosamine, the remaining 3% being galactosamine. No hexose or sulfate could be detected. Sodium dodecyl sulfate--polyacrylamide gel electrophoresis showed no protein associated with this glycosaminoglycan. It appears that the secretion of hyaluronic acid into the airways may be the result of pulmonary inflammation induced by the toxic effects of methylene chloride.
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PMID:Hyaluronic acid--an indicator of pulmonary injury? 746 58


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