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Alterations in glycan chains of the cell surface glycoconjugates are frequently implicated to modulate many biological processes such as cell-cell interaction,cell migration,differentiation and development.Cultured embryonic (E18) rat cortical neurons underwent apoptosis in response to the camptothecin in a dose-dependent manner.The lectin histochemistry showed that the binding of FITC-conjugated Maackia amurensis agglutinin (MAA),which is specific for terminal α2,3-sialic acid residues,to apoptotic neurons significantly and progressively increased comparing to that of normal cells.Analysis of cellular total proteins of apoptotic neurons by SDS-PAGE and lectin blotting using HRP-labeled MAA revealed that the expression of terminal α2,3-sialic acid residues on an unknown protein with an apparent molecular mass of 25.6 kDa increased on the apoptotic neurons with the increasing concentration of camptothecin.