Concanavalin A lectin

Ramstrom, O., Lohmann, S., Bunyapaiboonsri, T., Lehn, J.-M. Dynamic combinatorial carbohydrate libraries probing the binding site of the concanavalin A lectin. Chem. Eur. J. 2004,10, 1711-1715. 

Fig. 2. Schematic representation of Concanavalin A lectin tetramer forming a cross-linked lattice with dimmer 18. (See color plate 1.)...

Group-specific Protein A Concanavalin A Lectins PolyU Poly A Poly Lys Triazine dye Nucleoside Boronic acid Thiol IGG D-Sugars Carbohydrates Nucleic acids Nucleic acids Nucleic acids Nucleotides Nucleotides 1,2-cw-Diol sugars Cysteine... 

Casas-Solvas JM, Ortiz-Salmeron E, Garcia-Fuentes L, Vargas-Berenguel A (2008) Ferrocene-mannose conjugates as electrochemical molecular sensors for concanavalin A lectin. Org Biomol Chem 6 4230 235... 

Concanavalin A is a plant lectin from the jack bean (Canavalia ensiformis) which binds with high affinity to mannose residues of glycoproteins. Concanavalin A is known to stimulate the tyrosine kinase activity of the INSR (3-subunit with consecutive activation of kinases downstream the insulin receptor (IRS, PI 3-kinase). It is believed that Concanavalin A stimulates the activation and autophosphorylation of the INSR kinase through aggregation of the receptor, although the precise mechanism of action is unclear. 

D. Page, D. Zanini, and R. Roy, Macromolecular recognition Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers, Bioorg. Med. Chem., 4 (1996) 1949-1961. 

M. Kohn, J. M. Benito, C. O. Mellet, T. K. Lindhorst, and J. M. Garcia Fernandez, Functional evaluation of carbohydrate-centred glycoclusters by enzyme-linked lectin assay Ligands for Concanavalin A, ChemBioChem, 5 (2004) 771-777. 

Thus, oxygen radical production by leukocytes can be responsible for cancer development. However, the levels of leukocyte oxygen radical generation depend on the type of cancer. For example, PMNs and monocytes from peripheral blood of patients with lung cancer produced a diminished amount of superoxide [169], Timoshenko et al. [170] observed the reduction of superoxide production in bronchial carcinoma patients after the incubation of neutrophils with concanavalin A or human lectin, while neutrophils from breast cancer patients exhibited no change in their activity. Chemotherapy of lung and colorectal carcinoma patients also reduced neutrophil superoxide production. Human ALL and AML cells produced, as a rule, the diminished amounts of superoxide in response to PMA or FMLP [171], On the other hand total SOD activity was enhanced in AML cells but diminished in ALL cells, while MnSOD in AML cells was very low. It has been proposed that decreased superoxide production may be responsible for susceptibility to infections in cancer patients. 

AMPA receptors desensitize within milliseconds upon exposure to AMPA, and kainate receptors likewise upon exposure to kainate. AMPA and kainate receptors can be securely distinguished from one another by their response to two drugs, cyclothiazide and the lectin concanavalin A [10], Cyclothiazide relieves AMPA receptor desensitization without affecting kainate receptors. 

The first allosteric modulators discovered to act on AMPA/KA receptors were the plant lectins, including concanavalin A (ConA), that block receptor desensitization, probably through binding to Y-1 inked oligosaccharides (51,52). It was soon discovered that certain benzothiazides, such as diazoxide and cyclothiazide, also act on the same allosteric site controlling non-NMDA receptor desensitization (53-55). Interestingly, ConA and cyclothiazide show high selectivity for KA and AMPA receptors, respec-... 

Glucose oxidase, glycoproteins from plasma membranes of rat liver Analytical and semi preparative separations Lectin Affinity (Concanavalin A) disks [76]... 

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