| pubmed-article:19926787 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19926787 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:19926787 | lifeskim:mentions | umls-concept:C0052088 | lld:lifeskim |
| pubmed-article:19926787 | lifeskim:mentions | umls-concept:C0596019 | lld:lifeskim |
| pubmed-article:19926787 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
| pubmed-article:19926787 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19926787 | pubmed:dateCreated | 2010-1-18 | lld:pubmed |
| pubmed-article:19926787 | pubmed:abstractText | Adenovirus expressing ClC-3 (Ad-ClC-3) induces Cl(-)/H(+) antiport current (I(ClC-3)) in HEK293 cells. The outward rectification and time dependence of I(ClC-3) closely resemble an endogenous HEK293 cell acid-activated Cl(-) current (ICl(acid)) seen at extracellular pH <or= 5.5. ICl(acid) was present in smooth muscle cells from wild-type but not ClC-3 null mice. We therefore sought to determine whether these currents were related. ICl(acid) was larger in cells expressing Ad-ClC-3. Protons shifted the reversal potential (E(rev)) of I(ClC-3) between pH 8.2 and 6.2, but not pH 6.2 and 5.2, suggesting that Cl(-) and H(+) transport become uncoupled at low pH. At pH 4.0 E(rev) was completely Cl(-) dependent (55.8 +/- 2.3 mV/decade). Several findings linked ClC-3 with native ICl(acid); 1) RNA interference directed at ClC-3 message reduced native ICl(acid); 2) removal of the extracellular "fast gate" (E224A) produced large currents that were pH-insensitive; and 3) wild-type I(ClC-3) and ICl(acid) were both inhibited by (2-sulfonatoethyl)methanethiosulfonate (MTSES; 10-500 microm)-induced alkanethiolation at exposed cysteine residues. However, a ClC-3 mutant lacking four extracellular cysteine residues (C103_P130del) was completely resistant to MTSES. C103_P130del currents were still acid-activated, but could be distinguished from wild-type I(ClC-3) and from native ICl(acid) by a much slower response to low pH. Thus, ClC-3 currents are activated by protons and ClC-3 protein may account for native ICl(acid). Low pH uncouples Cl(-)/H(+) transport so that at pH 4.0 ClC-3 behaves as an anion-selective channel. These findings have important implications for the biology of Cl(-)/H(+) antiporters and perhaps for pH regulation in highly acidic intracellular compartments. | lld:pubmed |
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| pubmed-article:19926787 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19926787 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19926787 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19926787 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19926787 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19926787 | pubmed:author | pubmed-author:VolkKenneth... | lld:pubmed |
| pubmed-article:19926787 | pubmed:author | pubmed-author:LambFred SFS | lld:pubmed |
| pubmed-article:19926787 | pubmed:author | pubmed-author:MatsudaJames... | lld:pubmed |
| pubmed-article:19926787 | pubmed:author | pubmed-author:FilaliMohamme... | lld:pubmed |
| pubmed-article:19926787 | pubmed:author | pubmed-author:CollinsMalia... | lld:pubmed |
| pubmed-article:19926787 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19926787 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:19926787 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:19926787 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19926787 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19926787 | pubmed:pagination | 2569-79 | lld:pubmed |
| pubmed-article:19926787 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
| pubmed-article:19926787 | pubmed:meshHeading | pubmed-meshheading:19926787... | lld:pubmed |
| pubmed-article:19926787 | pubmed:meshHeading | pubmed-meshheading:19926787... | lld:pubmed |
| pubmed-article:19926787 | pubmed:meshHeading | pubmed-meshheading:19926787... | lld:pubmed |
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