Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ruthenium red was used to stain microfibrils in rat aorta after incubation of the tissues with or without one of the enzymes trypsin, collagenase, phospholipase C, chondroitinase ABC, hyaluronidase or neuraminidase, or the reducing agent dithiothreitol. Microfibrils exhibiting periodicity of ruthenium red binding were associated with elastic laminae and collagen fibrils and appeared to attach these structures to each other as well as to basal lamina. Microfibrils in rat and human aorta demonstrated fibronectinlike immunoreactivity, therefore fibronectin may be a component of aorta microfibrils and important in the architecture of blood vessels.
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PMID:Microfibrils in the aorta. 622 39

In order to elucidate the close relationship between the formation of fibrous long spacing fibers (FLS) and collagenase activity, electron microscopic studies on the rat skin using tissue culture technique were performed. In culture of newborn rat skin, a large number of FLS was formed in the dermis in which activity of endogenous collagenase was markedly elevated. Ethylenediaminetetraacetic acid (EDTA) supplemented to the culture medium completely arrested the formation of the FLS; subsequent exposure to bacterial collagenase resulted in the appearance of FLS in the same fashion. In another set of experiments utilizing exogenous enzyme digestion with bacterial collagenase or chondroitinase ABC on skins of 1-day-old and 1-year-old rats, it was demonstrated that the FLS formed by incubation with bacterial collagenase were found only in the regions of the dermis where reticular fibers were identified by light microscopy. There was no effect of chondroitinase ABC on FLS formation. These studies indicate that the FLS are formed in the presence of elevated endogenous collagenase and might be derived from reticular fibers which are degraded by collagenase.
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PMID:The effect of collagenase on the formation of fibrous long spacing collagen aggregates. 625 71

The effect of streptozotocin-induced diabetes on the glycosaminoglycan composition of rat renal cortical tissue was evaluated. Glycosaminoglycans were isolated and purified from the kidney cortex of control and diabetic rats by means of digestion with collagenase, pronase and ethanol precipitation. Subsequent fractionation was performed by ion exchange chromatography on Dowex 1-X2 Cl using various concentrations of sodium chloride solution. The glycosaminoglycan in each fraction was characterized by digestion with hyaluronidase, chondroitinase AC and ABC. The undigested glycosaminoglycans were separated after each enzyme digestion and quantitated. The glycosaminoglycan composition of each fraction was computed from the enzyme digestion profile. The results indicate that in renal cortex of streptozotocin induced diabetic rats there was a significant reduction in the levels of dermatan sulfate, heparan sulfate and hyaluronic acid, while the chondroitin sulfate remained unaffected. In light of this finding, the significance of these anionic polysaccharides in renal functions is discussed.
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PMID:Alterations in the rat renal glycosaminoglycans in streptozotocin-induced diabetes. 660 Sep 34

Age-related changes in renal function have been attributed to alterations in the chemical composition of the kidney tissues. Hence, the glycosaminoglycan composition of the renal cortex and medulla at varying age intervals was investigated. Glycosaminoglycans were isolated from the tissues by means of digestion with collagenase and pronase and purified by ethanol precipitation. Subsequent separation of various polyanions was accomplished by ion exchange chromatography on a Dowex 1-X2 column, using sodium chloride buffers of increasing ionic strengths. The glycosaminoglycans in each fraction were identified and quantitated by digestion with specific enzymes, including hyaluronidase, chondroitinase AC and ABC. The enzyme resistant material was separated and further digested with nitrous acid to quantitate the proportion of heparon sulfate. The results indicate that the glycosaminoglycan content of the renal medulla was much higher than the cortex at all the age intervals studied, and age-induced reduction was mainly cortical. There was a significant reduction in the heparan sulfate content of the cortex in aging. Interestingly, the major glycosaminoglycan content of the medulla was hyaluronic acid, which showed a sharp increase during aging, whereas heparan sulfate declined. Chondroitin sulfate was not altered due to age in either tissue. The molecular weight of hyaluronic acid was determined by column chromatography. Results indicate that the size of hyaluronate in the cortex was small and did not vary with age. In the medulla of the younger age group, a considerable amount of large size hyaluronate was observed. As age increased, the size decreased. The results strongly suggest that alteration in the renal glycosaminoglycans may be partly responsible for the age related protinuria and ionic imbalance.
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PMID:Alterations of renal cortex and medullary glycosaminoglycans in aging dog kidney. 662 71

