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)

By in vivo and in vitro methods of immunofluorescence, antibody to rat collagen and to rat kidney show the same regular, linear fluorescence following the outlines of the renal glomerular capillaries. Absorption of each antiserum with its homologous antigen completely removed the antibody for immunofluorescence, while absorption with the heterologous antigen had no effect. The nephrotoxicity persisted in the anti-kidney serum absorbed with collagen. By pretreatment of frozen normal rat kidney sections with various enzymes followed by immunofluorescence, it was shown that trypsin and hyaluronidase had no effect on the subsequent fluorescence of either antibody; papain reduced the fluorescence; and pepsin and Pronase acted on both antigens so that no fluorescence was present. One preparation of neuraminidase, derived from V. cholerae, reduced fluorescence of both antibodies in some preparations, but the same enzyme derived from influenza virus or C. perfringens had no effect on either. Collagenase completely prevented fluorescence of the antibody to collagen and had no effect on that to rat kidney. The findings in this study show that the antibody to collagen is directed to collagen in rat renal glomerular basement membranes and that the antibody to rat kidney reacts with some antigen other than collagen in these membranes.
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PMID:Comparison of reactions of antibodies to rat collagen and to rat kidney in the basement membranes of rat renal glomeruli. 430 40

Noninbred Sprague-Dawley rats were maintained on a choline-deficient diet containing 0.05% ethionine. After 10-13 weeks, livers were dispersed with collagenase, lysozyme, collagenase and hyaluronidase. Pronase, or a selected batch of trypsin. The highest yield of cells with histochemically demonstrable gamma-glutamyl transpeptidase (GGT) was obtained with trypsin. After velocity sedimentation in an isokinetic gradient of Ficoll in tissue culture medium, two modal populations of cells with histochemically demonstrable GGT were observed. The first mode contained cells that were morphologically different from hepatocytes and that may be oval cells. The second, more rapidly sedimenting modal population of cells with GGT was morphologically similar to hepatocytes as assessed with Wright's stain; the location of this population in the gradient was the same as the location of cells with the appearance of hepatocytes that lacked iron and that had decreased glucose 6-phosphatase. In multiple experiments, the purest fractions contained 71.7 +/- 3.5% cells (mean +/- SD) with the appearance of hepatocytes with histochemically demonstrable GGT.
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PMID:Separation of two populations of cells with gamma-glutamyl transpeptidase from carcinogen-treated rat liver. 611 83

The location and chemical composition of anionic sites in Bruch's membrane (BM) were examined using cationic probe molecules demonstrable in electron microscopic preparations and tissue digestion with specific degradative enzymes. Ruthenium red and native lysozyme revealed densities distributed at regular intervals in two major components of BM: the basal laminae of the retinal pigment epithelium (RPE) and choriocapillary endothelium (EN). Staining was not observed with succinylated lysozyme (anionic). Colloidal iron also failed to stain BM components. Following crude heparinase treatment at 43 degrees C (specific for heparan sulfate) anionic sites in the RPE basal lamina were not demonstrable with either ruthenium red or native lysozyme. Sites in the EN basal lamina were not affected. Chondroitinase treatment removed almost all of the ruthenium red-positive material in the EN basal lamina; lysozyme binding here was markedly reduced. No changes were observed in the RPE basal lamina after chondroitinase digestion. There was no morphological evidence for site removal by either neuraminidase or leech hyaluronidase, although a detachment of the RPE from BM often occurred after incubation of eye tissue in the latter. Pronase E removed all stainable material. These findings indicate that anionic sites in BM consist to a large extent of chondroitin sulfates and heparan sulfate.
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PMID:Location and chemical composition of anionic sites in Bruch's membrane of the rat. 617 64

Monocellular suspensions of epithelial cells from mammary glands of rabbits at 20-22 days of pregnancy were prepared by sequential dissociation with collagenase-hyaluronidase followed by Pronase. Maintenance in D-valine-substituted minimum essential medium (D-valine-MEM) supplemented with 10% dialyzed calf serum yielded monolayers enriched for rabbit mammary epithelial cells (RMEC). RMEC specifically and reversibly bound bovine PRL with Ka = 1.41-1.85 x 10(9)M-1. Association of lactogen with RMEC receptor followed bimolecular reaction kinetics with rate of 5.17 (+/- 0.75) x 10(5)M-1 sec-1 at 24 C, and 1.03 (+/- 0.11) x 10(6)M-1 sec-1 at 37 C. Dissociation was first order (K-1 = 5.97 (+/- 0.70) x 10(-5) sec-1) and was unaffected by the presence of lactogen. Specific binding determined with an excess of unlabelled bPRL was 66-77% of the total binding, and was optimal at pH 7.4. The binding reaction reached equilibrium in 2 h at 37 C, in 3 h at 24 C, and after 24 h at 4 C. Studies of binding capacity revealed the presence of 4.6-6.3 x 10(3) sites per cell, competition for which was limited to hormones demonstrating lactogenic activity. Recovered lactogen was not degraded by incubation with or dissociation from RMEC. Approximately 25% of the radioactivity remained associated with the cells even upon prolonged incubation. These studies demonstrated several advantages of RMEC for the investigation of hormone-receptor interaction and receptor regulation.
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PMID:Kinetic characterization of [125I] iodo-prolactin in binding to primary monolayer cultures of rabbit mammary epithelium. 628 30

