Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Media of pig aorta was extracted with 1 M NaCl and 2 M MgCl2 to remove most of the soluble collagen, proteoglycans and glycoproteins. The glycoproteins remaining in the residue were extracted with 6 M urea-0.1 M mercaptoethanol. The urea soluble proteins were precipitated by dialysis, redissolved in 4 M guanidine-0.05 M DTT and were S-carboxamidomethylated (CM-guanidine extract). This extract was further fractionated by a variety of methods in order to separate a glycoprotein from collagen and proteoglycans. Caesium chloride density-gradient ultracentrifugation of the CM-guanidine extract separated a minor proteoglycan peak from a major glycoprotein fraction still containing some hydroxyproline. This major glycoprotein fraction was excluded as a single peak from Sephadex G 100 and G 200 in 4 M guanidinium chloride or in 6 M urea-0.2 per cent SDS. Sodium dodecylsulphate gel electrophoresis separated this high molecular weight Sephadex fraction into a major low molecular weight (approximately 35000 daltons) component and a minor high molecular weight component. This glycoprotein fraction could also be separated from a collagenous fraction and from proteoglycans by ion exchange chromatography on DEAE cellulose or by gelfiltration on Sepharose 4 B in 6 M urea-0.02 M EDTA-0.2 per cent SDS at pH 7.0. The isolated glycoprotein fraction is rich in dicarboxylic amino acids, contains galactose, mannose, (glucose), N-acetylglucosamine and sialic acid. The S-carboxamidomethyl glycoprotein preparation interacts with acid soluble calf skin collagen on isoelectric focusing in sucrose gradient in urea. This interaction is in favour of the biological role claimed for structural glycoproteins during fibrogenesis and differentiation.
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PMID:Structural glycoprotein from the media of pig aorta. Aggregation of the S-carboxamidomethyl subunits. 1 33

Extracts of human peripheral blood polymorphonuclear leukocyte granules, and two purified proteases derived from such extracts, an elastase and a chymotrypsin-like enzyme, degrade isolated bovine nasal cartilage proteoglycan at neutral pH. Viscosity studies indicate that the leukocyte granule extracts lack hyaluronidase activity and that their degradative effect on proteoglycan at physiological pH is due entirely to proteolytic action. Sepharose 4B gel chromatography and SDS-polyacrylamide gel electrophoresis of proteoglycan fractions treated with leukocyte granule enzymes at pH 7.0 indicate that they degrade one of the proteoglycan link proteins, release a fragment from the hyaluronic acid-binding portion of the proteoglycan subunit core protein, and break down the remainder of the proteoglycan subunit molecule into peptide fragments with varying numbers of chondroitin sulfate chains. Immunodiffusion studies indicate that the antigenic determinants of the proteoglycan subunit core protein and the link proteins survive treatment with granule proteases. Similar degradation of human articular cartilage proteoglycan by granule neutral proteases can be presumed to occur, in view of the similarity of structure of human articular and bovine nasal cartilage proteoglycans. The release of granule enzymes in the course of neutrophil-mediated inflammation can thus result in the degradation of cartilage matrix proteoglycan, leading to cartilage destruction and joint injury.
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PMID:Degradation of cartilage proteoglycan by human leukocyte granule neutral proteases--a model of joint injury. II. Degradation of isolated bovine nasal cartilage proteoglycan. 12 83

The state of chick embryo chondroblasts in culture was found to be sensitive to both fibronectin and another substance(s) (activity A) which could be extracted from chick embryo fibroblasts with 1 M urea or from conditioned medium. In the presence of either of these activities at concentrations of 25-150 micrograms/ml, chondroblasts, which normally grow as mixed cultures of floating and adherent cells, all immediately became attached to the tissue culture dish and spread. After several days, the morphology of these typically epithelioid cells became fibroblastic. This did not involve a selection process, since the effect was reversible. The synthetic program of these cells was also dramatically modified: the cultures no longer synthesized the chondroblast-unique type IV sulfated proteoglycan and began synthesizing alpha 2 collagen chains typical of fibroblastic or early limb bud cells. Fibronectin was resolved from activity A by gelatin affinity chromatography or gel filtration. Both activities were trypsin-sensitive. The two activities differed, however, on the basis of how the protein fractions in which they were found migrated in SDS-polyacrylamide gels, their specific activities and their effects on cell morphology and cell growth.
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PMID:Fibronectin alters the phenotypic properties of cultured chick embryo chondroblasts. 47 27

