concanavalin-a has been researched along with Muscular-Dystrophy--Animal* in 4 studies
4 other study(ies) available for concanavalin-a and Muscular-Dystrophy--Animal
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Changes of soluble glycoproteins in dystrophic (dy/dy) mouse muscle shown by lectin binding.
Lectin binding sites in skeletal muscle from normal and dystrophic (dy/dy) C57 BL/6J mice were demonstrated by use of histochemistry and electrophoresis combined with electron microscopy. The following lectins were used: Canavalia ensiformis Con A, Triticum vulgaris (WGA), Glycine max (SBA), Griffonia simplicifolia (GS II), Arachis hypogaea (PNA), Pisum sativum (PSA) and Lens culinaris (LCA). After incubation of frozen sections with Con A, WGA, GS II, PSA and LCA a sarcoplasmic staining was observed in both normal and dystrophic muscle. The most consistent light microscopic observations in the dystrophic muscles were a decreased staining intensity of the sarcoplasm after incubation with Con A, WGA, PSA and LCA, but not with GS II, and a strong staining of the interfiber connective tissue. Supernatants, deprived of organelles and membranes, were prepared from normal and dystrophic muscle by high speed centrifugation. Lectin stained Western blots of the supernatant from dystrophic muscle showed two bands (120 and 67 K) with high affinities to avidin. Further this supernatant contained two glycoprotein bands (180 and 140 K) with affinities to Con A and a number of glycoprotein bands with apparent molecular weights below 67 K showing affinities to LCA and PSA. None of these glycoprotein bands could be detected in the supernatant from normal muscle. These changes of the muscle carbohydrate components might be involved in the expression of the dystrophic syndrome This seems to be the first report on changes of soluble glycoproteins in muscular dystrophy. Topics: Animals; Blotting, Western; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Glycoproteins; Histocytochemistry; Lectins; Male; Mice; Mice, Inbred C57BL; Microscopy, Electron; Muscles; Muscular Dystrophy, Animal; Organelles; Peanut Agglutinin; Plant Lectins; Solubility; Wheat Germ Agglutinins | 1992 |
Suppression of Con A mitogen-induced proliferation of normal spleen cells by macrophages from chickens with hereditary muscular dystrophy.
Spleen cells from chickens with hereditary muscular dystrophy (MD) give low blastogenic responses to the T cell mitogen concanavalin A (Con A) while exhibiting normal mitogen stimulated blastogenic responses to the T cell mitogen phytohemagglutinin (PHA). The addition of MD spleen cells to normal spleen cells caused a marked suppression of the Con A response of the normal cells while not affecting the PHA response of the normal cells. The suppressive activity by the MD spleen cells requires viable cells and is contact mediated. The suppressive activity is attributed to the presence in MD spleens of a population of suppressor cells with characteristics typical of macrophages. The suppressor cell activity was not removable by complement-mediated lysis using anti-T or anti-B sera, but it was reversible by treatment with carrageenan or carbonyl iron magnet, by passage through a Sephadex G-10 column, and by adherence to plastic petri dishes or glass beads. MD spleen cells depleted of the suppressor cell population remained unable to respond to Con A. Topics: Animals; Antilymphocyte Serum; Cell Membrane Permeability; Cell Separation; Cell Survival; Chickens; Complement System Proteins; Concanavalin A; Dose-Response Relationship, Immunologic; Female; Immune Tolerance; Isoantigens; Lymphocyte Activation; Macrophages; Male; Muscular Dystrophy, Animal; Phytohemagglutinins; Spleen | 1984 |
Concanavalin A binding sites on the erythrocytes of normal and genetically dystrophic chickens.
Red blood cells (RBCs) were obtained from genetically dystrophic chickens (Dy) and age-matched controls (C). Dy-RBCs had a lower titer of agglutination to concanavalin A (Con A) compared to C-RBCs. In order to ascertain the difference in agglutination, Con A binding on RBCs was studied, using 125I-labeled Con A ([125I]Con A) and ferritin conjugate to Con A (Fer-Con A). Kinetic analysis of [125I]Con A binding to Dy-RBCs showed a reduction of major binding sites of Con A. There was no difference in the apparent association constant for the major binding sites of Con A between Dy-RBCs and C-RBCs. Quantitative analysis of Con A binding site distribution on RBCs using Fer-Con A showed a remarkable diminution of ferritin particles tagged on the surface of Dy-RBCs. There was no significant difference in the distribution pattern of ferritin particles between Dy-RBCs and C-RBCs. Topics: Agglutination Tests; Animals; Binding Sites; Chickens; Concanavalin A; Erythrocytes; Iodine Radioisotopes; Male; Muscular Dystrophy, Animal; Tissue Distribution | 1983 |
Demonstration of a cellular defect in the thymus of hereditary muscular dystrophic chickens.
The thymuses of different aged hereditary muscular-dystrophic (MD) chickens were examined for abnormalities. Histochemical analyses showed a normal cellular profile. Thymic myoid cells were normal as to numbers, size, distribution, and metabolic status. The thymuses of MD chickens, however, exhibited two abnormalities not found in age and sex-matched normal controls. The thymus lobes were smaller in size and weighed less than the thymus lobes from controls, and the thymus cells from MD chickens gave reduced Con A and elevated PHA-T-cell mitogen-mediated blastogenic responses. Topics: Animals; Chickens; Concanavalin A; Female; Lymphocyte Activation; Male; Muscular Dystrophy, Animal; Organ Size; Phytohemagglutinins; Spleen; Thymus Gland | 1982 |