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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-2-20
pubmed:abstractText
Acidic extracellular solution activates transient H(+)-gated currents in dorsal root ganglion (DRG) neurons. The biophysical properties of three degenerin/epithelial sodium (DEG/ENaC) channel subunits (BNC1, ASIC, and DRASIC), and their expression in DRG, suggest that they might underlie these H(+)-gated currents and function as sensory transducers. However, it is uncertain which of these DEG/ENaC subunits generate the currents, and whether they function as homomultimers or heteromultimers. We found that the biophysical properties of transient H(+)-gated currents from medium to large mouse DRG neurons differed from BNC1, ASIC, or DRASIC expressed individually, but were reproduced by coexpression of the subunits together. To test the contribution of each subunit, we studied DRG from three strains of mice, each bearing a targeted disruption of BNC1, ASIC, or DRASIC. Deletion of any one subunit did not abolish H(+)-gated currents, but altered currents in a manner consistent with heteromultimerization of the two remaining subunits. These data indicate that combinations of two or more DEG/ENaC subunits coassemble as heteromultimers to generate transient H(+)-gated currents in mouse DRG neurons.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10222339, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10457052, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10764638, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10772247, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10798398, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10821274, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10829030, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10842183, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10852210, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-10923674, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11069180, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11082481, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11120882, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11306621, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11353858, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11457851, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11528414, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11588175, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-11754838, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-1726795, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-6275299, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-6970348, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-7762608, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-8107805, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-8626462, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-8631835, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9037075, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9062189, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9074782, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9261094, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9360943, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9368048, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9687356, http://linkedlifedata.com/resource/pubmed/commentcorrection/11854527-9707631
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2338-43
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11854527-Animals, pubmed-meshheading:11854527-COS Cells, pubmed-meshheading:11854527-Cloning, Molecular, pubmed-meshheading:11854527-DNA, Complementary, pubmed-meshheading:11854527-Electrophysiology, pubmed-meshheading:11854527-Epithelial Sodium Channel, pubmed-meshheading:11854527-Ganglia, Spinal, pubmed-meshheading:11854527-Hydrogen, pubmed-meshheading:11854527-Hydrogen-Ion Concentration, pubmed-meshheading:11854527-Ion Channels, pubmed-meshheading:11854527-Mice, pubmed-meshheading:11854527-Mice, Knockout, pubmed-meshheading:11854527-Nerve Tissue Proteins, pubmed-meshheading:11854527-Neurons, pubmed-meshheading:11854527-Neurons, Afferent, pubmed-meshheading:11854527-Protein Binding, pubmed-meshheading:11854527-RNA, Messenger, pubmed-meshheading:11854527-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11854527-Sodium Channels, pubmed-meshheading:11854527-Time Factors
pubmed:year
2002
pubmed:articleTitle
Heteromultimers of DEG/ENaC subunits form H+-gated channels in mouse sensory neurons.
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