Corneal epithelial cells from 15-day chick embryos produce a fibronectin-rich extracellular matrix when cultured on glass, plastic and fibronectin-coated substrata. Cell culture in the presence of Streptomyces hyaluronidase or chondroitinase ABC resulted in considerable reduction of the matrix; collagenase had a lesser effect but nevertheless also reduced the matrix. In all enzyme treatments the cells attached and spread to form characteristic epithelial cell islands, but the marginal cells of these islands showed a marked reduction in the number of lamellipodia and focal contacts. Also, the immunofluorescent staining pattern for fibronectin was considerably reduced. Control cells cultured on a fibronectin-coated surface were able to reorganize the fibronectin into fibrils, whereas cells cultured in enzymes showed little or no ability to do so. The cellular reorganization of fibronectin could also be inhibited by the addition of L-azetidine-2-carboxylic acid (LACA), an inhibitor of collagen secretion. Cells plated out in the presence of LACA spread much better on collagen substrata than on plastic, glass or fibronectin. However, in all cases very little fibronectin matrix was detectable in the epithelial islands. The results suggest that components of the extracellular matrix (ECM) such as collagen, hyaluronic acid and chondroitin sulphates are not essential for the initial attachment and spreading of corneal epithelial cells in culture, but are important in the development of the ECM, and in maintaining a flattened morphology and spreading behaviour. It is suggested that fibronectin plays an important role in these interactions and that the ability of cells to organize fibronectin into fibrils is dependent on the presence of other ECM components such as glycosaminoglycans and collagen.
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PMID:Role of glycosaminoglycans and collagen in the development of a fibronectin-rich extracellular matrix in cultured embryonic corneal epithelial cells. 674 72

Wharton's jelly of human umbilical cord is known to contain hyaluronic acid and sulphated glycosaminoglycans (probably as proteoglycans) immobilized in an insoluble collagen fibril network. A secondary, independent, insoluble network based on glycoprotein microfibrils of 13 nm diameter and interpenetrated with the collagen network has now been found in amounts corresponding to 9% of the weight of collagen. Elastin, however, is absent. Tissue slices placed in physiological buffer swell to two-fold their in vivo volume. This is due to the influence of the polysaccharides since treatment with either testicular hyaluronidase, Streptomyces hyaluronidase or chondroitinase ABC, causes their quantitative removal and abolishes the swelling tendency of tissue. Tissue so treated remains close to its in vivo volume indicating that for this state the fibrillar network, overall, is in its relaxed unstressed configuration. Subsequent treatment with a protease causes the degradation of the glycoprotein microfibril network and a two-fold increase in tissue volume while treatment with bacterial collagenase, resulting in the solubilization of 46% of the collagen, causes only a slight deswelling. These results suggest that the unstressed configuration of the network system at the in vivo volume of tissue is due to the collagen network being held in compression by the microfibril network. With intact tissue protease digestion with trypsin, in addition, causes a preferential release of sulphated glycosaminoglycans. Hyaluronic acid, however, remains largely immobilized.
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PMID:Evidence for a mechanical coupling of glycoprotein microfibrils with collagen fibrils in Wharton's jelly. 682 35

Chick embryo epiphyseal cartilage has been shown to contain three different proteoglycan species (PG-H, PG-Lb, and PG-Lt). This report is concerned with the purification and characterization of the third proteoglycan, PG-Lt. The proteoglycan can be separated from the other two by virtue of its low buoyant density in a CsCl density gradient and further purified by consecutive ion exchange and gel chromatography. The final preparation is composed of PG-Lt monomer and PG-Lt oligomer. The amino acid composition of PG-Lt is quite different from that of PG-H and PG-Lb and rather resembles that of collagens with respect to high content of glycine and high degrees of hydroxylation of proline and lysine. PG-Lt monomer is composed of disulfide-bonded subunits of Mr congruent to 120,000 and 190,000 as demonstrated by its gel electrophoretic behavior after reduction with 2-mercaptoethanol. The latter, but not the former, contains dermatan sulfate chains with glucuronic acid/iduronic acid residues and yields a protein-enriched core molecule of Mr congruent to 100,000 after digestion with chondroitinase ABC. Both of the protein subunits are completely digestible with bacterial collagenase. Immunofluorescence microscopic examination of cartilage tissues, using an antibody against PG-Lt, shows that this proteoglycan exists in both the cartilage matrix and perichondrial noncartilagenous region. When chondrocytes are plated onto tissue culture dishes, the antibody stains strands found on the cell surfaces and in the intercellular space of substrate-attached cell layers, suggesting that PG-Lt mediates cell-to-cell and cell-to-substrate contacts.
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PMID:Isolation and characterization of a third proteoglycan (PG-Lt) from chick embryo cartilage which contains disulfide-bonded collagenous polypeptide. 687 91