The alpha chains and the major CNBr - derived peptides of collagen of growth cartilage were studied in the following syndromes: thanatophoric dwarfism, pseudothanatophoric dwarfism, achondroplasia, pseudoachondroplasia, diastrophic dwarfism, metatropic dwarfism, Kniest disease, parastremmatic dwarfism, multiple exostoses, Blount disease and pycnodysostosis. After extraction of proteoglycans the collagen was solubilized by limited pepsin digestion purified, and the alpha chains were analysed by electrophoresis. The major CNBr - derived peptides were obtained by cleaving directly the cartilage after proteoglycan extraction. In some syndromes purified collagen was also cleaved. The CNBr peptides were analyzed by disc electrophoresis in SDS-polyacrylamide. Human normal growth cartilage and baboon cartilage were used as controls. The pattern of alpha chains and of major CNBr peptides was similar in all the cases studied, except one case of lethal diastrophic dwarfism in which the pattern of peptides showed the presence of type I collagen in quantities detectable by the present method. However in a milder case of diastrophic dwarfism the pattern of CNBr peptides was found normal. The present study does not exclude possible abnormalities of collagen at a higher lever of supramolecular organization in osteochondrodysplasias.
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PMID:[Study by gel electrophoresis, of alpha chains and of CNBr peptides of collagen from epiphyseal cartilage in chondrodysplasia]. 108

Epidermal growth factor (EGF) receptors were demonstrated on cultured rabbit costal chondrocytes. After crosslinking, the receptors on the cells with 125I-EGF, one major band of 170 KDa was separated by SDS-PAGE. Scatchard analysis demonstrated two classes of EGF receptors with Kd values of 0.3 nM and 1.6 nM. The numbers of high and low affinity receptors were 3,000 and 10,000 per cell, respectively. EGF receptors on chondrocytes were increased by treatment with retinoic acid and interleukin-1 beta, which inhibited proteoglycan synthesis. On the other hand, parathyroid hormone and dibutyryl cyclic AMP, which stimulated proteoglycan synthesis, decreased the number of EGF receptors. Treatments with these agents did not change the affinity of the receptors. These findings suggest that the number of EGF receptors is a negative marker of chondrocyte differentiation.
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PMID:Demonstration of receptors for epidermal growth factor on cultured rabbit chondrocytes and regulation of their expression by various growth and differentiation factors. 131 19

Synthesis of sulphated proteoglycans was compared in human erythroleukaemia (HEL) cells grown under control conditions and under stimulation by dimethyl sulphoxide (DMSO) and phorbol 12-myristate 13-acetate (PMA). Synthesis of [35S]sulphate-labelled proteoglycans by DMSO-treated cells was decreased by about 35% relative to controls, but synthesis of proteoglycans by PMA-treated cells increased 3-4-fold. Control and DMSO-treated cells secreted 65% of the newly synthesized proteoglycans, but PMA-treated cells secreted more than 90%. Sepharose CL-6B chromatography and SDS/PAGE suggested the presence of several proteoglycans in the cells and culture medium. The PMA-treated cells synthesized a low-Mr proteoglycan (Kav. 0.3( that was not present in controls and DMSO-treated cultures. The proteoglycans of the cells and medium from control, DMSO-treated and PMA-treated cultures could be separated into three fractions by octyl-Sepharose chromatography. The proteoglycans were resistant to trypsin but were degraded by Pronase and papain to fragments similar in size to the NaOH/NaBH4-generated glycosaminoglycans. The average chain length of the glycosaminoglycans (Kav. 0.20 on Sepharose CL-6B for controls) was decreased by DMSO (Kav. 0.25) and by PMA (Kav. 0.30-0.38). Chondroitin ABC lyase digestion of the proteoglycans from the medium of the control cultures produced two core proteins at Mr 31,000 and 36,000. The DMSO medium proteoglycans had only the 31,000-Mr core protein, and the PMA culture medium proteoglycans had core proteins of Mr 27,000, 31,000 and 36,000. Changes in synthesis of proteoglycans induced by DMSO or PMA may have relevance for the maturation of haematopoietic cells.
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PMID:Proteoglycan synthesis in human erythroleukaemia (HEL) cells. 137 1

