SELENIUM - INHIBITION OF MICROTUBULE FORMATION AND INTERACTION WITH TUBULIN

被引：16

作者：

LEYNADIER, D ^{[1
]}

PEYROT, V ^{[1
]}

CODACCIONI, F ^{[1
]}

BRIAND, C ^{[1
]}

机构：

[1] FAC PHARM MARSEILLE,PHYS PHARMACEUT LAB,27 BD JEAN MOULIN,F-13385 MARSEILLE 5,FRANCE

来源：

CHEMICO-BIOLOGICAL INTERACTIONS | 1991年 / 79卷 / 01期

关键词：

SELENITE; MICROTUBULE PROTEINS; SULFHYDRYL GROUPS; TUBULIN;

D O I：

10.1016/0009-2797(91)90055-C

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have studied the interaction of Na2SeO3 with microtubule proteins and tubulin. This selenium compound inhibits the polymerization of MTP (half-inhibition occurred for Na2SeO3 10-mu-M), and to a lesser that of tubulin. This effect of selenite is related to the formation of disulfide bridges between tubulin sulfhydryl groups, inducing a conformational change of the protein. This is corroborated by the modified binding of colchicine and vinblastine in presence of selenium. The selenite inhibitory concentrations are similar to the toxic blood levels of selenium (40-mu-M).

引用

页码：91 / 102

页数：12

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