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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2000-7-10
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pubmed:abstractText |
Mammalian sodium/bile acid cotransporters (SBATs) constitute a subgroup of the sodium cotransporter superfamily and function in the enterohepatic circulation of bile acids. They are glycoproteins with an exoplasmic N-terminus, seven or nine transmembrane segments, and a cytoplasmic C-terminus. They exhibit no significant homology with other members of the sodium cotransporter family and there is limited structure/function information available for the SBATs. Membrane-impermeant methanethiosulfonates (MTS) inhibited bile acid transport by alkylation of cysteine 270 (apical SBAT)/266 (basolateral SBAT) that is fully conserved among the sodium/bile acid cotransporters. The accessibility of this residue to MTS reagent is regulated by the natural substrates, sodium and bile acid. In experiments with the apical SBAT, sodium alone increases the reactivity with the thiol reagents as compared to sodium-free medium. In contrast, bile acids protect the SBATs from inactivation, although only in the presence of sodium. The inhibition and protection data suggest that cysteine 270/266 lies in a sodium-sensitive region of the SBATs that is implicated in bile acid transport.
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pubmed:grant |
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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/(2-(trimethylammonium)ethyl)methanet...,
http://linkedlifedata.com/resource/pubmed/chemical/(2-sulfonatoethyl)methanethiosulfona...,
http://linkedlifedata.com/resource/pubmed/chemical/Bile Acids and Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Mesylates,
http://linkedlifedata.com/resource/pubmed/chemical/Organic Anion Transporters...,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/Taurocholic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/sodium-bile acid cotransporter
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6743-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10828993-Amino Acid Sequence,
pubmed-meshheading:10828993-Animals,
pubmed-meshheading:10828993-Bile Acids and Salts,
pubmed-meshheading:10828993-Biological Transport,
pubmed-meshheading:10828993-Carrier Proteins,
pubmed-meshheading:10828993-Cell Line,
pubmed-meshheading:10828993-Enzyme Inhibitors,
pubmed-meshheading:10828993-Humans,
pubmed-meshheading:10828993-Kinetics,
pubmed-meshheading:10828993-Mesylates,
pubmed-meshheading:10828993-Molecular Sequence Data,
pubmed-meshheading:10828993-Mutagenesis, Site-Directed,
pubmed-meshheading:10828993-Organic Anion Transporters, Sodium-Dependent,
pubmed-meshheading:10828993-Sulfhydryl Reagents,
pubmed-meshheading:10828993-Symporters,
pubmed-meshheading:10828993-Taurocholic Acid,
pubmed-meshheading:10828993-Transfection
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pubmed:year |
2000
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pubmed:articleTitle |
Inhibition of the human sodium/bile acid cotransporters by side-specific methanethiosulfonate sulfhydryl reagents: substrate-controlled accessibility of site of inactivation.
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pubmed:affiliation |
University of California at Los Angeles and the Veterans' Affairs Greater Los Angeles Healthcare System, Los Angeles, California 90073, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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