Publication Date:
1984-08-17
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sariban-Sohraby, S -- Burg, M -- Wiesmann, W P -- Chiang, P K -- Johnson, J P -- New York, N.Y. -- Science. 1984 Aug 17;225(4663):745-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6463652" target="_blank"〉PubMed〈/a〉
Keywords:
Aldosterone/*physiology
;
Amiloride/pharmacology
;
Amphibians
;
Animals
;
Biological Transport, Active/drug effects
;
Cell Line
;
Cell Membrane/drug effects/*metabolism
;
Kidney/metabolism
;
Methylation
;
S-Adenosylhomocysteine/pharmacology
;
S-Adenosylmethionine/pharmacology
;
Sodium/*metabolism
;
Tubercidin/pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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