{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361981469192583296.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1152/ajpcell.1998.275.1.c189"}},{"identifier":{"@type":"URI","@value":"https://journals.physiology.org/doi/pdf/10.1152/ajpcell.1998.275.1.C189"}}],"dc:title":[{"@value":"Hypotonicity activates a lanthanide-sensitive  pathway for K<sup>+</sup> release in A6 epithelia"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p> The nature of the pathway for K<jats:sup>+</jats:sup> release activated during regulatory volume decrease (RVD) in A6 epithelia was investigated by measuring cell thickness (T<jats:sub>c</jats:sub>) as an index of cell volume and by probing K<jats:sup>+</jats:sup> efflux with<jats:sup>86</jats:sup>Rb as tracer for K<jats:sup>+</jats:sup>(R<jats:sub>Rb</jats:sub>). Cell swelling was induced by sudden reduction of basolateral osmolality (from 260 to 140 mosmol/kgH<jats:sub>2</jats:sub>O). Experiments were performed in the absence of Na<jats:sup>+</jats:sup>transport. Apical R<jats:sub>Rb</jats:sub> was negligible in iso- and hyposmotic conditions. On the other hand, osmotic shock increased basolateral R<jats:sub>Rb</jats:sub>([Formula: see text]) rapidly, reaching a maximum 7 min after the peak in T<jats:sub>c</jats:sub>. Quinine (0.5 mM) completely inhibited RVD and [Formula: see text]. Also verapamil (0.2 mM) impeded volume recovery considerably; lidocaine (0.2 mM) did not exert a noticeable effect. The K<jats:sup>+</jats:sup> channel blocker Ba<jats:sup>2+</jats:sup> (30 mM) delayed RVD but could not prevent complete volume recovery. Cs<jats:sup>+</jats:sup> inhibited RVD noticeably at concentrations <40 mM. With large Cs<jats:sup>+</jats:sup> concentrations (>40 mM), the initial osmometric swelling was followed by a gradual increase of T<jats:sub>c</jats:sub>, suggesting activation of Cs<jats:sup>+</jats:sup> influx. Chronic exposure of the basolateral surface to 0.5 mM La<jats:sup>3+</jats:sup> or Gd<jats:sup>3+</jats:sup> completely abolished RVD and[Formula: see text]. Acute administration of lanthanides at the time of osmolality decrease did not affect the initial phase of RVD and reduced [Formula: see text]only slightly. Apical Gd<jats:sup>3+</jats:sup> exerted an inhibitory effect on RVD and [Formula: see text]. The effect of Gd<jats:sup>3+</jats:sup> should therefore be localized at an intracellular site. The role of Ca<jats:sup>2+</jats:sup> entry could be excluded by failure of extracellular Ca<jats:sup>2+</jats:sup>removal to inhibit volume recovery. In contrast to lanthanides, chronically and acutely administered Mg<jats:sup>2+</jats:sup> (0.5 mM) inhibited RVD and[Formula: see text] by ∼50%. These data suggest that K<jats:sup>+</jats:sup> excretion during RVD occurs through a rather poorly selective pathway that does not seem to be directly activated by membrane stretch. </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381981469192583296","@type":"Researcher","foaf:name":[{"@value":"Patrick De Smet"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Physiology, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000 Louvain, Belgium"}]},{"@id":"https://cir.nii.ac.jp/crid/1381981469192583297","@type":"Researcher","foaf:name":[{"@value":"Jinqing Li"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Physiology, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000 Louvain, Belgium"}]},{"@id":"https://cir.nii.ac.jp/crid/1381981469192583298","@type":"Researcher","foaf:name":[{"@value":"Willy Van Driessche"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Physiology, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000 Louvain, Belgium"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"03636143"},{"@type":"EISSN","@value":"15221563"}],"prism:publicationName":[{"@value":"American Journal of Physiology-Cell Physiology"}],"dc:publisher":[{"@value":"American Physiological Society"}],"prism:publicationDate":"1998-07-01","prism:volume":"275","prism:number":"1","prism:startingPage":"C189","prism:endingPage":"C199"},"reviewed":"false","url":[{"@id":"https://journals.physiology.org/doi/pdf/10.1152/ajpcell.1998.275.1.C189"}],"createdAt":"2017-12-24","modifiedAt":"2024-06-17","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360567185438824320","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Suppression of cell membrane permeability by suramin: involvement of its inhibitory actions on connexin 43 hemichannels"}]},{"@id":"https://cir.nii.ac.jp/crid/2051151842050489728","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Regulation of WNK1 kinase by extracellular potassium"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1152/ajpcell.1998.275.1.c189"},{"@type":"CROSSREF","@value":"10.1111/bph.12693_references_DOI_8TYTvTEshHqslppe4m0zHimigPK"},{"@type":"CROSSREF","@value":"10.1007/s10157-010-0378-9_references_DOI_8TYTvTEshHqslppe4m0zHimigPK"}]}