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:3.1.6.4 (chondroitinase)
2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of streptozotocin-induced diabetes on the structure of heparan sulfate (HS) prepared from rat kidney glycosaminoglycans (GAG) was evaluated. GAG were isolated and purified from the kidneys of diabetic and age-matched control rats by standard procedures. HS was prepared from GAG by digestion with chondroitinase ABC and precipitation with cetylpyridinium chloride. The tissue dry weight of diabetic kidneys was greater than that of the controls. The amounts of protein and DNA per tissue dry weight were decreased in the diabetic group, while GAG and hydroxyproline remained unchanged. The above information indicates that the extracellular components are increased in diabetes. There was no significant difference in the amount of HS to tissue dry weight between the diabetic and control groups. When the molecular weight of the HS from both groups was compared by Sephacryl S-300 HR column chromatography, the HS peak for the diabetic kidney indicated a slightly higher molecular weight and the base of the peak was broader than that for the controls. A reduction in N-sulfate residues was observed in Sephadex G-50 profiles after nitrous acid degradation of the HS. The ratio of glucuronic acid to its epimer, iduronic acid, in diabetic kidney HS was slightly lower than that in the controls. This indicates that diabetes may influence the carbohydrate chain structure of the HS in the kidney. Quantitative and qualitative changes in the kidney HS may contribute to the symptoms associated with diabetic nephropathy.
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PMID:Effect of streptozotocin-induced diabetes on the structure of heparan sulfate from rat kidneys. 253 90

Previous studies have shown that lymphocytes carry cell surface receptors for sulphated polysaccharides (SPS), and SPS recognition may play a role in lymphocyte migration and positioning in vivo. This paper describes attempts to isolate and characterize the endogenous glycosaminoglycans (GAGs) of murine spleen and determine whether splenic lymphocytes carry cell surface receptors for these GAGs. A procedure was devised for isolating GAGs from murine spleen in good yield and high purity and the GAG preparation was then radiolabelled for subsequent binding studies. It was found that the splenic GAGs bound to murine splenocytes in a saturable, rapid and reversible manner with only a small subpopulation of the splenic GAG preparation being involved in binding. This reactive species was chondroitinase ABC-resistant and nitrous acid-sensitive, indicative of a heparan sulphate/heparin-like molecule. Furthermore, using immunofluorescent flow cytometry studies it was demonstrated that the majority of spleen cells have receptors for these GAGs. Subsequent ion-exchange fractionation and SDS-PAGE analysis of chondroitinase ABC-resistant GAGs confirmed that the splenic GAG recognized by splenocytes was a heparan sulphate/heparin molecule of approximately 20,000 MW with a binding affinity to splenocytes of approximately 5 X 10(-8) M. Additional binding inhibition studies indicated two possible binding sites for splenic GAGs on the splenocyte surface, one being fully inhibited by a range of SPS such as heparin (both coagulant and anticoagulant forms), pentosan sulphate, fucoidan, dextran sulphate, lambda- and iota-carrageenan, and the second being partially inhibited by kappa-carrageenan. The possible relevance of these heparan sulphate/heparin receptors on splenocytes to lymphocyte positioning in vivo is discussed.
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PMID:Receptors on lymphocytes for endogenous splenic glycosaminoglycans. 254 Oct 72

Three types (T1, T2, T3) of proteoglycan (PG) filaments, as demonstrated by cuprolinic blue (CB) under critical electrolyte concentration method in the epithelial-stromal interface of the guinea pig lateral prostate, were characterized cytochemically by using a number of glycosaminoglycan(GAG)-degrading enzymes and nitrous acid. The results showed that T1 filaments located in basement membranes of the epithelium, endothelium, and smooth muscle cells, were removed by nitrous acid, heparitinase, and pronase but resistant to chondroitinase (Ch)-ABC and Ch-AC, heparinase, neuraminidase, and Streptomyces (S) hyaluronidase. The T1 filaments, therefore, contain heparan sulfate. The T2 filaments closely linked to collagen fibrils were removed by Ch-ABC, Ch-ABC plus S-hyaluronidase, and pronase but were resistant to nitrous acid, heparitinase, heparinase, neuraminidase, and S-hyaluronidase. These show that T2 filaments are rich in dermatan sulfate. The T3 filaments in the interstitial spaces and on the surface of fibroblasts were removed by Ch-ABC, Ch-AC, and pronase but were resistant to heparitinase, heparinase, hyaluronidase, neuraminidase, and nitrous acid. They are, therefore, rich in chondroitin sulfate.
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PMID:Cytochemical characterization of cuprolinic blue-stained proteoglycans in the epithelial-stromal interface of the guinea pig lateral prostate. 271 Jun 91

