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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2001-6-18
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23009-17
pubmed:dateRevised
2010-9-20
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
pubmed:year
2001
pubmed:articleTitle
BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells.
pubmed:affiliation
Centro de Biologia Molecular "Severo Ochoa," Universidad Autónoma de Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't