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 nature of Cuprolinic Blue-positive anionic filaments in mouse lung alveoli has been characterized. The contrast of filaments in the alveolar basement membrane of type I epithelial cells was lost on treatment with nitrous acid and pronase (without prefixation). In contrast, neither neuraminidase, chondroitinase ABC or AC, nor Streptomyces hyaluronidase had any effect. Treatment with pronase (after prefixation) and 2.0 M MgCl2 (after prefixation) also had no effect, indicating that the filaments are heparan sulphate proteoglycans. The filaments in the alveolar basement membrane of type II epithelial cells and in the capillary basement membrane of the endothelial cells were also nitrous acid sensitive, but chondroitinase ABC-insensitive. A model in which the whole alveolus contains a single layer of heparan sulphate-containing proteoglycan monomers is proposed. Furthermore, the collagen fibril associated filaments remained unaffected after treatment with nitrous acid, neuraminidase or Streptomyces hyaluronidase, or after digestion with pronase (after prefixation) and treatment with 2.0 M MgCl2 (after prefixation). These filaments, however, could no longer be detected when digestion with chondroitinase ABC or pronase (without prefixation) was applied; chondroitinase AC treatment clearly affected the filaments, although they still were visible. These results indicate that the filaments are dermatan sulphate-containing proteoglycans. Some functional aspects of the proteoglycans are discussed.
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PMID:Staining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic blue-positive, anionic sites. 620 77

Proteoglycans were studied in articular cartilage of human femoral condyles. On the basis of the histochemical data obtained by means of light microscopy (AB + CEC MgCl2; pre-incubation with hyaluronidase or with chondroitinase ABC), the proteoglycan concentration as well as the keratan sulfate-chondroitin sulfate ratio seemed to increase proportionally to the articular cartilage depth. AB-proteoglycan particles of various shapes (filament-like or leaf-like) and sizes (10 nm or 16-18 nm), depending on the articular cartilage depth and on the histochemical conditions (as above), were visualized in thin sections. Similar heterogeneity of elongated non-collagen particles was shown in replicas of fresh freeze-fractured and deep-etched specimens. An interpretation of the distribution and nature of articular cartilage proteoglycans was made by comparing the obtained morphological findings.
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PMID:Heterogeneity of proteoglycan particles in thin sections and replicas of human articular cartilage. 624 53

The levels of metalloproteinases and metalloproteinase inhibitors were measured in rheumatoid synovial fluid. Reliable estimates of total enzyme and inhibitor levels in the synovial fluids were obtained only after hyaluronidase treatment and gel filtration. Three latent metalloproteinases were found which, after activation, degraded collagen, proteoglycan, and gelatin. These enzymes closely resembled the metalloproteinases secreted into connective tissue culture medium. In addition to alpha 2 macroglobulin, an Mr 30,000 collagenase inhibitor was detected which closely resembled the tissue inhibitor of metalloproteinase found in tissue culture medium.
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PMID:Metalloproteinases and collagenase inhibitors in rheumatoid synovial fluid. 632 10

Proteoglycans and glyco(link)proteins are demonstrated in the cartilage matrix using immunohistochemical reactions, ruthenium red staining and concanavalin A-peroxidase procedure. Specific antibodies against proteoglycan monomers revealed a loose matrix structure in the interterritorial area of nasal cartilage. Thin filaments of 49-87 nm in length with a knob on one end corresponding to the protein core of proteoglycan monomers were found in irregular contacts with collagen fibres. Following hyaluronidase digestion the immunohistochemical reactions became more intense, and the matrix structure is suggestive of a network of single filaments which are presumably coupled together longitudinally at the sites of small matrix granules. These matrix granules proved to be glyco(link)proteins of proteoglycan aggregate. Immunohistochemical reactions combined with other methods can reveal an in situ structure of proteoglycan aggregate of hyaline cartilage, which contributes substantially to what has been known about the proteoglycan aggregates on the basis of physico-chemical data and has been verified in monomolecular electron microscopic specimens. The enzymatic treatments of cartilage slices suggest that some of the partially digested proteoglycan monomers are required to be present for the preservation of the structural integrity of cartilage tissue.
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PMID:Localization of antigenic components in proteoglycan aggregate of bovine nasal cartilage. 634 27

