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)

Chick embryonic skeletal muscle synthesizes three major types of proteoglycans: large chondroitin sulfate proteoglycans, small dermatan sulfate proteoglycans and small heparan sulfate proteoglycans. A monoclonal antibody has been raised which recognizes the small dermatan sulfate proteoglycan. Immunoblot analysis of a partially purified preparation of skeletal muscle proteoglycans indicates that the antibody reacts with a molecule which migrates with an estimated Mr of 100,000. Prior treatment of the proteoglycans with chondroitinase results in immunostaining of a species of estimated Mr 45,000. These values for the intact proteoglycan and its core protein suggest that the antibody is directed against a proteoglycan of the PG-II or decorin class. Immunohistochemistry indicates a widespread distribution of the proteoglycan, which is localized in connective tissue septa of skeletal and cardiac muscle, dermis, tendon, bone, perichondrium and cornea. Immunoblot analysis of the proteoglycan core proteins from these tissues demonstrates that the antibody recognizes the same 45,000-dalton band in each tissue. The widespread tissue distribution is also consistent with the antibody being directed against an epitope of PG-II. Neither the glycosaminoglycan chains nor N-linked oligosaccharides are required for reactivity and the antibody cross-reacts with other avian material, but not mammalian. This antibody, which has been designated CB-1, reveals developmental stage-specific changes in the deposition of PG-II in embryonic limb bud and skeletal muscle.
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PMID:Generation of a monoclonal antibody against avian small dermatan sulfate proteoglycan: immunolocalization and tissue distribution of PG-II (decorin) in embryonic tissues. 178 33

The major proteoglycan in bovine parietal pericardium is a low molecular weight dermatan-sulfate proteoglycan. It possesses structural and immunologic characteristics similar to those of the small proteoglycan found in tendon. We demonstrate that digestion of purified pericardial proteoglycan with low levels of V8 protease results in the liberation of the glycosaminoglycan chain and of a 40 kDa resistant fragment. A similar 40 kDa fragment can be obtained by V8 protease digestion of the proteoglycan deglycosylated by chondroitinase ABC. Although the protein core size of the pericardial proteoglycan is similar to that of tendon PG II, the size of the glycosaminoglycan chain liberated from the former is smaller. The pericardial proteoglycan and its V8 protease products reacted with an anti-PG II antiserum by immunoblotting. The anti-PG-II antibody localized in the pericardial tissue by the immunoperoxidase technique. The presence of intrachain disulfide bonds in the structure of pericardial proteoglycan core protein and V8 resistant fragment was demonstrated by their decreased electrophoretic mobility after disulfide reduction. Digestion of pericardial proteoglycan with Cathepsin C resulted in a rapid liberation of the glycosaminoglycan chain from the core protein, indicating that its attachment site was very close to the amino terminus. Ultrastructural examination of pericardial tissue utilizing Cuprolinic Blue revealed a periodic association of the proteoglycan with the d/e band on the collagen fibrils. Electron microscopic immunohistochemical studies confirmed the perifibrillar association of pericardial proteoglycan. The present data demonstrate that, although the pericardial proteoglycan possesses some unique structural features, it shares structural and immunological characteristics to place it in the category of the small PG II family.
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PMID:Bovine pericardial proteoglycan: biochemical, immunochemical and ultrastructural studies. 267 26

Low molecular mass proteoglycans (PG) were isolated from human articular cartilage and from pig laryngeal cartilage, which contained protein cores of similar size (Mr 40-44 kDa). However, the PG from human articular cartilage contained dermatan sulphate (DS) chains (50% chondroitinase AC resistant), whereas chains from pig laryngeal PG were longer and contained only chondroitin sulphate (CS). Disaccharide analysis after chondroitinase ABC digestion showed that the human DS-PG contained more 6-sulphated residues (34%) than the pig CS-PG (6%) and both contained fewer 6-sulphated residues than the corresponding high Mr aggregating CS-PGs from these tissues (86% and 20% from human and pig respectively). Cross-reaction of both proteoglycans with antibodies to bovine bone and skin DS-PG-II and human fibroblasts DS-PG suggested that the isolated proteoglycans were the humans DS-PG-II and pigs CS-PG-II homologues of the cloned and sequenced bovine proteoglycan. Polyclonal antibodies raised against the pig CS-PG-II were shown to cross-react with human DS-PG-II. SDS/polyacrylamide-gel analysis and immunoblotting of pig and human cartilage extracts showed that some free core protein was present in the tissues in addition to the intact proteoglycan. The antibodies were used in a competitive radioimmunoassay to determine the content of this low Mr proteoglycan in human cartilage extracts. Analysis of samples from 5-80 year-old humans showed highest content (approximately 4 mg/g wet wt.) in those from 15-25 year-olds and lower content (approximately 1 mg/g wet wt.) in older tissue (greater than 55 years). These changes in content may be related to the deposition and maintenance of the collagen fibre network with which this class of small proteoglycan has been shown to interact.
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PMID:Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage. 319 90