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 molecular weight secretion product of cell lines established from duct cell-derived human pancreatic adenocarcinomas was investigated in this study. After metabolic labeling and molecular sieve chromatography of culture medium, a product appeared in the void volume of a Superose 6 column that could be labeled with [3H]glucosamine, but not with [35S]sulfate. After further purification by anion exchange chromatography it was analyzed and demonstrated to be hyaluronan (HA). CsCl density gradient centrifugation revealed a density of 1.45 g/cm3 in a 4 M guanidinium hydrochloride solution. [3H]Glucosamine-labeled material could be degraded by digestion with hyaluronidase from two sources, but not with heparitinase I or chondroitinase AC. Sugar analysis revealed glucuronic acid and glucosamine at a molar ratio of 1:1. When the amount of HA synthesized by different pancreatic adenocarcinoma cell lines was compared, the values of the cell lines PaTu 8902 and PaTu II were about five- to tenfold higher than those of the lines PaTu 8988s, PaTu 8988t or HPAF, but an order of magnitude lower than in murine 3T3 fibroblasts. HA synthesis per cell decreased with increasing cell density. In serum-free cultures of cell lines with high HA synthesis it was 3 to 5 times higher compared to cultures that were supplemented with serum. We conclude that pancreatic adenocarcinoma cells secrete hyaluronan and thus contribute to the extracellular matrix of the tumor tissue. In pancreatic carcinoma cells, regulation of HA biosynthesis seems not to be positively correlated to proliferation as has been demonstrated for fibroblasts.
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PMID:Hyaluronan is a secretory product of human pancreatic adenocarcinoma cells. 164 63

We detected glomerular anionic sites in fixed, LR Gold-embedded ultra-thin tissue sections using cationic colloidal gold. Manual and computer-assisted quantitation were compared, and the influence of pH and glycosaminoglycan-degrading enzymes on site expression was examined. Both quantitation methods produced similar results. Alteration of pH within a narrow range (pH 2.5-3.0) markedly affected the staining pattern. At pH 2.5, epithelial and endothelial glycocalyx and regular sites restricted to the lamina rara externa were stained. At pH 3.0 and above, glycocalyx was unstained but intracellular and nuclear staining was present; glomerular basement membrane (GBM) and mesangial matrix sites were abundant. After chondroitinase ABC or hyaluronidase digestion, GBM staining was eliminated at pH 2.0 and reduced at pH 7.0 (p less than 0.001), suggesting that degraded sites are associated with chondroitin sulfate or hyaluronic acid. By contrast, prolonged heparitinase I digestion was ineffective at either pH. Digestion of purified substrates revealed crossreactivity of heparitinase towards chondroitin sulfate and of chondroitinase towards hyaluronic acid. Since tissue sites were reduced by chondroitinase but not heparitinase, we suggest that degradation is due to hyaluronidase activity of chondroitinase and the anionic sites are associated with hyaluronic acid. However, the influence of pH indicates that lamina rara externa sites are structurally distinct from other GBM anionic sites.
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PMID:Detection of glomerular anionic sites in post-embedded ultra-thin sections using cationic colloidal gold. 190 27

When cells dissociated from the neonatal rat brains are plated on a poly-lysine-coated surface in a serum-free medium, they display a strange morphology: a dark and extended cell body. Preincubation of the surface with fetal bovine serum was found to inhibit the appearance of this strange contraction of the basal cell sheets in a dose-dependent manner. This finding indicated the presence of a factor(s) in the serum, which might be an appropriate substratum for prolonged survival of brain neurons. In the current study, this factor was highly purified through DEAE ion-exchange chromatography followed by gel filtration. The factor was eluted from a Superose column at fractions corresponding to a molecular weight greater than 1000 kDa. By SDS-PAGE analysis, these fractions were found to contain a major band (>/=1000 kDa) positive for alcian blue and few minor bands faintly stainable with Coomassie blue. The activity of the purified sample, inducing the morphological change in cells, was diminished by incubation with chondroitinase ABC. Neither heparitinase II, hyaluronidase, nor trypsin modified the activity. An authentic chondroitin sulfate (type B) mimicked the serum action on the morphology of brain cells in early stages of culture. Taking these findings together, it is suggested that the factor in serum beneficial for the attachment of brain cells is composed of a chondroitin sulfate with a Mr greater than 1000 kDa. Cortical cells dissociated from the neonatal rat brain attached well to the purified factor-coated surface and displayed a healthy morphology: an optically-reflective cell body with thick neurites for at least 3 days in the absence of serum.
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PMID:A culture substratum appropriate for brain cells is a chondroitin sulfate glycosaminoglycan in serum. 947 1

We tested the hypothesis that matrix glycosaminoglycans contribute to lung tissue viscoelasticity. We exposed lung parenchymal strips to specific degradative enzymes (chondroitinase ABC, heparitinase I, and hyaluronidase) and determined whether the mechanical properties of the tissue were affected. Subpleural parenchymal strips were obtained from Sprague-Dawley rats and suspended in a Krebs-filled organ bath. One end of the strip was attached to a force transducer and the other to a servo-controlled lever arm that effected sinusoidal oscillations. Recordings of tension and length at different amplitudes and frequencies of oscillation were recorded before and after enzyme exposure. Resistance, dynamic elastance, and hysteresivity were estimated by fitting the equation of motion to changes in tension and length. Quasi-static stress-strain curves were also obtained. Exposure to chondroitinase and heparitinase I caused significant increases in hysteresivity, no decrement in resistance, and similar decreases in dynamic elastance relative to control strips exposed to Krebs solution only. Conversely, measures of static elastance were different in treated versus control strips. Hyaluronidase treatment did not alter any of the mechanical measures. These data demonstrate that digestion of chondroitin sulfate and heparan sulfate alters the mechanical behavior of lung parenchymal tissues.
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PMID:Effect of glycosaminoglycan degradation on lung tissue viscoelasticity. 1115 10