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)

The murine monoclonal antibody (MAb) designated DF3 has defined a high m.w. antigen detectable in human breast carcinomas and in human milk. DF3 antigen is detectable on apical borders of secretory mammary epithelial cells and in the cytosol of less differentiated malignant cells. DF3 antigen expression has been shown to correlate with the degree of human breast tumor differentiation, and the detection of a cross-reactive species in human milk has suggested that DF3 antigen might be useful as a biochemical marker of differentiated mammary epithelial cells. To further characterize DF3 antigen, we have developed an approach to purify the cross-reactive species by using gel filtration and antibody affinity chromatography. The affinity column-purified DF3 antigen was absorbed by wheat germ agglutinin and peanut agglutinin, but not by concanavalin A or lentil lectin. In contrast, wheat germ agglutinin inhibited MAb DF3 reactivity with the purified antigen, whereas there was little, if any, inhibition when using peanut agglutinin. These findings are thus consistent with the involvement of terminal N-acetyl-D-neuraminic acid and/or N-acetylglucosamine residues in the antigenic site. DF3 antigenicity was also sensitive to neuraminidase, but not chondroitinase ABC, chondroitinase AC, chondroitin-4-sulfatase, or hyaluronidase. Furthermore, DF3 antigen was sensitive to Pronase, subtilisin BPN', and alpha-chymotrypsin. The presence of O-glycosidic linkages between carbohydrate and protein in the DF3 antigenic site was further supported by the presence of NaBH4-sensitive sites. Together, these results suggest that sialyl oligosaccharides present on a peptide backbone are required for maintaining DF3 antigenicity. Similar findings have been demonstrated for DF3 antigen purified from both human milk and breast cancer effusions. However, the DF3 antigen in human milk consisted of a single high m.w. species, whereas the tumor-associated antigen consisted of two distinct glycoproteins with m.w. of 330,000 and 450,000. These findings may be relevant to the recent demonstration that distinct high m.w. DF3 antigens are elevated in the circulation of patients with breast carcinoma.
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PMID:Purification and characterization of a high molecular weight glycoprotein detectable in human milk and breast carcinomas. 404 99

Ultrastructural studies on human lung were performed with special attention to the interstitial acid mucopolysaccharides by Ruthenium Red staining and several enzyme digestion tests with Streptomyces hyaluronidase, chondroitinase ABC, chondroitinase AC, heparinase, trypsin and collagenase. Periodic lateral granules on the major cross bands of collagen fibrils and amorphous coats on them became visible by Ruthenium Red staining. The surface of elastic fibres, associated microfibrils, and some fine fibrils 10-20 nm in diameter were stained. Ruthenium Red also stained the surface of fibroblast and smooth muscle cells, basement membrane and filamentous long segments. In the interstructural space, granular substances 10-80 nm in diameter and fine filaments 3--4 nm thick, which formed a fine reticular network, were clearly observed. They were not visible on the usual thin section. The granular substances were located on the cross points of the fine filaments. They spread continuously and connected with each of the cells and extracellular structures in the pulmonary interstitium. The results of the enzyme digestion tests on the Ruthenium Red-positive material are discussed.
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PMID:Electron microscopic observations on pulmonary connective tissue stained by Ruthenium Red. 617 14

The nature of Cuprolinic Blue-positive anionic filaments in mouse lung alveoli has been characterized. The contrast of filaments in the alveolar basement membrane of type I epithelial cells was lost on treatment with nitrous acid and pronase (without prefixation). In contrast, neither neuraminidase, chondroitinase ABC or AC, nor Streptomyces hyaluronidase had any effect. Treatment with pronase (after prefixation) and 2.0 M MgCl2 (after prefixation) also had no effect, indicating that the filaments are heparan sulphate proteoglycans. The filaments in the alveolar basement membrane of type II epithelial cells and in the capillary basement membrane of the endothelial cells were also nitrous acid sensitive, but chondroitinase ABC-insensitive. A model in which the whole alveolus contains a single layer of heparan sulphate-containing proteoglycan monomers is proposed. Furthermore, the collagen fibril associated filaments remained unaffected after treatment with nitrous acid, neuraminidase or Streptomyces hyaluronidase, or after digestion with pronase (after prefixation) and treatment with 2.0 M MgCl2 (after prefixation). These filaments, however, could no longer be detected when digestion with chondroitinase ABC or pronase (without prefixation) was applied; chondroitinase AC treatment clearly affected the filaments, although they still were visible. These results indicate that the filaments are dermatan sulphate-containing proteoglycans. Some functional aspects of the proteoglycans are discussed.
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PMID:Staining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic blue-positive, anionic sites. 620 77

