Effect of Zinc Ions on the Interaction of S-100 Protein with Brain Microtubule Proteins(Biological)

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In the presence of Zn^<2+>, S-100 protein inhibited microtubule assembly in vitro in a concentration-dependent fashion and the inhibition was reversed by adding ethylenediaminetetraacetic acid (EDTA). Both the rate and extent of microtubule assembly were inhibited. At low Zn^<2+> concentrations, electron microscopic observation demonstrated that normal microtubules were formed for the most part in the presence of S-100 protein, while polymorphic forms were predominant in its absence. An interaction between S-100 protein and microtubule proteins was directly demonstrated by Zn^<2+>-dependent affinity chromatography on S-100 protein coupled to Sepharose 4B. A considerable amount of tubulin dimer was retained by the column in the presence of Zn^<2+> and was eluted with EDTA, suggesting the possibility of a Zn^<2+>-dependent interaction between S-100 protein and tubulin dimer.
公益社団法人日本薬学会の論文
1986-12-25