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)

Histochemical localization of the estrogen-induced sulfated glycoproteins was made in the estrogen-treated rabbit uterus. Biochemical studies by a group of Endo et al, affirmed these particular glycoproteins were PAS-positive and metachromatic as stained with TB. No sign of digestion, however, has been detected in a series of tests with alpha-amylase, testicular hyaluronidase, streptomyces hyaluronidase, chondroitinase AC and chondroitinase ABC, and heparinase. The apical portions of the epithelial and glandular cells, obviously expanded by the estrogen treatment, display strong beta-metachromasia with TB (pH 4.0), saliva-resistant PAS-positive reactions, and also alcianophilia with AB (pH 2.5). These reactions are not reduced after the treatment with the enzymes above-mentioned. Meanwhile, in the stromal matrix, the same enzymes give an influence to diminish the reactions to various extent. Our results suggest that the estrogen-induced sulfated glycoprotein is definitely localized in the apical portions of the epithelial and glandular cells. The identity is emphasized between the substance that is elucidated in the histochemical sections and the sulfated glycoproteins that have been specified solely by means of biochemical assays.
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PMID:Histochemical localization of estrogen induced sulfated glycoprotein in rabbit uterus. 5 8

Micro-scale isolation of sulfated glycopeptide from tissue was achieved by successive application of pronase digestion (Step 1), cetylpyridinium chloride-fractionation (Step 2), crude heparinase digestion or chondroitinase ABC digestion plus nitrous acid treatment (Step 3) and preparative cellulose acetate membrane-electrophoresis (Step 4). By this method, sulfated glycopeptide was obtained in a high yield from estrogen-treated rabbit uterus.
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PMID:A method for micro-scale isolation of sulfated glycopeptide from tissue. 52 51

Acidic glycoconjugates (glycosaminoglycans and glycoprotein) were obtained, from myometrium of ovariectomized rabbit under estrogenic condition, by pronase digestion, fractionation with cetylpyridinium chloride and Dowex I column chromatography, in succession. Composition of acidic glycoconjugates was determined enzymatically, employing Streptomyces hyaluronidase, chondroitinase AC II, chondroitinase ABC and crude heparinase. Each glycoconjugate was distributed in 3 approximately 8 fractions obtained by Dowex I column chromatography, indicating its charge and/or molecular heterogeneity. Acidic glycoconjugates consisted of hyaluronic acid (13.4%), chondroitin sulfates A plus C (39.4%), dermatan sulfate (24.6%), heparan sulfate (18.7%) and acidic glycoprotein (most probably sialoglycoprotein) (3.9%). Composition of acidic glycoconjugates in myometrium differed remarkably from that in whole uterus. Myometrium was abundant in chondroitin sulfate isomers (chondroitin sulfates A plus C plus dermatan sulfate), but lacked sulfated glycoprotein. The present results suggested that myometrium and endometrium of uterus may play quite different roles in reproduction.
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PMID:Composition of acidic glycoconjugates (glycosaminoglycans and glycoprotein) in myometrium of rabbit uterus under estrogenic condition. 71 60

An inhibitory component that diminishes estrogen receptor (ER) binding to nuclei in vitro is present in cytosol prepared from calf uterus. The inhibitor is heat stable and resistant to enzymatic treatment with trypsin, chymotrypsin, proteinase K, deoxyribonuclease I, or ribonucleases A, T1, and U2. Results of chromatography on DEAE-cellulose and Sephadex G-150 indicate that the factor is a negatively charged macromolecule. Inhibitory activity is sensitive to sequential digestion with chondroitinase ABC, hyaluronidase, and heparinase. Approximately 70% of the inhibitory activity is destroyed by treatment with heparinase alone. Heparitinase destroys only 30% of this activity. Furthermore, the addition of pure hyaluronic acid or chondroitin sulfate to the ER-nuclei binding assay results in little inhibition, whereas addition of heparin inhibits 75% of receptor binding. Overall, these results indicate that glycosaminoglycans, present in bovine uterine cytosol, are capable of inhibiting ER-nuclei interactions. The most potent inhibitory glycosaminoglycan displays heparin-like characteristics.
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PMID:Characterization of a cytosolic inhibitor of calf estrogen receptor binding to nuclei. 330 79

Of the four known tissue inhibitors of metalloproteinases (TIMPs), TIMP-3 is distinguished by its tighter binding to the extracellular matrix. The present results show that glycosaminoglycans such as heparin, heparan sulfate, chondroitin sulfates A, B, and C, and sulfated compounds such as suramin and pentosan efficiently extract TIMP-3 from the postpartum rat uterus. Enzymatic treatment by heparinase III or chondroitinase ABC also releases TIMP-3, but neither one alone gives complete release. Confocal microscopy shows colocalization of heparan sulfate and TIMP-3 in the endometrium subjacent to the lumen of the uterus. Immunostaining of TIMP-3 is lost upon digestion of tissue sections with heparinase III and chondroitinase ABC. The N-terminal domain of human TIMP-3 was expressed and found to bind to heparin with affinity similar to that of full-length mouse TIMP-3. The A and B beta-strands of the N-terminal domain of TIMP-3 contain two potential heparin-binding sequences rich in lysine and arginine; these strands should form a double track on the outer surface of TIMP-3. Synthetic peptides corresponding to segments of these two strands compete for heparin in the DNase II binding assay. TIMP-3 binding may be important for the cellular regulation of activity of the matrix metalloproteinases.
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PMID:TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. 1090 Jan 94