Ricinus lectins

Ricinus lectin RCAii0 Ricinus communis GalNAc, (3-Gal, 3-Gal... 

Sphyris, N., Lord, J.M., Wales, R. and Roberts, L.M. (1995) Mutational analysis of the Ricinus lectin B-chains. Galactose-binding ability of the 2 gamma subdomain of Ricinus communis agglutinin B-chain. J Biol Chem, 270, 20292-20297. 

Ricin is a 66-kilodalton (kd) globular protein that makes up 1% to 5% by weight of the bean of the castor plant, Ricinis communis. The toxic heterodimer consists of a 32-kd A-chain that is disulfide-bonded to a 32-kd B-chain.21 The toxin is stored in the matrix of the castor bean, together with a 120,000-d ricinus lectin.22 Both chains are glycoproteins containing mannose carbohydrate groups the two 32-kd chains must be associated for toxicity. 

There is still some discordance about markers for ATI cells [17, 18]. Varieties of glycocalyx appear to be expressed in ATI versus ATII cells, which can be distinguished by the binding of specific lectins. Lycopersicon esculen-tum lectin, for example, appears to adhere specifically to the apical plasma membrane of ATI cells [19, 20], Other lectin markers that have been reported in AEC typing are Ricinus communis agglutinin, Erythrina cristagalli lectin, soybean lectin and Bauhinia purpurea agglutinin (all for the ATI phenotype),... 

Lectin toxicity - nausea, diarrhea, headache, confusion, dehydration, death Wisteria, castor bean (Ricinus communis) Lectins bind to cell surfaces Ricin - blocks protein synthesis, very toxic, 5 to 6 beans can kill a child... 

Circular dichroism (CD) has been utilized to investigate the effect of saccharides on the conformation of lectins in solution. CD has demonstrated saccharide-induced conformational changes in the lectins from Canavalia ensiformis (7), Dolichos biflorus (8), Ricinus communis (9), and Triticum vulgaris (10). The present study uses circular dichroism to assess the secondary structure of SBA and to measure conformational transitions induced by the saccharides which bind to this lectin. These and previous studies will contribute to a clearer understanding of the unique properties of these sugar-binding proteins. 

Fig. 15.—Human IgA, Glycopeptide871 Showing the Carbohydrate-binding Loci for Various Lectins, [a. Limulus polyphemus b, Triticum vulgaris c, Ricinus communis d, Sophora japonica e, Abrus precatorius f, Cytisus sessilifolius g, Phaseolus vulgaris-, h, Canavalia ensiformis i, Lens culinaris j, Pisum sativus k, Vicia faba-, 1, Bandeiraea simplicifolia II m, Solanum tuberosum and n, Ulex europeus II.]...

Ricin was found by Stillmark in 1889 as the first plant lectin derived from the seeds of the castor plant, Ricinus communis L., a member of the Euphorbiaceae or spurge family. Other members of this family include the popular houseplants poinsettia E. pulcherrima), and the croton species. The term castor bean is used commonly to refer to both the plant and seed of R. communis. Ricinus communis commonly grows along streams and riverbeds in addition to subtropical locations high in nutrients. Ricinus communis is a coarse perennial, 10-13 m tall in the tropics, with a stem 7.5-15 cm... 

Olsnes, S., Saltvedt, E., Pihl, A. (1974a). Isolation and comparison of galactose-binding lectins Jrom Abrus precatorius and Ricinus communis. J. Biol. Chem. 249 803-10. 

Lectin PNA Arachis hypogaea Lectin RCA 120 Ricinus communis Lectin SNA Sambucus nigra... 

Mannoji H, Yeger H, Becker LE (1986) A specific histochemical marker (lectin Ricinus communis agglutinin-1) for normal human microglia, and application to routine histopathology. Acta Neuro-pathol (Berl) 71 341-343. 

Hegde, R. and Fodder, S.K. (1998) Evolution of tetrameric lectin Ricinus communis agglutinin from two variant groups of ricin toxin dimers. Eur J Biochem, 254, 596-601. 

Nicolson, G.L., Lacorbiere, M. and Hunter, T.R. (1975) Mechanism of cell entry and toxicity of an affinity-purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts. Cancer Res, 35, 144—155. 

Olsnes, S., Pappenheimer, A.M., Jr. and Meren, R. (1974a) Lectins from Abrus precatorius and Ricinus communis. II. Hybrid toxins and their interaction with chain-specific antibodies. J Immunol, 113, 842-847. 

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