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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-4-7
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pubmed:abstractText |
In cholinergic neurons, high-affinity choline uptake in presynaptic terminals is the rate-limiting step in acetylcholine synthesis. Using information provided by the Caenorhabditis elegans Genome Project, we cloned a cDNA encoding the high-affinity choline transporter from C. elegans (cho-1). We subsequently used this clone to isolate the corresponding cDNA from rat (CHT1). CHT1 is not homologous to neurotransmitter transporters, but is homologous to members of the Na+-dependent glucose transporter family. Expression of CHT1 mRNA is restricted to cholinergic neurons. The characteristics of CHT1-mediated choline uptake essentially match those of high-affinity choline uptake in rat brain synaptosomes.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Hemicholinium 3,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Uptake Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/choline transporter
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-6256
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
120-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10649566-Amino Acid Sequence,
pubmed-meshheading:10649566-Animals,
pubmed-meshheading:10649566-Binding, Competitive,
pubmed-meshheading:10649566-CHO Cells,
pubmed-meshheading:10649566-Caenorhabditis elegans,
pubmed-meshheading:10649566-Carrier Proteins,
pubmed-meshheading:10649566-Cell Membrane,
pubmed-meshheading:10649566-Choline,
pubmed-meshheading:10649566-Cloning, Molecular,
pubmed-meshheading:10649566-Cricetinae,
pubmed-meshheading:10649566-DNA, Complementary,
pubmed-meshheading:10649566-Hemicholinium 3,
pubmed-meshheading:10649566-Membrane Transport Proteins,
pubmed-meshheading:10649566-Molecular Sequence Data,
pubmed-meshheading:10649566-Monosaccharide Transport Proteins,
pubmed-meshheading:10649566-Neurons,
pubmed-meshheading:10649566-Neurotransmitter Uptake Inhibitors,
pubmed-meshheading:10649566-Oocytes,
pubmed-meshheading:10649566-Organ Specificity,
pubmed-meshheading:10649566-Phylogeny,
pubmed-meshheading:10649566-RNA, Messenger,
pubmed-meshheading:10649566-Rats,
pubmed-meshheading:10649566-Sequence Homology, Amino Acid,
pubmed-meshheading:10649566-Sodium
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pubmed:year |
2000
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pubmed:articleTitle |
Identification and characterization of the high-affinity choline transporter.
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pubmed:affiliation |
Department of Neurochemistry, Faculty of Medicine, University of Tokyo and CREST of Japan Science and Technology Corporation, Bunkyo-ku, Tokyo 113-0033, Japan. okuda@m.u-tokyo.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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