Linked Life Data

12183454

Source:http://linkedlifedata.com/resource/pubmed/id/12183454

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2002-10-15
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
40066-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12183454-Animals, pubmed-meshheading:12183454-Anions, pubmed-meshheading:12183454-Chloride Channels, pubmed-meshheading:12183454-Chlorides, pubmed-meshheading:12183454-DNA Primers, pubmed-meshheading:12183454-Electrophysiology, pubmed-meshheading:12183454-HeLa Cells, pubmed-meshheading:12183454-Humans, pubmed-meshheading:12183454-Immunoblotting, pubmed-meshheading:12183454-In Situ Hybridization, pubmed-meshheading:12183454-Mutagenesis, Site-Directed, pubmed-meshheading:12183454-Oligonucleotides, Antisense, pubmed-meshheading:12183454-Oocytes, pubmed-meshheading:12183454-Patch-Clamp Techniques, pubmed-meshheading:12183454-Protein Binding, pubmed-meshheading:12183454-RNA, Complementary, pubmed-meshheading:12183454-RNA, Messenger, pubmed-meshheading:12183454-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:12183454-Time Factors, pubmed-meshheading:12183454-Transfection, pubmed-meshheading:12183454-Xenopus, pubmed-meshheading:12183454-Xenopus laevis
pubmed:year
2002
pubmed:articleTitle
ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl- channels and volume regulation in HeLa cells and Xenopus laevis oocytes.
pubmed:affiliation
Instituto de Ciencias Biomédicas, Facultad de Medicina Universidad de Chile, Santiago 6530499, Chile.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't