The viscoelastic properties of culture medium obtained from confluent 3T3-L1 preadipocytes, after differentiation with isobutyl-methylxanthine and dexamethasone, were studied with a rotational Couette viscometer. In close association with adipocyte differentiation, the culture medium showed gel-like properties, in concert with an increase in viscosity. This behavior vanishes after digestion by Streptomyces hyaluronidase or chondroitinase ABC, but not after application of collagenase, pronase, trypsin, DNase, or neuraminidase, or by treatment with EDTA or mercaptoethanol, indicating that the primary substance responsible for this behavior is hyaluronic acid. The material revealed a non-Newtonian behavior with an irreversible disruption of the network by shear force at high speeds. The viscosity of the medium, containing about 1 microgram/ml of hyaluronic acid, was calculated to be similar to that of a solution containing 1.7 mg high molecular weight hyaluronic acid per milliliter of stock culture medium. The comparison of rheological properties between the culture medium and solutions of hyaluronic acid indicated the possibility of a highly organized network in the culture medium that is more complicated than a simple interaction between homologous hyaluronic acid molecules. The non-Newtonian behavior depends on the hyaluronic acid concentration in the medium as well as on the length of exposure of the 3T3-L1 cells to the isobutyl-methylxanthine/dexamethasone mixture. The results point toward the possibility of interaction between hyaluronic acid and binding proteins.
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PMID:Rheological effects of the presence of hyaluronic acid in the extracellular media of differentiated 3T3-L1 preadipocyte cultures. 768 59

The molecular specificity of the dental papilla of a bell-stage tooth was studied by production of dental-papilla-reactive monoclonal antibodies (Mabs). One of the Mabs, designated 7C5, recognized an epitope present in glycosaminoglycan. Several lines of evidence suggested that the 7C5-epitope consists of chondroitin 6-sulfate. The Mab did not react with mouse dental epithelium, but reacted uniformly with mesenchymal tissue in the mandibular process and accumulated in the dental sac and in the papilla of bell-stage tooth germs. The 7C5-staining was lost from the differentiating odontoblasts, while the staining in the molar tooth papilla was accumulated in the subodontoblastic layer. In the developing mouse incisor, the 7C5-epitope was restricted to the lingual-posterior area. The 7C5-epitope was also present in pulpal tissue and predentin of different types of teeth of various mammalian species, including man, sheep, swine, and rat. Collagenase pre-treatment of tissue sections abolished the bulk of the 7C5-reactivity in peridental mesenchyme during embryonic stages while leaving the staining of the dental papilla intact. In newborn and adult teeth, collagenase also impaired the reactivity in the pulp except for the subodontoblastic layer. This suggests the existence of different subpopulations of the 7C5-epitope containing proteoglycans in dental papilla and pulp. A high-molecular-weight proteoglycan, sensitive to chondroitinase ABC but not to heparinase or heparitinase, was immunoprecipitated by 7C5 from extracts of bell-stage mouse tooth germs. We suggest that the evolutionary conservation of chondroitin 6-sulfate in the dental pulp reflects its properties as non-terminally differentiated tissue and perhaps the retention of a potential to differentiate to odontoblasts.
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PMID:A chondroitin sulfate epitope in mammalian dental pulp and its developmental expression in mouse dental papilla. 769 81

Different proteoglycan (PG) populations were isolated from normal human aorta by extraction of minced tissue with 4M GuHCl and by further digestion of the residue with collagenase. Dissociative extraction induced a complete disappearance of Alcian Blue positive material, which was demonstrable by transmission electron microscopy before the treatment around collagen fibrils and in pericellular areas. However, 4M GuHCl extraction solubilized only an average of 60% of aorta total hexuronate content. Collagenase treatment of the residue resulted in a complete loss of collagen fibril organization, which was coupled with a further hexuronate recovery, accounting for about one third of total tissue content. The bulk of PGs obtained in collagenase digest was retained by Sepharose CL-4B column. Their sulphated glycosaminoglycan (GAG) composition differed from PGs extracted with 4M GuHCl, containing only chondroitin sulphate (CS) and heparan sulphate (HS), without detectable traces of dermatan sulphate (DS). Moreover, they contained hyaluronic acid. The results obtained by agarose polyacrylamide gel electrophoresis (APGE) and Octyl-Sepharose chromatography, followed by further APGE and Sepharose CL-4B gel-filtration, carried out before and after treatment with Chondroitinase ABC and AC and Heparinase I and III, suggested that collagenase digest contained different PG populations, carrying mainly either CS or HS chains. Moreover, HS containing PGs showed higher hydrodynamic size and stronger properties of hydrophobic interactions than CS containing PGs.
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PMID:Collagenase-extractable proteoglycans from lesion-free areas of human aorta. 820 40


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