{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T09:52:40Z","timestamp":1768470760962,"version":"3.49.0"},"reference-count":39,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2010,6,29]],"date-time":"2010-06-29T00:00:00Z","timestamp":1277769600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2010,7]]},"abstract":"<jats:p>This study was undertaken to investigate whether the mechanism of increased Na<jats:sup>+<\/jats:sup>\u2013K<jats:sup>+<\/jats:sup>\u20132Cl<jats:sup>\u2212<\/jats:sup> (NKCC1) cotransporter activity by osmotic shrinkage involved AMP\u2010activated protein kinase (AMPK) activation. AMPK was found to phosphorylate a recombinant GST\u2010dogfish (1\u2013260) NKCC1 fragment at Ser38 and Ser214, corresponding to Ser77 and Ser242 in human NKCC1, respectively. Incubation of human erythrocytes with 20 \u03bc<jats:sc>m<\/jats:sc> A769662 AMPK activator increased Ser242 NKCC1 phosphorylation but did not stimulate <jats:sup>86<\/jats:sup>Rb<jats:sup>+<\/jats:sup> uptake. Under hypertonic conditions in human red blood cells (RBCs) incubated with 0.3 <jats:sc>m<\/jats:sc> sucrose, NKCC1 activity increased as measured by bumetanide\u2010sensitive <jats:sup>86<\/jats:sup>Rb<jats:sup>+<\/jats:sup> uptake and AMPK was activated. However, there was no effect of AMPK\u03b11 deletion in mouse RBCs on the increased rate of <jats:sup>86<\/jats:sup>Rb<jats:sup>+<\/jats:sup> uptake induced by hyperosmolarity. AMPK activation by osmotic shrinkage of mouse RBCs was abrogated by 10 \u03bc<jats:sc>m<\/jats:sc> STO\u2010609 CaMKK\u03b2 inhibitor, but incubation with STO\u2010609 did not affect the increase in <jats:sup>86<\/jats:sup>Rb<jats:sup>+<\/jats:sup> uptake induced by hyperosmolarity. Osmotic shrinkage of human and mouse RBCs led to activation loop phosphorylation of the STE20\/SPS1\u2010related proline\/alanine\u2010rich kinase (SPAK) at Thr233, which was accompanied by phosphorylation of NKCC1 at Thr203\/207\/212, one of which (Thr207) is responsible for cotransporter activation. Therefore, phosphorylation\u2010induced activation of NKCC1 by osmotic shrinkage does not involve AMPK and is likely to be due to SPAK activation.<\/jats:p>","DOI":"10.1113\/jphysiol.2009.185900","type":"journal-article","created":{"date-parts":[[2010,5,5]],"date-time":"2010-05-05T02:04:05Z","timestamp":1273025045000},"page":"2315-2328","source":"Crossref","is-referenced-by-count":17,"title":["Stimulation of human and mouse erythrocyte Na<sup>+<\/sup>\u2013K<sup>+<\/sup>\u20132Cl<sup>\u2212<\/sup> cotransport by osmotic shrinkage does not involve AMP\u2010activated protein kinase, but is associated with STE20\/SPS1\u2010related proline\/alanine\u2010rich kinase 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