Colon cancer cells in culture synthesize and secrete mucin glycoproteins, which carry a number of cancer-associated antigens. However, the structures and mechanisms of biosynthetic processing are not well understood. Mucins synthesized and secreted by LS174T human colon cancer cells were compared to those in LS174T xenografts in athymic mice. Mucins radiolabeled with glucosamine or sulfate were purified by gel filtration and cesium chloride density gradient centrifugation. The mucins were of high molecular weight and were resistant to chondroitinase ABC, hyaluronidase and HNO2 treatment. They were, however, susceptible to pronase digestion and mild alkaline treatment. Using radiochemical precursors, the cellular mucin was shown to contain fucose, galactose, N-acetylgalactosamine, N-acetylglucosamine, N-acetylneuraminic acid, and sulfate. Oligosaccharides released by beta-elimination had N-acetylgalactosaminitol as the reduced amino sugar and also unreduced galactosamine, indicating that there is N-acetyl-galactosamine O-glycosidically attached to protein core and also peripheral N-acetyl-galactosamine not directly linked to protein. DEAE-cellulose chromatography of mucins showed two major peaks with both intracellular and secreted mucins, but xenograft mucins also had more acidic components. Sulfate-labeled mucins were shifted to less acidic peaks by neuraminidase digestion, which indicates that the same mucin molecules are both sialylated and sulfated. We conclude that the intracellular mucins of cultured colon cancer cells, those secreted into the medium, and those in nude mouse xenografts are chemically similar, but differ in sialic acid and sulfate content. This experimental model system, LS174T cells maintained in culture and as nude mouse xenografts, may be useful for further biosynthetic and structural studies of colon cancer mucin.
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PMID:Comparison of metabolically labeled mucins of LS174T human colon cancer cells in tissue culture and xenograft. 273 49

The distribution of proteoglycans in the trabecular tissue of human eyes was evaluated histochemically, using Cupromeronic Blue in combination with a series of enzyme digestions and nitrous acid treatment. Within the extracellular matrix of the trabecular meshwork, many Cupromeronic Blue-positive filaments were observed in association with collagen fibrils, basal lamina, a basal lamina-like material and a fine fibrillar-like material. Pretreatment with chondroitinase AC reduced the staining associated with the collagen fibrils, whereas filament staining in this location was completely eliminated by pretreatment with chondroitinase ABC. Nitrous acid treatment eliminated almost all the filament staining associated with the basal lamina and basal lamina-like material. When the tissue was treated with chondroitinase AC, chondroitinase ABC or nitrous acid, filament staining associated with the fine fibrillar-like material was reduced. After a combined treatment with nitrous acid followed by incubation with chondroitinase ABC, all filament staining in the trabecular meshwork was eliminated. These results are consistent with an interpretation that human trabecular tissue contains three distinct types of sulfated proteoglycans, namely chondroitin sulfate, dermatan sulfate and heparan sulfate-type proteoglycans. Proteoglycans containing chondroitin sulfate and dermatan sulfate are present in association with collagen fibrils. Proteoglycans of heparan sulfate-type are associated with the basal lamina and the basal lamina-like material. Chondroitin sulfate, dermatan sulfate and heparan sulfate-type proteoglycans are present in association with the fine fibrillar-like component. The basal lamina, basal lamina-like material and fine fibrillar-like components associated with these negatively charged proteoglycans may be important contributors to aqueous outflow resistance in the juxtacanalicular connective tissue.
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PMID:Distribution and characterization of sulfated proteoglycans in the human trabecular tissue. 279 61