Human vascular endothelial cells synthesize lactosaminoglycan-type glycoproteins which are found both associated with cells and secreted into the culture medium. Pronase-derived glycopeptides prepared from [3H]glucosamine-labeled glycoproteins were found to contain about 10% of the labeled products as a large size (Mr greater than 5000) 3H-labeled glycopeptide. Digestion of these 3H-labeled glycopeptides with endo-beta-galactosidase resulted in the release of smaller size saccharides, which were characterized as having the structure sialic acid----Gal----GlcNAc----Gal. Treatment of [3H]glucosamine-labeled cells with melittin caused 3H-labeled glycoconjugates to be released from the cells. Separation of released glycoproteins from proteoglycans by DEAE-cellulose chromatography indicated that melittin had released 25% of the total 3H-labeled glycoproteins from the cell and 3% of the 3H-labeled proteoglycans. The 3H-labeled glycoproteins were digested with Pronase and the resulting 3H-labeled glycopeptides were fractionated on Sephadex G-50. The large size fraction (Mr greater than 5000) now comprised about 30% of these released 3H-labeled glycopeptides. These high molecular weight 3H-labeled glycopeptides were degraded with endo-beta-galactosidase but not with testicular hyaluronidase. Analysis of the released 3H-labeled glycoproteins indicated a preferential release of glycoproteins of 70-90 kDa enriched in lactosaminoglycan-type oligosaccharides.
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PMID:Synthesis of lactosaminoglycan-containing glycoproteins by vascular endothelial cells. 670 15

An acidic glycoconjugate containing mannose, galactose and phosphate in approximately equimolar amounts was extracted from Leishmania donovani promastigotes and partially characterized. The glycoconjugate could be metabolically labeled with either [3H]mannose or [3H]galactose and was extractable from a delipidated residue fraction with water/ethanol/diethyl ether/pyridine/concentrated NH4OH (15:15:5:1:0.017) at 25 degrees C. The radioactively labeled glycoconjugate was found to possess the following characteristics: 1) comprised 45-60% of the total [3H]mannose label incorporated into macromolecules; 2) was soluble in alkaline solvents and 0.5% Triton X-100; 3) migrated as a broad band upon electrophoresis on sodium dodecyl sulfate-polyacrylamide gels with an approximate molecular weight of 15,000-30,000; 4) bound to DE52 cellulose and was eluted with a salt gradient of 0-0.1 M NaCl; 5) was insensitive to Pronase, hyaluronidase, chondroitinase, endo-beta-N-acetylglucosaminidase H, and endo-beta-galactosidase; and 6) possessed hydrophobic properties. An unusual feature of the glycoconjugate was its lability to mild acid hydrolysis (0.02 N HCl, 15 min, 60 degrees C). As determined by alkaline phosphatase and glycosidase digestion and paper chromatographic analysis, the major fragment generated by mild acid hydrolysis was found to be a phosphorylated galactosyl-beta-mannose disaccharide. All of these characteristics suggest that the glycoconjugate may be a polysaccharide and, possibly, may be important in parasite-host cell interactions.
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PMID:Expression of an unusual acidic glycoconjugate in Leishmania donovani. 670 85

The macromolecular basis of tissue swelling pressure and of the ability of tissue to exclude globular proteins, according to size, have been investigated using human umbilical cord. Exclusion data of tissue, and tissue from which the polysaccharides had been removed by hyaluronidase were compared. Exclusion of globular proteins by the polysaccharides, obtained by difference from the two sets of data, was similar to that reported for isolated polysaccharides in solution. It can be described by a sphere/cylinder geometric exclusion model. The exclusion behavior of the polysaccharide-free tissue was accounted for in terms of the component collagen fibrils, glycoprotein microfibrils and cells. Average pore diameters of 18 and 110 nm, respectively, for the intact tissue and for the polysaccharide-free tissue were estimated. Swelling pressure measurements were performed on intact, on hyaluronidase-treated and on hyaluronidase and then Pronase-treated tissues to obtain the contributions of the polysaccharides, of collagen and of microfibrils. Close to the in vivo volume of tissue, the swelling pressure is given almost entirely by the polysaccharides and is consistent with the osmotic pressure expected from the relative amounts of hyaluronic acid and proteoglycan present and their distribution in the extrafibrillar, extracellular space. Upon swelling or deswelling a small net contribution of the fibrillar system to the swelling pressure is evident.
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PMID:Macromolecular basis of globular protein exclusion and of swelling pressure in loose connective tissue (umbilical cord). 682 36

