{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T00:22:05Z","timestamp":1791073325913,"version":"4.1.0"},"reference-count":37,"publisher":"National Academy of Sciences","issue":"13","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,3,30]]},"abstract":"<jats:p>\n                    The cystic fibrosis transmembrane conductance regulator (CFTR) is expressed in many segments of the mammalian nephron, where it may interact with and modulate the activity of a variety of apical membrane proteins, including the renal outer medullary potassium (ROMK) K\n                    <jats:sup>+<\/jats:sup>\n                    channel. However, the expression of CFTR in apical cell membranes or its function as a Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channel in native renal epithelia has not been demonstrated. Here, we establish that CFTR forms protein kinase A (PKA)-activated Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channels in the apical membrane of principal cells from the cortical collecting duct obtained from mice. These Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channels were observed in cell-attached apical patches of principal cells after stimulation by forskolin\/3-isobutyl-1-methylxanthine. Quiescent Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channels were present in patches excised from untreated tubules because they could be activated after exposure to Mg-ATP and the catalytic subunit of PKA. The single-channel conductance, kinetics, and anion selectivity of these Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channels were the same as those of recombinant mouse CFTR channels expressed in\n                    <jats:italic>Xenopus laevis<\/jats:italic>\n                    oocytes. The CFTR-specific closed-channel blocker CFTR\n                    <jats:sub>inh<\/jats:sub>\n                    -172 abolished apical Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channel activity in excised patches. Moreover, apical Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channel activity was completely absent in principal cells from transgenic mice expressing the \u0394F508 CFTR mutation but was present and unaltered in ROMK-null mice. We discuss the physiologic implications of open CFTR Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    channels on salt handling by the collecting duct and on the functional CFTR\u2013ROMK interactions in modulating the metabolic ATP-sensing of ROMK.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0902661107","type":"journal-article","created":{"date-parts":[[2010,3,15]],"date-time":"2010-03-15T23:59:34Z","timestamp":1268697574000},"page":"6082-6087","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":34,"title":["Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA\u2013regulated apical chloride channels in cortical collecting duct"],"prefix":"10.1073","volume":"107","author":[{"given":"Ming","family":"Lu","sequence":"first","affiliation":[{"name":"Departments of aCellular and Molecular Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ke","family":"Dong","sequence":"additional","affiliation":[{"name":"Departments of aCellular and Molecular Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie E.","family":"Egan","sequence":"additional","affiliation":[{"name":"Pediatrics, Yale University School of Medicine, New Haven, CT 06520-8026"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerhard H.","family":"Giebisch","sequence":"additional","affiliation":[{"name":"Departments of aCellular and Molecular Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emile L.","family":"Boulpaep","sequence":"additional","affiliation":[{"name":"Departments of aCellular and Molecular Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven C.","family":"Hebert","sequence":"additional","affiliation":[{"name":"Departments of aCellular and Molecular Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,3,15]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.20.9262"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1152\/ajprenal.00184.2002"},{"key":"e_1_3_3_3_2","first-page":"F1038","article-title":"Both the wild type and a functional isoform of CFTR are expressed in kidney","volume":"270","author":"Morales MM","year":"1996","unstructured":"MM Morales, et al., Both the wild type and a functional isoform of CFTR are expressed in kidney. 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