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4 rezilta yo
Apoptosis induction by Maackia amurensis agglutinin in childhood acute lymphoblastic leukemic cells.
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Malignant transformation is known to be associated with changes in cell surface carbohydrate-architecture, which can be detected by lectins. In the present study, Maackia amurensis agglutinin (MAA), specific for NeuNAcalpha(2-->3)Gal/GalNAc showed strong binding with lymphoblasts of children having
Maackia amurensis agglutinin discriminates between normal and chronic leukemic human lymphocytes.
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Altered glycosylations of cell surface glycoproteins often accompany malignant transformation and lectins are useful for probing these alterations. Lymphocytes exhibit characteristic surface glycoproteins which serve as markers of cell status and development. The present work was undertaken to
Glycan moiety modifications of feline alpha1-acid glycoprotein in retrovirus (FIV, FeLV) affected cats.
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alpha1-Acid glycoprotein (AGP) is considered one of the major acute phase proteins in cats. In humans, AGP is a heavily glycosylated protein that undergoes several modifications of its glycan moiety during acute and chronic inflammatory pathologies. In this paper we present the feline AGPs (fAGP)
Detection of glycomic alterations induced by overexpression of p-glycoprotein on the surfaces of L1210 cells using sialic acid binding lectins.
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P-glycoprotein (P-gp) overexpression is the most frequently observed cause of multidrug resistance in neoplastic cells. In our experiments, P-gp was expressed in L1210 mice leukemia cells (S cells) by selection with vincristine (R cells) or transfection with the gene encoding human P-gp (T cells).
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