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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-7-10
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pubmed:abstractText |
We report that long-chain poly-L-glutamine forms cation-selective channels when incorporated into artificial planar lipid bilayer membranes. The channel was permeable to alkali cations and H(+) ions and virtually impermeable to anions; the selectivity sequence based on the single-channel conductance was H(+) >> Cs(+) > K(+) > Na(+). The cation channel was characterized by long-lived open states (often lasting for several minutes to tens of minutes) interrupted by brief closings. The appearance of the channel depended critically on the length of polyglutamine chains; ion channels were observed with 40-residue stretches, whereas no significant conductance changes were detected with 29-residue tracts. The channel-forming threshold length of poly-L-glutamine was thus between 29 and 40 residues. A molecular mechanics calculation suggests a mu-helix (. Biophys. J. 69:1130-1141) as a candidate molecular structure of the channel. The channel-forming nature of long-chain poly-L-glutamine may provide a clue to the elucidation of the pathogenetic mechanism of the polyglutamine diseases, a group of inherited neurodegenerative disorders including Huntington's disease.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10827970-10508741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10827970-10518935,
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2892-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10827970-Cations, Monovalent,
pubmed-meshheading:10827970-Humans,
pubmed-meshheading:10827970-Hydrogen-Ion Concentration,
pubmed-meshheading:10827970-Ion Channels,
pubmed-meshheading:10827970-Lipid Bilayers,
pubmed-meshheading:10827970-Liposomes,
pubmed-meshheading:10827970-Models, Molecular,
pubmed-meshheading:10827970-Neurodegenerative Diseases,
pubmed-meshheading:10827970-Peptides,
pubmed-meshheading:10827970-Protein Structure, Secondary,
pubmed-meshheading:10827970-Trinucleotide Repeat Expansion
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pubmed:year |
2000
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pubmed:articleTitle |
Poly-L-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases.
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pubmed:affiliation |
Research Institute of Neurodegenerative Diseases, Sendai 980-0871, Japan. monoi@biology.is.tohoku.ac.jp
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pubmed:publicationType |
Journal Article
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