Involvement of acetylated tubulin in the regulation of Na+,K+‐ATPase activity in cultured astrocytes

FEBS Letters

Barra, Héctor S¹  Previtali, Gabriela²  Casale, Cesar H² 

[1] Centro de Investigaciones en Quı́mica Biológica de Córdoba (CIQUIBIC), UNC-CONICET, Departamento Quı́mica Biológica, Facultad de Ciencias Quı́micas, Universidad Nacional de Córdoba, Ciudad Universitaria, 5000-Córdoba, Argentina;Departamento de Biologı́a Molecular, Facultad de Ciencias Exactas, Fı́sico-Quı́micas y Naturales, Universidad Nacional de Rı́o Cuarto, Rı́o Cuarto, Córdoba, Argentina

关键词: Tubulin;    Acetylated tubulin;    ATPase;    Astrocyte;    AMPA;    α-amino-3-hydroxy-5-methylisoxazol-4-propionic acid;    CNQX;    6-cyano-7-nitroquinoxaline-2;    3-dione;    D-AP5;    D-(−)-2-amino-5-phosphono-valeric acid;    HAT;    hydrophobic acetylated tubulin;    L-AP3;    L(+)-2-amino-3-phosphono-propionic acid;    NMDA;    N-methyl-D-aspartic acid;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;    THA;    DL-threo-β-hydroxyaspartate;   

DOI  :  10.1016/S0014-5793(02)03802-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The results presented support the view that the modulation of Na⁺,K⁺-ATPase activity in living cells involves the association/dissociation of acetylated tubulin with the enzyme. We found that the stimulation of Na⁺,K⁺-ATPase activity by L-glutamate correlates with decreased acetylated tubulin quantity associated with the enzyme. The effect of L-glutamate was abolished by the glutamate transporter inhibitor DL-threo-β-hydroxyaspartate but was not affected by either specific agonists or antagonists. The effect of L-glutamate seems to be mediated by Na⁺ entry resulting from glutamate transport, since the Na⁺ ionophore monensin produced stimulation of Na⁺,K⁺-ATPase activity with concomitant decrease of acetylated tubulin quantity associated with the enzyme.

【 授权许可】

Unknown