Two monoclonal antibodies, M32-1 (Ig-G1,k) and M39-2 (IgM,k), were prepared against high molecular weight (greater than 650 kDa) cytosol antigens (HMW-CA) of a human adenocarcinoma of the colon (GW-39). These monoclonal antibodies appeared to bind to determinants on two distinct high molecular weight colon antigens. One was shown by gel filtration to be a 650 kDa glycoprotein (gp650) containing at least one 300 kDa antigenic subunit (gp300). The other antigen eluted from a S-300 Sephacryl column at a molecular size of 600 kDa (gp600) and was resistant to dissociation by detergents, salts and chaotropic agents. The differential sensitivity of these two high molecular weight glycoproteins to treatment with trypsin, chondroitinase ABC, HNO2, endoglycosidase H and 2-mercaptoethanol suggest that monoclonal antibodies M39-1 and M39-2 react with distinct antigenic determinants located on two separate, high molecular weight, colon antigens. Since these antigens are only detected in extracts prepared from normal mucosa, well-differentiated tumors or margins of well-differentiated tumors, their expression appears to be related to a well-differentiated cell phenotype.
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PMID:Characterization of two monoclonal antibodies that recognize high molecular weight colon antigens. 292 Mar 72

67Ga uptake and heparan sulfate (HS) content were investigated during the recovery of mouse kidney from acute immune complex glomerulonephritis induced by daily injections of bovine serum, and the binding of 67Ga to glomerular basement membrane (GBM) was studied in vitro. The results were as follows. 67Ga uptake in the kidney increased after the start of bovine serum injection, and peaked on the 20th day. The uronic acid content in 1.2 M NaCl-soluble fraction (which contained predominantly HS) and the hydroxyproline content (an index of collagen) were increased at the 10th day, reaching a maximum at the 20th day. This pattern of HS content was essentially the same as that of 67Ga accumulation in the kidney. Urinary protein and gamma-GTP activity peaked at the 5th day, and these patterns were different from that of 67Ga uptake. 67Ga binding to GBM was significantly inhibited by treatments with HS-degrading enzyme (heparitinase), nitrous acid, trypsin or papain. However, the binding to GBM was unaffected by treatment with chondroitinase ABC. These results provide further evidence that the 67Ga-binding substance in tumor tissues and inflammatory lesions is probably HS.
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PMID:Renal gallium accumulation in mice with acute immune complex glomerulonephritis. 293 94

We have previously shown that asymmetric collagen-tailed acetylcholinesterase (AChE) is anchored to the extracellular matrix (ECM) by heparan sulfate proteoglycans (HSPGs). Here we present our studies on the characterization of such PGs from the ECM of rat skeletal muscles. After radiolabeling with 35SO4 for 24h, PGs were extracted from the muscle ECM with 4.0 M guanidine-HCl containing protease inhibitors. PGs were subsequently isolated using sequential DEAE-Sephacel chromatography, digestion with chondroitinase ABC, and Sepharose CL-4B. Two different hydrodynamic size species of HSPGs were found. One type had a Mr of 4-6 X 10(5) (Kav = 0.25) as estimated by gel chromatography in the presence of 1% SDS and accounted for 75% of the total HSPGs. The other HSPG had a Mr 1.5-2.5 X 10(5) (Kav = 0.41). The glycosaminoglycan (GAG) side chains (Mr 20,000 and 12,000) were found composed only of heparan sulfate as determined by nitrous acid oxidation and heparitinase treatment. The large-sized HSPG, which is concentrated in synaptic regions, contains only GAG chains of Mr 20,000, suggesting that each HSPG contains only one kind of heparan sulfate chain in its structure. Our results definitively establish by biochemical criteria that the basement membrane of mammalian skeletal muscle contains HSPGs, the likely matrix receptor for the immobilization of the asymmetric collagen-tailed AChE at the neuromuscular junction.
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PMID:Isolation of the heparan sulfate proteoglycans from the extracellular matrix of rat skeletal muscle. 295 79

