{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T22:29:43Z","timestamp":1787005783758,"version":"build-2736575974"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"15","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1996,7,23]]},"abstract":"<jats:p>In tight Na+-absorbing epithelial cells, the fate of Na+ entry through amiloride-sensitive apical membrane Na+ channels is matched to basolateral Na+ extrusion so that cell Na+ concentration and volume remain steady. Control of this process by regulation of apical Na+ channels has been attributed to changes in cytosolic Ca2+ concentration or pH, secondary to changes in cytosolic Na+ concentration, although cytosolic Cl- seems also to be involved. Using mouse mandibular gland duct cells, we now demonstrate that increasing cytosolic Na+ concentration inhibits apical Na+ channels independent of changes in cytosolic Ca2+, pH, or Cl-, and the effect is blocked by GDP-beta-S, pertussis toxin, and antibodies against the alpha-subunits of guanine nucleotide-binding regulatory proteins (Go). In contrast, the inhibitory effect of cytosolic anions is blocked by antibodies to inhibitory guanine nucleotide-binding regulatory proteins (Gi1\/Gi2. It thus appears that apical Na+ channels are regulated by Go and Gi proteins, the activities of which are controlled, respectively, by cytosolic Na+ and Cl-.<\/jats:p>","DOI":"10.1073\/pnas.93.15.8107","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:40:52Z","timestamp":1027680052000},"page":"8107-8111","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":65,"title":["Cytosolic Na+ controls and epithelial Na+ channel via the Go guanine nucleotide-binding regulatory protein."],"prefix":"10.1073","volume":"93","author":[{"given":"P","family":"Komwatana","sequence":"first","affiliation":[{"name":"Department of Physiology, University of Sydney, New South Wales 2006, Australia."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Dinudom","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Sydney, New South Wales 2006, Australia."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J A","family":"Young","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Sydney, New South Wales 2006, Australia."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D I","family":"Cook","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Sydney, New South Wales 2006, Australia."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1996,7,23]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.93.15.8107","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T14:55:57Z","timestamp":1649861757000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.93.15.8107"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,7,23]]},"references-count":0,"journal-issue":{"issue":"15","published-print":{"date-parts":[[1996,7,23]]}},"alternative-id":["10.1073\/pnas.93.15.8107"],"URL":"https:\/\/doi.org\/10.1073\/pnas.93.15.8107","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,7,23]]},"assertion":[{"value":"1996-07-23","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}