Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The polysaccharide from blackgram (Phaseolus mungo) has been previously reported to cause lower cholesterol, phospholipids and triglyceride levels in rats fed either low-or high-fat diets containing cholesterol. The effect of this polysaccharide fraction as compared to that of glucose and sucrose on the metabolism of glycosaminoglycans and glycoprotein has been studied. The pattern of change in the levels of different glycosaminoglycans varied in the different tissues. Sucrose fed animals gave lower levels of sulphated glycosaminoglycans in the aorta and liver. The polysaccharide and glucose fed animals gave comparable values in the aorta except in the case of chondroitin sulfate B which was higher and heparin lower in the polysaccharide group. L-glutamine:D-fructose-6-phosphate amino transferase and UDPG dehydrogenase were lowest in the sucrose fed animals and highest in the polysacchride group with the animals in the glucose group showing intermediate values, but UDPG pyrophosphorylase, while highest in the polysaccharide group, was similar in the glucose and sucrose groups. Some of the degrading enzymes studied-beta-glucuronidase, hyaluronidase and aryl sulphatase-were highest in the sucrose group and generally lowest in the polysaccharide group. Levels of 3'-phosphoadenosine-5'-phosphosulphate, the biological sulphating agent, the sulphate activating system which includes ATP sulphurylase and APS kinase and sulphotransferase activity were also lowest in the sucrose fed group and highest in the polysaccharide group. The glycoprotein concentration was highest in the liver and lowest in the kidney in the sucrose group.
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PMID:Nature of the dietary carbohydrate and metabolism of glycosaminoglycans and glycoproteins in rats. 17 34

Oligomers of hyaluronic acid were prepared by digestion of hyaluronic acid from rooster combs with testicular hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35), leech head hyaluronidase (hyaluronate 3-glycanohydrolase, EC 3.2.1.36), and with fungal hyaluronidase (hyaluronate lyase from Streptomyces hyalurolyticus). The oligomers were fractionated by gel permeation, using Sephadex G-50. Oligomers isolated after incubation of the hyaluronic acid with the testicular hyaluronidase were further modified. To prepare oligomers with N-acetylglucosamine at both ends, terminal nonreducing glucuronic acid residues were removed with beta-glucuronidase. Reducing terminal N-acetylglucosamine residues were removed by reaction under mildly alkaline conditions. The reducing terminal N-acetylglucosamine residues were also reduced with sodium borohydride to form N-acetylglucosaminitol. The potentials of the various oligosaccharides to bind to the proteoglycan from bovine nasal septum cartilage were estimated by determining their effectiveness as inhibitors of the proteoglycan-hyaluronate interaction. The present study shows that, to bind maximally to the proteoglycan, the hyaluronate oligosaccharide must be at least 10 sugar residues in length and be terminated at the nonreducing and reducing ends with a glucuronate residue and an N-acetylglucosamine residue, respectively. Sugar residues extended beyond this basic decasaccharide, do not interact with the hyaluronate binding site on the proteoglycan.
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PMID:Interactions of cartilage proteoglycans with hyaluronate. Inhibition of the interaction by modified oligomers of hyaluronate. 43 8

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

Pastereulla multocida organisms were separated from the blood of experimentally infected turkeys by differential centrifugation. An average of 92% of the residual host-cell contamination was removed from the pasteurellas by density gradient centrifugation in sucrose. Sucrose suspensions of the turkey-grown pasteurellas partially lysed after freezing and thawing. Treatment of freeze-thawed suspensions with DNAse, hyaluronidase, lysozyme, EDTA, and Triton X-100 did not influence their ability to induce protection against homologous and heterologous serotype challenge exposures. Lysozyme, EDTA, and Triton X-100 completely lysed the pasteurellas and rendered the cross-protection factor(s) filterable. Addition of adjuvant to completely lysed P multocida did not appear to enhance protection in turkeys against heterologous serotype challenge exposure. Adjuvant added to the pellet or supernatant fraction of centrifuged complete lysate enhanced protection in turkeys. Vaccines prepared from different serotypes of turkey-grown P multocida protected chickens and mice against homologous and heterologous serotype challenge exposures.
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PMID:Lysates of turkey-grown Pasteurella multocida: protection against homologous and heterologous serotype challenge exposures. 680 19

Matrix vesicles (MV) were shown to initiate mineralization in cartilage and other vertebrate tissues. However, the factors that drive this process remain to be fully elucidated. Recent studies have shown that a preformed nucleational core consisting mainly of a Ca(2+)-phosphatidylserine-Pi complex, is necessary for the accumulation of Ca2+ by MV. In addition, the collagens attached to the MV surface were shown to play an important role in stimulating Ca2+ uptake. In this study, we extend this knowledge by showing that both, the nucleational core and the collagens (types II and X), are co-requirements for rapid influx of Ca2+ into intact MV. MV to which collagen fragments were attached were released from hypertrophic chicken cartilage by trypsin and collagenase digestion (trypsin/collagenase-released MV (TCRMV), while "collagen-free" MV were released by hyaluronidase and collagenase digestion (hyaluronidase/collagenase-released MV (HCRMV). In contrast to TCRMV which showed active uptake of Ca2+, HCRMV showed only little uptake. However, binding of native type II collagen to HCRMV stimulated uptake of Ca2+. Sucrose gradients separated TCRMV and HCRMV into three different density fractions: a low density top fraction (SI), an intermediate density middle fraction (SII), and a high density pellet fraction (SIII). The SIII fractions of TCRMV and HCRMV contained significantly higher levels of mineral ions than did the SI and SII fractions. Only the SIII fraction of TCRMV which contained a stable nucleational core and surface-attached collagens, showed active Ca2+ uptake; all other sucrose fractions of TCRMV and HCRMV showed little or no uptake. Detergent treatment to purposely rupture the membrane greatly enhanced Ca2+ uptake by the SIII fraction of HCRMV, presumably by exposing the internal nucleational core. Addition of either native type II or type X collagen to the intact SIII fraction of HCRMV stimulated Ca2+ uptake to a level similar to that of the SIII fraction of TCRMV; however, incubation of the SI and SII fractions of either TCRMV or HCRMV with type II or X collagen did not activate Ca2+ uptake. These findings indicate that both a functional nucleational core and surface-attached collagens need to be present to support active mineralization of MV.
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PMID:Roles of the nucleational core complex and collagens (types II and X) in calcification of growth plate cartilage matrix vesicles. 805 Oct 98