A monoclonal antibody against arterial smooth muscle cell chondroitin sulfate proteoglycan has been developed. Incubation of [35S]-methionine labeled proteoglycans with MAb 941 quantitatively immunoprecipitated all the chondroitin sulfate proteoglycan (CSPG) synthesized by these cells. Digestion of the immunoprecipitate with chondroitin AC lyase revealed one major protein band (Mr 420,000) and two minor bands (Mr 509,000 and 390,000) on SDS-PAGE that are composed of very similar peptides when analyzed by limited peptide digestion by S. aureus V8 protease. Additional studies demonstrated that this monoclonal antibody recognized an epitope on the chondroitin sulfate chains. However, only a minor subpopulation (5-12%) of the alkaline-borohydride released glycosaminoglycan chains was immunoprecipitated and this subset of chains was slightly larger than the non-immunoprecipitated chains. High pressure liquid chromatography analysis of the disaccharides generated from the immunoprecipitated glycosaminoglycan chains demonstrated that these chains were enriched in chondroitin-6-sulfate relative to chondroitin-4-sulfate (2:1) while that of the non-immunoprecipitated chains had a ratio of 1:1. These studies indicate that at least two distinct pools of chondroitin sulfate chains are present on all the chondroitin sulfate proteoglycan synthesized by arterial smooth muscle cells: a major population (89-95%) containing 6-sulfate and 4-sulfate in relatively equal proportion and a minor population (5-12%) which is hydrodynamically larger with a 6-sulfate to 4-sulfate ratio of 2:1.
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PMID:Characterization of a chondroitin sulfate proteoglycan synthesized by monkey arterial smooth muscle cells in vitro. 137 3

Two extracellular matrix proteins of brain tissue, neuronectin (NEC1) and cytotactin (CT), are disulfide-bonded multimers of M(r) 180,000-250,000 subunits. The previously known distribution of these molecules is, however, very different. Human NEC1 is found throughout the white matter of rostral segments of the adult central nervous system (CNS) but not in rostral gray matter or in caudal CNS segments, including the cerebellum. In contrast, CT is absent or expressed at a low level in the adult chicken cerebrum but highly expressed in the cerebellum. Despite these differences in distribution, results obtained with antibodies that recognize NEC1 and CT in several vertebrate species indicate that these molecules are identical or at least closely related: (1) alpha NEC1 antibodies recognize proteins affinity-purified with CT-binding proteoglycan; (2) proteins recognized by alpha NEC1 and alpha CT antibodies in cells constitutively expressing the molecules, cells in which expression is induced by growth factors and phorbol ester and cells treated with tunicamycin (to block glycosylation) are identical in subunit composition and mobility on SDS gels; (3) the removal of NEC1 from culture supernatants by immunoprecipitation removes all molecules reactive with alpha CT antibodies and vice versa; (4) immunoblots of brain extracts with alpha NEC1 and alpha CT antibodies yield identical results. Having demonstrated the structural similarity between NEC1 and CT, we reexamined their distribution in the CNS. Surprisingly, the temporal and spatial distribution pattern of NEC1/CT varied greatly among species. Immunohistochemical and immunoblot experiments with adult human CNS tissues revealed significant levels of NEC1/CT in rostral but not caudal segments. In contrast, in cows and pigs the molecule is found throughout the CNS. Adult rat and mouse brains show regionally restricted expression of NEC1/CT in several areas of the cerebrum--distinct from those showing NEC1/CT in the human--and in the molecular layer of the cerebellum. Tests with fetal and newborn tissues revealed that CNS development in humans, cows and pigs is not accompanied by the marked decline in NEC1/CT levels or the changes in subunit composition found in the chicken CNS. The marked species diversity in temporospatial expression patterns suggests that intrinsic and/or extrinsic elements controlling the expression of NEC1/CT have diverged during vertebrate evolution.
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PMID:Species diversity of neuronectin and cytotactin expression patterns in the vertebrate central nervous system. 138 32

