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

CASALE CH; PREVITALI, G; BARRA H. S.

FEBS LETTERS

ELSEVIER SCIENCE BV

Año: 2003 vol. 534 p. 115 - 118

0014-5793

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 e¡ect of L-glutamate was abolished by the glutamate transporter inhibitor DL-threo-L-hydroxyaspartate but was not a¡ected by either speci¢c agonists or antagonists.The e¡ect 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.