{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:38:57Z","timestamp":1759541937482},"reference-count":35,"publisher":"American Physiological Society","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2001,4,1]]},"abstract":"<jats:p> Insulin stimulates K<jats:sup>+<\/jats:sup> transport by the Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase in human fibroblasts. In other cell systems, this action represents an automatic response to increased intracellular [Na<jats:sup>+<\/jats:sup>] or results from translocation of transporters from an intracellular site to the plasma membrane. Here we evaluate whether these mechanisms are operative in human fibroblasts. Human fibroblasts expressed the \u03b1<jats:sub>1<\/jats:sub> but not the \u03b1<jats:sub>2<\/jats:sub> and \u03b1<jats:sub>3<\/jats:sub> isoforms of Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase. Insulin increased the influx of Rb<jats:sup>+<\/jats:sup>, used to trace K<jats:sup>+<\/jats:sup> entry, but did not modify the total intracellular content of K<jats:sup>+<\/jats:sup>, Rb<jats:sup>+<\/jats:sup>, and Na<jats:sup>+<\/jats:sup> over a 3-h incubation period. Ouabain increased intracellular Na<jats:sup>+<\/jats:sup> more rapidly in cells incubated with insulin, but this increase followed insulin stimulation of Rb<jats:sup>+<\/jats:sup> transport. Bumetanide did not prevent the increased Na<jats:sup>+<\/jats:sup> influx or stimulation of Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase. Stimulation of the Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>- ATPase by insulin did not produce any measurable change in membrane potential. Insulin did not affect the affinity of the pump toward internal Na<jats:sup>+<\/jats:sup> or the number of membrane-bound Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPases, as assessed by ouabain binding. By contrast, insulin slightly increased the affinity of Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase toward ouabain. Phorbol esters did not mimic insulin action on Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase and inhibited, rather than stimulated, Rb<jats:sup>+<\/jats:sup> transport. These results indicate that insulin increases the turnover rate of Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPases of human fibroblasts without affecting their number on the plasma membrane or modifying their dependence on intracellular [Na<jats:sup>+<\/jats:sup>]. <\/jats:p>","DOI":"10.1152\/ajpcell.2001.280.4.c912","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T20:32:16Z","timestamp":1514147536000},"page":"C912-C919","source":"Crossref","is-referenced-by-count":8,"title":["Insulin increases the turnover rate of Na<sup>+<\/sup>-K<sup>+<\/sup>-ATPase in human fibroblasts"],"prefix":"10.1152","volume":"280","author":[{"given":"Nicola","family":"Longo","sequence":"first","affiliation":[{"name":"Division of Medical Genetics, Department of Pediatrics, Emory University, Atlanta, Georgia 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