The specific binding and nature of the epitope recognized by monoclonal antibody (Mab) 1H10, which binds an antigen expressed on human cervical tumors, was characterized by enzyme digestion, lectin competition assay and immuno-electron microscopy. Membrane homogenates of CaSki cervical carcinoma cells were digested with various enzymes, then analysed by SDS-PAGE and immunoblotting. Cells grown on coverslips were treated with various enzymes and in situ binding of Mab 1H10 to cells was analysed by electron microscopy. The ability of lectin-conjugates to block Mab 1H10 binding to CaSki cells was also examined. Treatment of samples with sodium periodate abrogated antigen recognition by Mab 1H10. Neuraminidase and hyaluronidase digestion decreased but did not eliminate Mab 1H10 binding to cells in situ. Chondroitinase ABC digestion, in contrast, removed Mab 1H10 binding sites both in vitro and in situ. Trypsin and chymotrypsin digestion of cell membrane homogenates decreased the molecular weight of the Mab 1H10 antigen but did not decrease the binding intensity. Wheat germ agglutinin (WGA) strongly bound to CaSki cells and partially blocked Mab 1H10 binding, indicating that the antigen contains N-acetyl-galactosamine residues at or near the epitope recognized by Mab 1H10. Ricinus communis agglutinin (RCA) exhibited a similar binding pattern to WGA. However, concanavalin A bound only weakly to CaSki cells and was ineffective at blocking Mab 1H10 binding. The tumor-associated antigen recognized by Mab 1H10 is concluded to be a chondroitin sulphate glycoprotein or proteoglycan rather than a mucopolysaccharide or lipoprotein.
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PMID:Characterization of a human cervical carcinoma-associated antigen by lectin binding and immuno-electron microscopy. 142 5

Incorporation of radioactive sulfate to hatched veliger larvae of the gastropod muricid Concholepas concholepas indicated that over 87% of the sulfated macromolecules were found in the detergent insoluble fraction, rich in extracellular matrix (ECM) components. The sulfated material was solubilized with guanidine salt followed by urea dialysis and fractionated by DEAE-Sephacel chromatography. Three sulfated compounds eluting at 0.7, 1.1, and 3.0 M NaCl, called peaks I, II, and III, respectively, were obtained. The sulfated compound present in peak I was degraded by pronase or sodium alkaline treatment to a small sulfated resistant material, suggesting the presence of a proteoglycan (PG). Filtration analysis on Sephacryl S-500 and SDS-PAGE of the intact PG indicates that it has a high molecular weight (360,000 to over 1 x 10(6)). Monoclonal antibodies (mAb) against this PG were produced. The specificity of one mAb, the 6H2, was demonstrated by size chromatography and ELISA analysis. The epitope recognized by this mAb seems to be present in the core protein of the PG. Both the extent of sulfation and the presence of different sulfated species of PGs were evaluated during the development of this mollusc. A twelvefold increase in the incorporation of sulfate to PGs per milligram of protein was found in veliger larvae compared to blastula-glastula stages. This change correlated well with the differential expression of the sulfated PG present in peak I. Biochemical and immunological analysis indicate that high levels of this PG are found in veliger and trocophore larvae in comparison with blastula-gastrula and early juveniles.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A high molecular weight proteoglycan is differentially expressed during development of the mollusc Concholepas concholepas (Mollusca; Gastropoda; Muricidae). 146 Apr 34


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