Source:http://linkedlifedata.com/resource/pubmed/id/20658517
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-10-27
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pubmed:abstractText |
We investigated the possible functional- and physical protein-interactions between two airway Cl(-) channels, SLC26A9 and CFTR. Bronchial CFBE41o- cell lines expressing CFTR(WT) or CFTR(?F508) were transduced with SLC26A9. Immunoblots identified a migrating band corresponding to SLC26A9 present in whole-cell lysates as on apical membrane of cells grown on polarized filters. CFTR levels were increased by the presence of SLC26A9 in both CFTR(WT) and CFTR(?F508) cell lines. In CFBE41o- cells and CFBE41o-/CFTR(WT) cells transduced with SLC26A9, currents associated to the protein expression were not detected. However, the forskolin (FK)-stimulated currents were enhanced in SLC26A9-transduced cells compared to control cells. Therefore, the presence of SLC26A9 resulted in an increase in CFTR activity (same % of CFTR((inh)-172) or GlyH-101 inhibition in both groups). In CFBE41o-/CFTR(?F508) cells transduced with SLC26A9 (at 27°C), a current associated to the protein expression was also lacking. FK-stimulated currents and level of CFTR((inh)-172) inhibition were not different in both groups. The presence of SLC26A9 in Xenopus oocytes expressing CFTR also enhanced the FK-stimulated currents as compared to oocytes expressing CFTR alone. This stimulation was mostly linked to CFTR. An enhancement of FK-stimulated currents was not found in oocytes co-expressing SLC26A9 and CFTR(?F508). In conclusion, in both protein expression systems used, SLC26A9 stimulates CFTR activity but not that of CFTR(?F508). Our co-immunoprecipitation studies demonstrate a physical interaction between both anion channels. We propose as an alternative hypothesis (not exclusive) to the known SLC26A9-STAS domain/CFTR interaction, that SLC26A9 favors the biogenesis and/or stabilization of CFTR, leading to stimulated currents.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Cystic Fibrosis Transmembrane...,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/SLC26A9 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1097-4652
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
212-23
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pubmed:meshHeading |
pubmed-meshheading:20658517-Animals,
pubmed-meshheading:20658517-Antiporters,
pubmed-meshheading:20658517-Bronchi,
pubmed-meshheading:20658517-Cell Line,
pubmed-meshheading:20658517-Chlorides,
pubmed-meshheading:20658517-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:20658517-Forskolin,
pubmed-meshheading:20658517-Gene Expression Regulation,
pubmed-meshheading:20658517-Humans,
pubmed-meshheading:20658517-Patch-Clamp Techniques,
pubmed-meshheading:20658517-Xenopus laevis
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pubmed:year |
2011
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pubmed:articleTitle |
SLC26A9 stimulates CFTR expression and function in human bronchial cell lines.
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pubmed:affiliation |
Laboratoire de Biologie et Physiopathologie des Systèmes Intégrés, Université de Nice-Sophia Antipolis, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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