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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5733
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pubmed:dateCreated |
2005-7-15
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pubmed:abstractText |
Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.
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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/4,4'-Diisothiocyanostilbene-2,2'-Dis...,
http://linkedlifedata.com/resource/pubmed/chemical/APOL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Anions,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Colicins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
pubmed-author:BrasseurRobertR,
pubmed-author:HombléFabriceF,
pubmed-author:JacquetAlainA,
pubmed-author:LinsLaurenceL,
pubmed-author:NolanDerek PDP,
pubmed-author:Pérez-MorgaDavidD,
pubmed-author:Paturiaux-HanocqFrançoiseF,
pubmed-author:PaysAnnetteA,
pubmed-author:PaysEtienneE,
pubmed-author:PoelvoordePhilippeP,
pubmed-author:TebabiPatriciaP,
pubmed-author:VanhammeLucL,
pubmed-author:VanhollebekeBenoitB
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
469-72
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pubmed:dateRevised |
2007-8-13
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pubmed:meshHeading |
pubmed-meshheading:16020735-4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid,
pubmed-meshheading:16020735-Amino Acid Sequence,
pubmed-meshheading:16020735-Animals,
pubmed-meshheading:16020735-Anions,
pubmed-meshheading:16020735-Apolipoproteins,
pubmed-meshheading:16020735-Cells, Immobilized,
pubmed-meshheading:16020735-Chlorides,
pubmed-meshheading:16020735-Colicins,
pubmed-meshheading:16020735-Escherichia coli,
pubmed-meshheading:16020735-Humans,
pubmed-meshheading:16020735-Intracellular Membranes,
pubmed-meshheading:16020735-Ion Channels,
pubmed-meshheading:16020735-Lipid Bilayers,
pubmed-meshheading:16020735-Lipoproteins, HDL,
pubmed-meshheading:16020735-Lysosomes,
pubmed-meshheading:16020735-Models, Molecular,
pubmed-meshheading:16020735-Molecular Sequence Data,
pubmed-meshheading:16020735-Mutation,
pubmed-meshheading:16020735-Permeability,
pubmed-meshheading:16020735-Protein Conformation,
pubmed-meshheading:16020735-Protein Structure, Secondary,
pubmed-meshheading:16020735-Protein Structure, Tertiary,
pubmed-meshheading:16020735-Recombinant Proteins,
pubmed-meshheading:16020735-Trypanosoma brucei brucei
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pubmed:year |
2005
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pubmed:articleTitle |
Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes.
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pubmed:affiliation |
Laboratory of Molecular Parasitology, IBMM, Université Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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