{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,19]],"date-time":"2026-02-19T20:35:07Z","timestamp":1771533307413,"version":"3.50.1"},"reference-count":0,"publisher":"American Physiological Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1997,9,1]]},"abstract":"<jats:p> The activity of Na(+)-K(+)-ATPase can be regulated by hormones that activate adenosine 3',5'-cyclic monophosphate-dependent protein kinase (PKA). Here, using a site-directed phosphorylation state-specific antibody, we show that hormonal regulation of Na(+)-K(+)-ATPase can occur via phosphorylation of Ser-943 on its alpha-subunit. cDNAs coding for wild-type rat Na(+)-K(+)-ATPase and Na(+)-K(+)-ATPase in which the PKA phosphorylation site Ser-943 was mutated to Ala were stably and transiently transfected into COS cells. In COS cells expressing wild-type Na(+)-K(+)-ATPase the beta-adrenergic agonist isoproterenol (1 microM) significantly increased the level of phosphorylation of the alpha-subunit. Phosphorylation was accompanied by a significant inhibition of the enzyme activity, as reflected by a decrease in ATP hydrolysis and 86Rb+ transport. The effect of isoproterenol was reproduced by the PKA activator forskolin used in combination with the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine and was abolished by the specific PKA inhibitor H-89. Okadaic acid, an inhibitor of protein phosphatases 1 and 2A, enhanced phosphorylation and inhibition of Na(+)-K(+)-ATPase induced by isoproterenol. The changes in activity of Na(+)-K(+)-ATPase linearly correlated with the extent of the alpha-subunit of Na(+)-K(+)-ATPase being phosphorylated. When Ser-943 was replaced by alanine, stimulation of the phosphorylation and inhibition of the activity of Na(+)-K(+)-ATPase induced by isoproterenol, alone or in combination with okadaic acid, were not observed. These results indicate that, in intact cells, modulation of the activity of Na(+)-K(+)-ATPase can be achieved by regulation of the state of phosphorylation of Ser-943. Moreover, they provide a biochemical mechanism by which beta-adrenergic agonists can regulate Na(+)-K(+)-ATPase activity. <\/jats:p>","DOI":"10.1152\/ajpcell.1997.273.3.c893","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T16:11:29Z","timestamp":1514131889000},"page":"C893-C901","source":"Crossref","is-referenced-by-count":55,"title":["PKA-mediated phosphorylation and inhibition of Na(+)-K(+)-ATPase in response to beta-adrenergic hormone"],"prefix":"10.1152","volume":"273","author":[{"given":"X. J.","family":"Cheng","sequence":"first","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Fisone","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O.","family":"Aizman","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Aizman","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Levenson","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P.","family":"Greengard","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Aperia","sequence":"additional","affiliation":[{"name":"Department of Woman and Child Health, St. Goran's Children's Hospital,Karolinska Institute, Stockholm, Sweden."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1997.273.3.C893","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:34:08Z","timestamp":1718652848000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1997.273.3.C893"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,9,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1997,9,1]]}},"alternative-id":["10.1152\/ajpcell.1997.273.3.C893"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1997.273.3.c893","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,9,1]]}}}