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Results for “Receptors, Concanavalin A”

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At least 19 recordsLinked to original sources
PubMed1976

Active cell edge and movements of concanavalin A receptors of the surface of epithelial and fibroblastic cells.

Movements of the receptors of concanavalin A on various parts of the surfaces of substrate-attached cells were compared. Cultured mouse embryo cells of several types were used: epithelial kidney cells and normal and transformed fibroblasts. Initial distribution of receptors was random on the cells of all types. Binding of concanavalin A induced patching of its receptors on all the cell parts. In contrast, directional centripetal movement of receptors was observed only on the surface of certain cell parts, namely, only the surface of peripheral lamellar cytoplasm was cleared of the receptors. Clearing was always initiated in the zone of lamellar cytoplasm located near active cell edges. In epithelial sheets, clearing was not observed on the surface of central cells that had no lamellar cytoplasm. Concanavalin A receptors on the cleared areas of cell surface were gradually restored after the end of incubation. It is suggested that anchoring of the patches of membrane receptors by cortical microfilaments is possible only on the surface of pseudopods and of lamellar cytoplasm but not on the surface of other cell parts. Besides receptor movements, this hypothesis may be explain differences in the adhesive properties of various parts of the cell surface.

Animals↗
PubMed1982

Concanavalin A receptor sites on lymph node cells in vivo and in vitro.

The distribution and density of receptors for concanavalin A (Con A) on the surfaces of cells of intact and isolated popliteal and axillary lymph nodes were investigated in the rabbit. Intact lymph nodes were perfused via the subcapsular (marginal) sinus with either Con A peroxidase or Con A ferritin, fixed with glutaraldehyde, and processed for electron microscopy. Both Con A peroxidase and Con A ferritin were distributed on the plasmalemma of lymphocytes, macrophages, neutrophils, plasma cells, reticular endothelial cells, and the vascular endothelium. Counts of Con A-conjugated ferritin particles indicated that the density of Con A receptors was generally similar for lymphocytes, macrophages, and neutrophils but lower on plasma cells. When lymph node cells were isolated by mechanical methods and exposed to Con A ferritin, the label was homogenously distributed on the cell surfaces of most cells. However, Con A binding was significantly higher on the surface of isolated cells than in the intact node. It is suggested that the increase in density of Con A binding sites on isolated cells may possibly be due to an unmasking of cell surface moieties in which additional Con A receptor sites become available as a result of the isolation procedure. The density of Con A ferritin binding sites was also significantly lower on the surface of isolated plasma cells than the lymphocyte and macrophage, suggesting that the density distribution of cell surface saccharides is different for various lymphoid cells.

Animals↗
PubMed1975

Isolation of a concanavalin A receptor from mouse L cells.

A cell surface glycoprotein receptor for concanavalin A (Con A) has been isolated from mouse L cells. The isolation procedure involved dissolving whole L cells in 0.3 M lithium diiodosalicylate and extracting with aqueous phenol. The Con A receptor, which was found in the aqueous phase of this extract, was further purified by affinity chromatography on a column of Con A-Sepharose; the receptor was adsorbed to Con A-Sepharose and eluted with 0.1 M methyl alpha-D-glucopyranoside or with 0.1 M methyl alpha-D-mannopyranoside, but not with other monosaccharides. The cell surface location of the Con A receptor purified in this way was confirmed by showing that it can be isolated from purified L cell plasma membranes and by demonstrating that it can be labeled from the exterior surface of intact L cells by the nonpenetrating galactose oxidase-KB3H4 system. Biochemical studies of the Con A receptor have shown that it migrates on sodium dodecyl sulfate-polyacrylamide gels as a single component having an apparent molecular weight of approximately 100,000. Its N-terminal amino acid is valine and it has carbohydrate attached at several (at least five) different sites along the polypeptide chain.

Amino Acid Sequence↗
PubMed1979

Feline lymphocytes: observations on surface membrane concanavalin A receptor mobility.

The mechanics of concanavalin A receptor mobility of the feline lymphocyte surface membrane were investigated, utilizing fluorescein-labeled lectin to quantitate lymphocyte capping. The results of this study indicated that lectin concentration and buffer selection were critical for extensive receptor redistribution with cap formation of feline lymphocytes. Maximal capping was obtained with 50 microgram of concanavalin A/ml of minimal essential medium. The mean capping rate of peripheral blood lymphocytes increased significantly with colchicine exposure at 10(-7) M concentration. The mean values of capping increased slightly with advancing age of feline donors, although this difference was not statistically significant. Concurrent work has indicated that concanavalin A capping may be useful in the study of immunosuppression in feline leukemia virus-infected cats.

Age Factors↗
PubMed1989

[Distribution and lateral mobility of concanavalin A receptors in the course of cell cycle of human gastric cancer cells].

The distribution and lateral mobility of Con A receptors in the course of the cell cycle has been studied on human gastric low-differentiated mucous adenocarcinoma cells (MGC 80-3). Synchronized MGC 80-3 cells in monolayer were labeled with F-ConA in the different phases of cell cycle. The discontinuous pattern of surface labelling was present during G1, S and G2, while there were marked differences among them. The cells in mitosis displayed uniform distribution of Con A receptors complex with strong fluorescence. The fluorescence photobleaching recovery method has been used to determine the lateral mobilities of Con A receptors complex. There was marked difference among various phases for mobility pattern and diffusion coefficient. The pattern of mobility of Con A receptor complex was appeared diffusion mobility in M and G1 phases, while flow pattern occurred in S and G2 phases. The diffusion coefficient (D) G1 greater than M, the rate of flow S greater than G2, but mobile fraction in G2 phase is higher than other phases. These results showed that dynamic properties of Con A receptor are apparently different which were regulated by the cell cycle.

Adenocarcinoma, Mucinous↗