Source:http://linkedlifedata.com/resource/pubmed/id/12682043
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
25
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pubmed:dateCreated |
2003-6-16
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pubmed:abstractText |
The mechanism for the cellular extrusion of sulfated conjugates is still unknown. In the present study, we investigated whether human wild type ABCG2 transports estrone 3-sulfate (E1S) using membrane vesicles from cDNA-transfected mouse lymphoma cell line (P388 cells). The uptake of [3H]E1S into ABCG2-expressing membrane vesicles was stimulated by ATP, and the Km value for [3H]E1S was determined to be 16.6 microm. The ABCG2-mediated transport of [3H]E1S was potently inhibited by SN-38 and many sulfate conjugates but not by glucuronide and glutathione conjugates or other anionic compounds. Other sulfate conjugates such as [3H]dehydroepiandrosterone sulfate (DHEAS) and [35S]4-methylumbelliferone sulfate (Km = 12.9 microm) and [35S]6-hydroxy-5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)benzothiazole (E3040) sulfate (Km = 26.9 microm) were also transported by ABCG2. Although [3H]methotrexate, [3H]17beta-estradiol-17beta-D-glucuronide, [3H]2,4-dinitrophenyl-S-glutathione, and [14C]4-methylumbelliferone glucuronide were transported by ABCG2, this took place to a much lesser extent compared with [3H]E1S. It was suggested that ABCG2 preferentially transports sulfate conjugates and that E1S and DHEAS are the potential physiological substrates for this transporter.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ABCG2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Dehydroepiandrosterone Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Steroids,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfuric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Xenobiotics
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22644-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12682043-ATP-Binding Cassette Transporters,
pubmed-meshheading:12682043-Animals,
pubmed-meshheading:12682043-Biological Transport,
pubmed-meshheading:12682043-Dehydroepiandrosterone Sulfate,
pubmed-meshheading:12682043-Drug Resistance, Neoplasm,
pubmed-meshheading:12682043-Humans,
pubmed-meshheading:12682043-Kinetics,
pubmed-meshheading:12682043-Lymphoma,
pubmed-meshheading:12682043-Mice,
pubmed-meshheading:12682043-Neoplasm Proteins,
pubmed-meshheading:12682043-Recombinant Proteins,
pubmed-meshheading:12682043-Steroids,
pubmed-meshheading:12682043-Sulfuric Acids,
pubmed-meshheading:12682043-Transfection,
pubmed-meshheading:12682043-Tumor Cells, Cultured,
pubmed-meshheading:12682043-Xenobiotics
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pubmed:year |
2003
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pubmed:articleTitle |
ABCG2 transports sulfated conjugates of steroids and xenobiotics.
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pubmed:affiliation |
School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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