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)

Mannose-(Man) and N-acetylglucosamine- (GlcNAc)-terminated glycoproteins are cleared from blood by carbohydrate-specific receptors present on both hepatic endothelial and Kupffer cells. It is not known whether the same receptors are present on each cell type or the relative contributions to glycoprotein metabolism made by Kupffer and endothelial cells. Here we report experiments where data from glycoprotein metabolism by purified populations of isolated rat hepatic endothelial and Kupffer cells have been analyzed by mathematical modelling and parameter estimation. Kupffer cells had significantly higher binding rate constants (k'21) than endothelial cells for agalactoorosomucoid (AGOR) and hyaluronidase, but lower k12 ('off-rate') indicating that Kupffer cells had higher affinities for Man/GlcNAc-terminated glycoproteins than endothelial receptors. Furthermore, although endothelial cells had similar affinities (k'21 and k12) for AGOR and hyaluronidase, the 'off-rate' of Kupffer cells was significantly greater for AGOR than for hyaluronidase, indicating that Kupffer cell receptors have lower affinity for AGOR. Internalization and ligand catabolic rates also differed between the two cell types. The data indicate that Kupffer and endothelial cells appear to have different Man/GlcNAc receptors and that the destination of a glycoprotein and its subsequent processing is determined by the structure of a glycoprotein's oligosaccharide.
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PMID:Uptake and processing of glycoproteins by isolated rat hepatic endothelial and Kupffer cells. 233 92

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

Experiments with immobilized concanavalin A strongly suggest a glycoprotein nature of three honey-bee venom enzymes, phospholipase A2, hyaluronidase and acid phosphatase. The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Mannose, fucose and N-acetylglucosamine, but not galactose nor N-acetylgalactosamine, are present in the con A-binding fraction of bee venom. It is therefore concluded that only N-glycosidically linked carbohydrate occurs in bee venom glycoproteins.
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PMID:The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. 665 11