Collagens type I, II, III, IV, and V and the minor cartilage collagens, 1 alpha 2 alpha 3 alpha, C-PS 1, and C-PS 2, were purified, antibodies raised, and then used in immunofluorescence studies on bovine nasal cartilage (BNC). Punctate localisation was seen with the type II antibody. However, pretreatment of sections with hyaluronidase to remove the proteoglycan resulted in diffuse staining over all the section with this antibody. Antibodies to 1 alpha 2 alpha 3 alpha, C-PS 1, and C-PS 2 collagens gave no staining on untreated BNC sections, but after treatment with hyaluronidase all 3 antibodies showed as a diffuse 'halo' round each chondrocyte lacuna. Anti-type I, anti-type III, and anti-type IV collagen antibodies did not stain untreated or enzyme treated BNC. Type V collagen antibodies gave a bright ring in the pericellular region of the lacunae of hyaluronidase-treated BNC. This was unexpected, as we could not detect type V collagen biochemically in the same cartilage. Anti-fibronectin antibodies stained areas distant from the chondrocytes, these areas being distinct from those stained by 1 alpha 2 alpha 3 alpha and C-PS antibodies, suggesting that fibronectin is not associated with these collagens in BNC. These results suggest that different collagen types may have different locations within the cartilage matrix, that proteoglycans may inhibit antibody association with collagen, and that fibronectin is normally not associated with all types of collagen.
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PMID:Localisation of collagen types and fibronectin in cartilage by immunofluorescence. 635 12

Types I, III and V collagens and proteoglycan were localized in the aorta by indirect immunofluorescence techniques. Type I collagen was more prominent in media and adventitia than in intima while type III collagen predominated in intima and media but appeared less significant in adventitia. Type V collagen was observed in intima and media only and was seen surrounding smooth muscle cells. Type I collagen was located between elastic fibres but type III collagen appeared to envelop the fibres, suggesting an interaction between elastic fibres and type III collagen. Pretreatment of sections with testicular hyaluronidase caused no changes in staining for type I collagen, but adventitial areas showed increased staining for type III collagen. After digestion with chondroitinase ABC, intimal and medial areas showed increased staining for type III collagen. Therefore, type III collagen forms stronger interactions with proteoglycans and hyaluronic acid than does type I collagen and type III collagen in adventitia is largely masked by hyaluronic acid, while type III collagen in intima and media is associated with proteoglycan. Thus, type III collagen is a more significant component of adventitia than previously recognized. Proteoglycan was also partly localized along elastic fibres. It is, therefore, suggested that elastic fibres are coated with type III collagen, which itself is coated with proteoglycan.
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PMID:Investigation of relationships between collagens, elastin and proteoglycans in bovine thoracic aorta by immunofluorescence techniques. 635 43

The effects of polymethylmethacrylate (PMMA) on DNA, protein, and sulfated-proteoglycan synthesis by rabbit articular chondrocytes were observed in monolayer cultures. PMMA pellets in ratios of 1:1 and 1:2 (liquid monomer:powder) significantly reduced [3H]thymidine incorporation into DNA during the first 24 h of culture and less so after 48 and 72 h. The reduction in [3H]thymidine incorporation was restricted to the cohort of chondrocytes nearest the PMMA. Consequently, cellular proliferation was unaltered by PMMA. By contrast, PMMA failed to inhibit [3H]leucine or [3H]serine/35SO4 incorporation. Both control and PMMA (1:1)-treated chondrocyte CsCl density gradient medium fraction dA1 eluted as a retarded peak on Sepharose CL-2B under associative conditions. The average partition coefficient (Kav) of PMMA-treated fraction dA1 was 0.41, as compared with 0.27 for control cultures. The Kav of medium fraction dD1 (proteoglycan monomer) was unaltered. Both control and PMMA-treated dA1 fraction elution profiles on Sepharose CL-2B were altered by incubation with Streptomyces hyaluronidase, indicating the presence of proteoglycan aggregate. The PMMA-treated cultures synthesized smaller proteoglycan aggregates. Since PMMA has been a critical factor in the success of total joint arthroplasty, defining interactions of differentiated cells with the cement is imperative for an understanding of the effects of PMMA on the biology of cartilage and bone.
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PMID:Effects of polymethylmethacrylate on rabbit articular chondrocytes in monolayer culture. 638 80

