| http://purl.uniprot.org/citations/12183454 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12183454 | http://www.w3.org/2000/01/rdf-schema#comment | "Volume-sensitive osmolyte and anion channels (VSOACs) are activated upon cell swelling in most vertebrate cells. Native VSOACs are believed to be a major pathway for regulatory volume decrease (RVD) through efflux of chloride and organic osmolytes. ClC-3 has been proposed to encode native VSOACs in Xenopus laevis oocytes and in some mammalian cells, including cardiac and vascular smooth muscle cells. The relationship between the ClC-3 chloride channel, the native volume-sensitive osmolyte and anion channel (VSOAC) currents, and cell volume regulation in HeLa cells and X. laevis oocytes was investigated using ClC-3 antisense. In situ hybridization in HeLa cells, semiquantitative and real-time PCR, and immunoblot studies in HeLa cells and X. laevis oocytes demonstrated the presence of ClC-3 mRNA and protein, respectively. Exposing both cell types to hypotonic solutions induced cell swelling and activated native VSOACs. Transient transfection of HeLa cells with ClC-3 antisense oligonucleotide or X. laevis oocytes injected with antisense cRNA abolished the native ClC-3 mRNA transcript and protein and significantly reduced the density of native VSOACs activated by hypotonically induced cell swelling. In addition, antisense against native ClC-3 significantly impaired the ability of HeLa cells and X. laevis oocytes to regulate their volume. These results suggest that ClC-3 is an important molecular component underlying VSOACs and the RVD process in HeLa cells and X. laevis oocytes."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m205132200"xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Hidalgo J."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Wilson S.M."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Horowitz B."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Hume J.R."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Andrade Y.N."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Hermoso M."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/author | "Satterwhite C.M."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/pages | "40066-40074"xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/title | "ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl- channels and volume regulation in HeLa cells and Xenopus laevis oocytes."xsd:string |
| http://purl.uniprot.org/citations/12183454 | http://purl.uniprot.org/core/volume | "277"xsd:string |
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