The presence of tubulin in human erythrocytes was demonstrated using five different antibodies. Tubulin was distributed among three operationally distinguishable pools: membrane, sedimentable structure and soluble fraction. It is known that in erythrocytes from hypertensive subjects (HS), the Na(+), K(+)-ATPase (NKA) activity is partially inhibited as compared with erythrocytes from normal subjects (NS). In erythrocytes from HS the membrane tubulin pool is increased by ~150%. NKA was found to be forming a complex with acetylated tubulin that results in inhibition of enzymes. This complex was also increased in erythrocytes from HS. Treatment of erythrocytes from HS with nocodazol caused a decrease of acetylated tubulin in the membrane and stimulation of NKA activity, whereas taxol treatment on erythrocytes from NS had the opposite effect. These results suggest that, in erythrocytes from HS, tubulin was translocated to the membrane, where it associated with NKA with the consequent enzyme inhibition.

We recently described the interaction of Na + ⁄ K + -ATP ase with acetylated tubulin in neural [1-3] and nonneural cells [4]. Formation of such a complex inhibits ATPase activity. Conversely, dissociation of the complex leads to activation of the enzyme. The ATPaseacetylated tubulin complex behaves as a hydrophobic

Manipulation of yeast cell polarity by external electric fields reveals electrochemical pathways that influence the distribution of membrane lipids and the polarity regulator Cdc4p.

These findings indicate that increased Mem-tub content contributes to reduced erythrocyte deformability in hypertensive animals.