Mitochondrial glycosidic residues contribute to the interaction between ruthenium amine complexes and the calcium uniporter

被引:4
作者
Correa, F [1 ]
Zazueta, C [1 ]
机构
[1] Inst Nacl Cardiol Ignacio Chavez, Dept Bioquim, Mexico City 14080, DF, Mexico
关键词
calcium uniporter; glycoproteins; mitochondria; ruthenium complex inhibitors;
D O I
10.1007/s11010-005-6754-1
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The role of glycosidic residues in the inhibitory properties of ruthenium complexes on mitochondrial calcium uptake was determined in mitoplasts. Our results showed that the binding and inhibitory properties of ruthenium amine complexes were modified when mitoplasts were exposed to N-glycosidase F action, but calcium uptake was not altered. N-linked proteins of the mitochondrial inner membrane were identified. We detected an 18-kDa protein that binds labeled Ru-360 under control conditions, but failed to bind the inhibitor after deglycosilation. A relationship between this protein and the action of ruthenium amine inhibitors of the mitochondrial uniporter is proposed.
引用
收藏
页码:55 / 62
页数:8
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