{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T01:35:50Z","timestamp":1793151350408,"version":"4.5.0"},"reference-count":59,"publisher":"American Physiological Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2001,8,1]]},"abstract":"<jats:p>The K-Cl cotransporters (KCCs) have a broad range of physiological roles, in a number of cells and species. We report here that Xenopus laevis oocytes express a K-Cl cotransporter with significant functional and molecular similarity to mammalian KCCs. Under isotonic conditions, defolliculated oocytes exhibit a Cl<jats:sup>\u2212<\/jats:sup>-dependent<jats:sup>86<\/jats:sup>Rb<jats:sup>+<\/jats:sup>uptake mechanism after activation by the cysteine-reactive compounds N-ethylmaleimide (NEM) and mercuric chloride (HgCl<jats:sub>2<\/jats:sub>). The activation of this K-Cl cotransporter by cell swelling is prevented by inhibition of protein phosphatase-1 with calyculin A; NEM activation of the transporter was not blocked by phosphatase inhibition. Kinetic characterization reveals apparent values for the Michaelis-Menten constant of 27.7 \u00b1 3.0 and 15.4 \u00b1 4.7 mM for Rb<jats:sup>+<\/jats:sup>and Cl<jats:sup>\u2212<\/jats:sup>, respectively, with an anion selectivity for K<jats:sup>+<\/jats:sup>transport of Cl<jats:sup>\u2212<\/jats:sup>= PO[Formula: see text] = Br<jats:sup>\u2212<\/jats:sup>&gt; I<jats:sup>\u2212<\/jats:sup>&gt; SCN<jats:sup>\u2212<\/jats:sup>&gt; gluconate. The oocyte K-Cl cotransporter was sensitive to several inhibitors, including loop diuretics, with apparent half-maximal inhibition values of 200 and 500 \u03bcM for furosemide and bumetanide, respectively. A partial cDNA encoding the Xenopus K-Cl cotransporter was cloned from oocyte RNA; the corresponding transcript is widely expressed in Xenopus tissues. The predicted COOH-terminal protein fragment exhibited particular homology to the KCC1\/KCC3 subgroup of the mammalian KCCs, and the functional characteristics are the most similar to those of KCC1 (Mercado A, Song L, Vazquez N, Mount DB, and Gamba G. 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