Source:http://linkedlifedata.com/resource/pubmed/id/11294831
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
25
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pubmed:dateCreated |
2001-6-18
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pubmed:abstractText |
The MAL proteolipid, an integral protein present in glycolipid- and cholesterol-enriched membrane (GEM) rafts, is an element of the machinery necessary for apical sorting in polarized epithelial Madin-Darby canine kidney cells. MAL was the first member identified of an extended family of proteins that have significant overall sequence identity. In this study we have used a newly generated monoclonal antibody to investigate an unedited member of this family, named BENE, which was found to be expressed in endothelial-like ECV304 cells and normal human endothelium. Human BENE was characterized as a proteolipid protein predominantly present in GEM rafts in ECV304 cells. Coimmunoprecipitation experiments revealed that BENE interacted with caveolin-1. Confocal immunofluorescence and electron microscopic analyses indicated that BENE mainly accumulated into intracellular vesicular/tubular structures that partially colocalize with internal caveolin-1. In response to cell surface cholesterol oxidation, BENE redistributed to the dilated vesicular structures that concentrate most of the caveolin-1 originally on the cell surface. After cessation of cholesterol oxidation, a detectable fraction of the BENE molecules migrated to the plasmalemma accompanying caveolin-1 and then returned progressively to its steady state distribution. Together, these features highlight the BENE proteolipid as being an element of the machinery for raft-mediated trafficking in endothelial cells.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/CAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/MALL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids
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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 |
22
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23009-17
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pubmed:dateRevised |
2010-9-20
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pubmed:meshHeading |
pubmed-meshheading:11294831-Amino Acid Sequence,
pubmed-meshheading:11294831-Animals,
pubmed-meshheading:11294831-Antibodies, Monoclonal,
pubmed-meshheading:11294831-Carrier Proteins,
pubmed-meshheading:11294831-Cattle,
pubmed-meshheading:11294831-Caveolin 1,
pubmed-meshheading:11294831-Caveolins,
pubmed-meshheading:11294831-Cell Line,
pubmed-meshheading:11294831-Cholesterol,
pubmed-meshheading:11294831-Endothelium,
pubmed-meshheading:11294831-Gene Expression Regulation,
pubmed-meshheading:11294831-Humans,
pubmed-meshheading:11294831-Membrane Proteins,
pubmed-meshheading:11294831-Microscopy, Immunoelectron,
pubmed-meshheading:11294831-Molecular Sequence Data,
pubmed-meshheading:11294831-Oxidation-Reduction,
pubmed-meshheading:11294831-Proteolipids,
pubmed-meshheading:11294831-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells.
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pubmed:affiliation |
Centro de Biologia Molecular "Severo Ochoa," Universidad Autónoma de Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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