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Science 17 August 1984:
Vol. 225. no. 4663, pp. 745 - 746
DOI: 10.1126/science.6463652
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Articles

Science, Vol 225, Issue 4663, 745-746
Copyright © 1984 by American Association for the Advancement of Science

articles

Methylation increases sodium transport into A6 apical membrane vesicles: possible mode of aldosterone action

S Sariban-Sohraby, M Burg, WP Wiesmann, PK Chiang, and JP Johnson

When isolated apical membrane vesicles prepared from cultured A6 epithelia were incubated in vitro with the methyl donor S-adenosylmethionine, the control rate of amiloride-inhibitable sodium transport was doubled. The methylation inhibitors 3-deazaadenosine and S-adenosyl homocysteine returned the S-adenosyl-methionine-stimulated sodium transport to control levels. Neither these agents nor adenosine affected sodium transport into control vesicles. In vesicles incubated with S-adenosyl-[3H-methyl]methionine, both membrane phospholipids and proteins were labeled, and this labeling was inhibited by deazaadenosine. In vesicles prepared from A6 cells treated with aldosterone, sodium transport was twice the control value and S-adenosylmethionine did not cause any further stimulation of transport. In those vesicles, both lipid and protein methylation were increased. These results suggest that methylation, which increases the rate of amiloride-sensitive sodium transport is involved in the action of aldosterone at the apical membrane level in epithelia.


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