Pronase-resistant low molecular weight stimulators for the activation of proacrosin to acrosin were found in rhesus monkey oviduct fluid collected before, during and after ovulation, but the presence of high concentrations of acrosin inhibitors before and after ovulation partly masked the stimulation in unfractionated fluid. This low molecular weight fraction of oviduct fluid had no detectable esterase or amidase activity by itself, and the stimulating factors were sensitive to digestion by hyaluronidase and chondroitin ABC lyase and were presumed to be glycosaminoglycans. Heparin and hyaluronic acid had similar effects. The presence of soluble glycosaminoglycans at the site of fertilization suggests that they may have a role in capacitation and fertilization.
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PMID:Stimulation of rhesus monkey (Macaca mulatta) proacrosin activation by oviduct fluid. 700 Oct 8

The biosynthesis of glycosaminoglycans (GAG) and glycopeptides was studied in rat kidney cortex, glomeruli, and isolated glomerular basement membranes (GBM). Rats were given four intraperitoneal injections of [(35)S]sulfate and [(3)H]glucosamine (over 10 hr) and sacrificed 14 hr after the last injection. Fractions of kidney glomeruli and purified GBM were prepared. The percent of the label incorporated into specific GAG or into glycopeptides was determined by selective degradative techniques in conjunction with gel filtration chromatography using the methods of Hart [Hart, G. W. (1976) J. Biol. Chem. 251, 6513-6521; Hart, G. W. (1978) Dev. Biol. 62, 78-98]. After digestion with Pronase and chromatography on Sephadex G-50, approximately 68% of the total (35)S radioactivity and 10-15% of the total (3)H radioactivity incorporated into cortex, glomeruli, or GBM was found in the GAG fraction, and the remainder ( approximately 32% of (35)S radioactivity and 85-90% of the (3)H radioactivity) was found in glycopeptide fractions. Treatment of GAG fractions isolated from the three sources (cortex, glomeruli, and GBM) with nitrous acid (which degrades heparan sulfates) indicated that the majority (85%, 65%, and 87%) of the (35)S radioactivity as well as the majority (60%, 50%, and 91%) of the (3)H radioactivity from all three sources was degraded by this treatment. When nitrous acid-resistant GAG from GBM were subjected to digestion with Streptomyces hyaluronidase (which degrades hyaluronic acid), approximately 6% of the (3)H-labeled material was sensitive to this treatment. The remaining (35)S- and (3)H-labeled GAG isolated from GBM were digested with chondroitinase ABC (which degrades chondroitin sulfates A and C and dermatan sulfate). Although the ratios of the types of GAG synthesized by all three sources were similar, in GBM the ratios of (35)S- to (3)H-labeled GAG and of (3)H-labeled glycopeptides to (3)H-labeled GAG were higher (2.5 times) than those found for glomeruli. The data demonstrate the synthesis of both sulfated and nonsulfated GAG by rat kidney cortex and glomeruli and their transport to and incorporation into the GBM. Heparan sulfate is the major GAG synthesized by glomeruli, but the glomeruli also synthesize smaller amounts of hyaluronic acid and chondroitin sulfates, which are in part incorporated into GBM. In addition, the renal cortex and the glomeruli synthesize glycopeptides, some of which are sulfated, and incorporate them into GBM.
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PMID:Sulfated and nonsulfated glycosaminoglycans and glycopeptides are synthesized by kidney in vivo and incorporated into glomerular basement membranes. 701 44

The binding of albumin to the glomerular capillary wall was studied using albumin-gold in perfused kidneys, the interaction of [3H]albumin with isolated glomeruli at 37 degrees C and 4 degrees C and the interaction at [3H]albumin with purified basement membrane. The albumin-gold was found to bind predominantly to the basement membrane and this interaction could be dissociated with high concentrations of albumin. There was binding of albumin to isolated rat glomeruli which exhibited temperature dependence. Glomeruli exhibited a binding site at both 37 degrees C and 4 degrees C with an association constant in the range of 1 to 3 x 10(4) M-1 that bound 7 x 10(13) molecules/glomerulus. At 37 degrees C, however, there was anomalous Scatchard binding behaviour at relatively higher concentrations of albumin (30 to 50 mg/ml) which could be due to either glomerular cell uptake or the appearance of multiple binding sites or both. The binding of albumin to isolated glomeruli and the glomerular albumin levels in isolated kidney perfusion could largely be accounted for by the binding of albumin to the glomerular basement membrane. The albumin binding to glomeruli at 37 degrees C was enhanced by Pronase digestion and heparinase digestion, but remained unchanged following trypsin treatment or neuraminidase treatment. Similarly, albumin was shown to bind to purified basement membrane preparations. This binding was also enhanced (approximately 80 times) by heparinase digestion but remained unchanged after digestion with chondroitinase ABC or hyaluronidase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Albumin interaction with the glomerular capillary wall in vitro. 778


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