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rdf:type |
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lifeskim:mentions |
umls-concept:C0007447,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0028630,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0086418,
umls-concept:C0205409,
umls-concept:C0225700,
umls-concept:C0439799,
umls-concept:C0521449
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pubmed:issue |
6
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pubmed:dateCreated |
2004-11-8
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pubmed:abstractText |
Here we report a 26- to 29-pS cation channel abundantly expressed in freshly isolated and primary cultured type II cells from rat or healthy human lungs. The channel was never spontaneously active in cell-attached patches but could be activated by cell permeabilization with beta-escin. Excised patch-clamp experiments revealed activation by Ca(2+) concentrations at the cytoplasmic side in the micromolar range. High concentrations of amiloride (>10 microM) at the extracellular side did not inhibit. The channel was equally permeable for K(+) and Na(+) but was essentially impermeable for Cl(-), Ca(2+), and Mg(2+). It was blocked by adenosine nucleotides (cytoplasmic side) with the following order of potency: AMP approximately ADP (EC(50) </= 10 microM) > ATP >> adenosine >> cyclic AMP. The blocking effect of ATP was reproduced by its nonhydrolyzable analogs AMPPNP or ATP-gamma-S. GTP did not inhibit. Cd(2+) blocked the channel with an EC(50) approximately 55.5 nM. We conclude that type II cells express a Ca(2+)-dependent, nucleotide-inhibited, nonselective, and Ca(2+)-impermeable cation channel (NSC(Ca/AMP)) with tonically suppressed activity. RT-PCR confirmed expression of TRPM4b, a channel with functional characteristics almost identical with NSC(Ca/AMP). Potential physiological roles are discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cadmium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Strontium
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1040-0605
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
287
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
L1284-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15321785-Adenosine Diphosphate,
pubmed-meshheading:15321785-Adenosine Monophosphate,
pubmed-meshheading:15321785-Adenosine Triphosphate,
pubmed-meshheading:15321785-Animals,
pubmed-meshheading:15321785-Cadmium,
pubmed-meshheading:15321785-Calcium,
pubmed-meshheading:15321785-Cation Transport Proteins,
pubmed-meshheading:15321785-Cations, Divalent,
pubmed-meshheading:15321785-Cell Adhesion,
pubmed-meshheading:15321785-Cytosol,
pubmed-meshheading:15321785-DNA Primers,
pubmed-meshheading:15321785-Humans,
pubmed-meshheading:15321785-Male,
pubmed-meshheading:15321785-Manganese,
pubmed-meshheading:15321785-Membrane Potentials,
pubmed-meshheading:15321785-Pulmonary Alveoli,
pubmed-meshheading:15321785-Rats,
pubmed-meshheading:15321785-Rats, Sprague-Dawley,
pubmed-meshheading:15321785-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15321785-Strontium
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pubmed:year |
2004
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pubmed:articleTitle |
Inhibition by cytoplasmic nucleotides of a new cation channel in freshly isolated human and rat type II pneumocytes.
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pubmed:affiliation |
Department of Physiology, Medical University of Innsbruck, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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