A high-performance liquid chromatography method for analyzing disaccharides derived from chondroitin sulfate glycosaminoglycans has been developed which employs a Whatman Partisil-10 PAC amino-cyano column and an acetonitrile/methanol/ammonium acetate solvent to resolve disulfated, monosulfated, and unsulfated disaccharides in a chromatographic run of less than 20 min. The single known trisulfated chrondroitin disaccharide can be eluted in an alternate solvent system containing the same mobile phase components in different proportions. Disaccharides were prepared for chromatography from glycosaminoglycans and proteoglycans of known compositions by digestion with chondroitinase ABC, with the exception of king crab cartilage glycosaminoglycan which was incubated sequentially with hyaluronidase and chondroitinase ABC. Disaccharides were extracted from the digestion mixtures in 80% ethanol, dried over nitrogen, resuspended in the HPLC solvent, and chromatographed at a flow rate of 1 ml/min. Unsaturated disaccharides in the column eluate were detected by continuous ultraviolet absorbance monitoring at 232 nm; alternatively, fractions were collected and assayed for uronic acid content or radioactivity. By utilizing the HPLC technique in conjunction with chondroitinase ABC and AC digestion and sulfatase hydrolysis, the epimeric structures of chondroitin sulfates E and H were confirmed. With this technique, rapid and reproducible analyses of chondroitin sulfate disaccharides generated from mouse mast cell proteoglycan and from glycosaminoglycans of squid cranial cartilage, shark skin, hagfish skin, and hagfish notocord were in close agreement with compositions obtained by other techniques.
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PMID:Analysis of polysulfated chondroitin disaccharides by high-performance liquid chromatography. 643 72

Degradation of cartilage matrix was studied by characterizing the size and amount of products released from cultures of fetal rat long bones into the medium. Na32SO4 was administered to pregnant rats and the fetal radii and ulnae were explanted 24 hours later and cultured in chemically defined medium. Under these conditions, 35S-activity is released from the cartilagenous ends of the explants into the culture medium gradually over 72 hours. The 35S-labeled molecules in the medium were smaller than proteoglycan monomers and larger than papain-released products when chromatographed on Sepharose 2B. The amount of 35S-activity released into the medium decreased when heat-inactivated rat serum or plasma or heparin was added to the medium. Adding proteases or hyaluronidases or freeze-thawing the tissue enhanced release of 35S-activity. Streptomyces hyaluronidase was chromatographed on CM-cellulose and Ultrogel to remove protease activity. The protease-free enzyme released 35S-labeled molecules, similar in size to proteoglycan monomers, from cartilage which was heated before culturing to inactivate endogenous enzymes. These results indicate that hyaluronidase can degrade matrix by releasing proteoglycan monomers. Other treatments released smaller 35S-labeled molecules. These findings indicate that endogenous enzymes degrade matrix proteoglycans into smaller units.
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PMID:Degradation of fetal rat cartilage in organ culture: effect of Streptomyces hyaluronidase. 644 66

Chondrocytes produce large pericellular coats in vitro that can be visualized by the exclusion of particles, e.g., fixed erythrocytes, and that are removed by treatment with Streptomyces hyaluronidase, which is specific for hyaluronate. In this study, we examined the kinetics of formation of these coats and the relationship of hyaluronate and proteoglycan to coat structure. Chondrocytes were isolated from chick tibia cartilage by collagenase-trypsin digestion and were characterized by their morphology and by their synthesis of both type II collagen and high molecular weight proteoglycans. The degree of spreading of the chondrocytes and the size of the coats were quantitated at various times subsequent to seeding by tracing phase-contrast photomicrographs of the cultures. After seeding, the chondrocytes attached themselves to the tissue culture dish and exhibited coats within 4 h. The coats reached a maximum size after 3-4 d and subsequently decreased over the next 2-3 d. Subcultured chondrocytes produced a large coat only if passaged before 4 d. Both primary and first passage cells, with or without coats, produced type II collagen but not type I collagen as determined by enzyme-linked immunosorbent assay. Treatment with Streptomyces hyaluronidase (1.0 mU/ml, 15 min), which completely removed the coat, released 58% of the chondroitin sulfate but only 9% of the proteins associated with the cell surface. The proteins released by hyaluronidase were not digestible by bacterial collagenase. Monensin and cycloheximide (0.01-10 microM, 48 h) caused a dose-dependent decrease in coat size that was linearly correlated to synthesis of cell surface hyaluronate (r = 0.98) but not chondroitin sulfate (r = 0.2). We conclude that the coat surrounding chondrocytes is dependent on hyaluronate for its structure and that hyaluronate retains a large proportion of the proteoglycan in the coat.
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PMID:Pericellular coat of chick embryo chondrocytes: structural role of hyaluronate. 650 14


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