Crude glycosaminoglycan (GAG) fraction was directly precipitated with cetylpyridinium chloride without prior dialysis of urine of orthopedic patients. The crude GAG fraction was then fractionated with trichloroacetic acid (TCA). The TCA-insoluble peptide-bound GAG fraction thus obtained was treated with alkali to eliminate the peptide moiety for enzymatic analysis. The GAG compositions of this fraction and the TCA-soluble fraction were determined by digestion with mucopolysaccharidases (chondroitinase AC, chondroitinase B, chondroitinase C, heparitinase and Streptomyces hyaluronidase). When the amount of the crude GAG fraction was small, no significant amount of the TCA-insoluble peptide-bound GAG fraction was obtained. The GAG composition of this case was also determined by the same procedures after direct alkali-treatment of the crude GAG fraction. The data indicated that the proportion of the TCA-insoluble peptide-bound GAG fraction was very small. The alkali-treated TCA-insoluble peptide-bound GAG fraction contained a larger proportion of heparan sulfate than the TCA-soluble GAG fraction. It was clearly demonstrated that the patients with Werner's syndrome and mucopolysaccharidosis I-S (Scheie) excreted large amounts of hyaluronic acid and dermatan sulfate respectively, into urines. It was indicated in most cases that major urinary GAG were chondroitin 4-sulfate, chondroitin 6-sulfate plus chondroitin and heparan sulfate, while minor ones were dermatan sulfate and hyaluronic acid. In addition, the data suggested a wide range of the degree of desulfation or urinary GAG, and the presence of significant amounts of keratan sulfate plus acidic glycopeptides in the urinary GAG fractions. The present data provided more precise information on urinary GAG from orthopedic patients than those reported previously.
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PMID:Enzymatic determination of urinary glycosaminoglycans from orthopedic patients. 640 65

Intima-media of thoracic aortas obtained from estrogen-treated, estrogen-progesterone-treated and sham-treated ovariectomized rabbits were separately digested with pronase after extraction of fat. Glycosaminoglycan fractions were then separated from the resulting glycoconjugate fractions by precipitation with cetylpyridinium chloride. The glycosaminoglycan levels increased after treatments with estrogen and estrogen-progesterone. Glycosaminoglycan compositions were determined by sequential digestion with Streptomyces hyaluronidase, chondroitinase AC, chondroitinase ABC and heparitinase 1. The proportions of dermatan sulfate and chondroitin sulfates AC increased after treatments with these hormones, while those of hyaluronic acid and heparan sulfate decreased. The changes of the proportions of dermatan sulfate and hyaluronic acid were dramatic. The changes of the glycosaminoglycan compositions with these hormones are thought to be an anti-atherosclerotic effect of these female hormones.
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PMID:Hormonal effects on glycosaminoglycans in thoracic aortas of rabbits. 643 34

The glycosaminoglycan (GAG) components of the proteoglycans (PG) in the epithelial and connective tissue extracellular compartments of human gingivae have been determined. Following proteolytic digestion of the separated tissues. GAG were identified electrophoretically. These were hyaluronic acid (HA), heparan sulfate (HS), dermatan sulfate (DS) and chondroitin-4 sulfate (ChS-4). Neither ChS-6 nor keratan sulfate (KS) was observed. Confirmation of the nature of the molecular species was obtained by the use of Streptomyces hyaluronidase, chondroitinase AC II and degradation with nitrous acid. Quantitatively, the major GAG component of the epithelial specimens was HS (59.6%), whilst DS (60.6%) constituted the major GAG of human gingival connective tissue.
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PMID:Glycosaminoglycans of human gingival epithelium and connective tissue. 645 53

Intima-media of porcine, canine, rabbit, and human thoracic aortas were separately digested with pronase, after extraction of fat. Glycosaminoglycan fractions were then separated from the resulting glycoconjugate fractions by precipitation with cetylpyridinium chloride. Glycosaminoglycan compositions were determined by sequential digestion with Streptomyces hyaluronidase, chondroitinase AC, chondroitinase ABC and heparitinase 1. All the tissues contained hyaluronic acid, chondroitin sulfates AC, dermatan sulfate and heparan sulfate. Of these glycosaminoglycans, chondroitin sulfates AC were the most prominent ones. Relatively large proportions of heparan sulfate were contained in these tissues except for canine aorta. It is noteworthy that the proportions of glycosaminoglycans in the intima-media of rabbit and human thoracic aortas with similar maturation were quite similar, although those of others differed from each other.
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PMID:Comparison of glycosaminoglycans from thoracic aortas of several mammals. 646 8

Glycosaminoglycan oligosaccharides generated by treatment of biosynthetically radiolabelled dermatan sulphate and hyaluronic acid with chondroitin AC lyase or testicular hyaluronidase may be resolved into a series of discrete bands by polyacrylamide-gel electrophoresis. Bands were identified by fixation in glacial acetic acid containing 20% (w/v) 2,5-diphenyloxazole followed by fluorography. The bands represented glycans which differed in size by one disaccharide unit. For the larger oligosaccharides (decasaccharides and above) of similar charge: mass ratio, there was a linear relationship between electrophoretic mobility and log Mr. However, the smaller species showed anomalous migration patterns. Consideration of the structures of the fragments produced by the different enzyme treatments suggests that copolymeric and homopolymeric oligosaccharides may be separated by polyacrylamide-gel electrophoresis. There are many potential applications of this technique, foremost amongst them being studies on the molecular size heterogeneity and patterns of enzyme-mediated depolymerization of native glycosaminoglycan chains and investigations into rates of polymer chain elongation and post-polymerization modification reactions so essential to glycosaminoglycan function.
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PMID:Separation of radiolabelled glycosaminoglycan oligosaccharides by polyacrylamide-gel electrophoresis. 647 95

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

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


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