| pubmed-article:1383206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1383206 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:1383206 | lifeskim:mentions | umls-concept:C0040578 | lld:lifeskim |
| pubmed-article:1383206 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1383206 | lifeskim:mentions | umls-concept:C0055363 | lld:lifeskim |
| pubmed-article:1383206 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:1383206 | pubmed:issue | 29 | lld:pubmed |
| pubmed-article:1383206 | pubmed:dateCreated | 1992-11-18 | lld:pubmed |
| pubmed-article:1383206 | pubmed:abstractText | We characterized the electrophysiological properties of a chloride channel protein isolated from bovine trachea after incorporation into planar lipid bilayers, and studied the effects of thiol-modulating agents on channel regulation both in bilayers and vesicular iodide uptake studies. Our experiments showed that this protein formed perfectly anion-selective channels in the bilayer, with an anion permeability sequence of I- (2.1) > NO3- (1.7) > Br- (1.2) > Cl- (1.0). The conductance of this channel was 25-30 picosiemens in 150 mM Cl-, and saturated with increasing chloride concentration. This channel could be completely inhibited by 4,4'-bis(isothiocyano)-2,2'-stilbenedisulfonate. Immunoblot analysis, using polyclonal antibodies (anti-p38), revealed one major band at 140 kDa. Upon reduction with dithiothreitol, 64- and 38-kDa polypeptides were observed. Functional experiments showed that reduction was accompanied by loss of 125I- uptake and single-channel activity. In the presence of dithiothreitol, only the low molecular mass protein forms (64 and 38 kDa) were detected by anti-p38 antibodies on Western blots. Cross-linking of S-S bonds with Cu(2+)-o-phenanthroline led to activation of chloride channels in vesicles and bilayers. Over-aggregation of chloride channels by this S-S cross-linking reagent caused inhibition of 125I- uptake by 80-100% and the abolishment of single-channel activity. We propose that the native chloride channel from bovine trachea can exist in vivo in different structural and functional forms depending upon its thiol-disulfide oxidation reduction status. The oxidized form has a molecular mass of 140 kDa and represents a fully active chloride channel. Inactivation of this channel might occur by over-aggregation of protein subunits, or by dissociation of the 140-kDa subunit by disulfide bond reduction. | lld:pubmed |
| pubmed-article:1383206 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1383206 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1383206 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1383206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1383206 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1383206 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1383206 | pubmed:author | pubmed-author:BenosD JDJ | lld:pubmed |
| pubmed-article:1383206 | pubmed:author | pubmed-author:CoxC ECE2nd | lld:pubmed |
| pubmed-article:1383206 | pubmed:author | pubmed-author:LatorreRR | lld:pubmed |
| pubmed-article:1383206 | pubmed:author | pubmed-author:FullerC MCM | lld:pubmed |
| pubmed-article:1383206 | pubmed:author | pubmed-author:ArrateM PMP | lld:pubmed |
| pubmed-article:1383206 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1383206 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1383206 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1383206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1383206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1383206 | pubmed:pagination | 20630-7 | lld:pubmed |
| pubmed-article:1383206 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1383206 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1383206 | pubmed:articleTitle | Functional reconstitution of a chloride channel protein from bovine trachea. | lld:pubmed |
| pubmed-article:1383206 | pubmed:affiliation | Department of Physiology and Biophysics, University of Alabama, Birmingham 35294. | lld:pubmed |
| pubmed-article:1383206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1383206 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1383206 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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