At the early stage of atherogenesis, circulating monocyte macrophages appear to adhere to the endothelial cell surface and migrate subendothelially to become foam cells. The mechanism of these macrophage-endothelial cell interactions was investigated. Adherent macrophages isolated from human blood were plated on [35S]O4-prelabeled extracellular matrix-coated dishes prepared from cultured porcine aortic endothelial cells. During incubation for 2-3 days at pH 7.4 either in the presence or absence of serum, macrophages solubilized the labeled extracellular matrix to a lower molecular weight component (Kav approximately equal to 0.5) than the materials (Kav = 0) released into the medium containing no cells. The degrading activity was not stored intracellularly but instead was found pericellularly, requiring continuous cell-matrix contact. Heparin (10 micrograms/ml) inhibited this degrading activity of macrophages. Degradation products were precipitated with cetylpyridinium chloride and were resistant to further digestion with alkali, pronase, or chondroitinase ABC, but were converted to further lower molecular weight fragments (Kav = 0.84) after nitrous acid digestion or heparitinase treatment. The intact glycosaminoglycan side chains determined by subjecting the extracellular matrix to cleavage with alkali or pronase were larger (Kav congruent to 0.20) than those of degradation products released by macrophages. These results suggest that the attachment and subsequent invasion of endothelial cells by monocyte macrophages may involve the production of extracellular-matrix heparan sulfate proteoglycan-degrading activity by these cells.
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PMID:Subendothelial extracellular-matrix heparan sulfate proteoglycan-degrading activity of human monocyte macrophages. 296 81

Rats infected with the helminth Nippostrongylus brasiliensis were injected i.p. with 2 mCi of [35S] sulfate on days 13, 15, 17, and 19 after infection. The intestines were removed from animals on day 20 or 21 after infection, the intestinal cells were obtained by collagenase treatment and mechanical dispersion of the tissue, and the 35S-labeled mucosal mast cells (MMC) were enriched to 60 to 65% purity by Percoll centrifugation. The cell-associated 35S-labeled proteoglycans were extracted from the MMC-enriched cell preparation by the addition of detergent and 4 M guanidine HCl and were partially purified by density gradient centrifugation. The isolated proteoglycans were of approximately 150,000 m.w., were resistant to pronase degradation, and contained highly sulfated chondroitin sulfate side chains. Analysis by high-performance liquid chromatography of chondroitinase ABC-treated 35S-labeled proteoglycans from these rat MMC revealed that the chondroitin sulfate chains consisted predominantly of disaccharides with the disulfated di-B structure (IdUA-2SO4----GalNAc-4SO4) and disaccharides with the monosulfated A structure (G1cUA----GalNAc-4SO4). The ratio of disaccharides of the di-B to A structure ranged from 0.4 to 1.6 in three experiments. Small amounts of chondroitin sulfate E disaccharides (GlcUA----GalNAc-4,6-diSO4) were also detected in the chondroitinase ABC digests of the purified rat MMC proteoglycans, but no nitrous acid-susceptible heparin/heparan sulfate glycosaminoglycans were detected. The presence in normal mammalian cells of chondroitin sulfate proteoglycans that contain such a high percentage of the unusual disulfated di-B disaccharide has not been previously reported. The rat intestinal MMC proteoglycans are the first chondroitin sulfate proteoglycans that have been isolated from an enriched population of normal mast cells. They are homologous to the chondroitin sulfate-rich proteoglycans of the transformed rat basophilic leukemia-1 cell and the cultured interleukin 3-dependent mouse bone marrow-derived mast cell, in that these chondroitin sulfate proteoglycans as well as rat serosal mast cell heparin proteoglycans are all highly sulfated, protease-resistant proteoglycans.
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PMID:Intestinal mucosal mast cells from rats infected with Nippostrongylus brasiliensis contain protease-resistant chondroitin sulfate di-B proteoglycans. 308 52


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