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MytiLec-1, a 17 kDa lectin with &#946;-trefoil folding that was isolated from the Mediterranean mussel (<i>Mytilus galloprovincialis</i>) bound to the disaccharide melibiose, Gal&#945;(1,6) Glc, and the trisaccharide globotriose, Gal&#945;(1,4) Gal&#946;(1,4) Glc. Toxicity of the lectin was found to be low with an LC₅₀ value of 384.53 &#956;g/mL, determined using the <i>Artemia</i> nauplii lethality assay. A fluorescence assay was carried out to evaluate the glycan-dependent binding of MytiLec-1 to <i>Artemia</i> nauplii. The lectin strongly agglutinated Ehrlich ascites carcinoma (EAC) cells cultured in vivo in Swiss albino mice. When injected intraperitoneally to the mice at doses of 1.0 mg/kg/day and 2.0 mg/kg/day for five consecutive days, MytiLec-1 inhibited 27.62% and 48.57% of cancer cell growth, respectively. Antiproliferative activity of the lectin against U937 and HeLa cells was studied by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay in vitro in RPMI-1640 medium. MytiLec-1 internalized into U937 cells and 50 &#956;g/mL of the lectin inhibited their growth of to 62.70% whereas 53.59% cell growth inhibition was observed against EAC cells when incubated for 24 h. Cell morphological study and expression of apoptosis-related genes (p53, Bax, Bcl-X, and NF-&#954;B) showed that the lectin possibly triggered apoptosis in these cells.