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Titolo:
BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells
Autore:
de Marco, MD; Kremer, L; Albar, JP; Martinez-Menarguez, JA; Ballesta, J; Garcia-Lopez, MA; Marazuela, M; Puertollano, R; Alonso, MA;
Indirizzi:
Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 o Ochoa, E-28049 Madrid, Spain CSIC, Ctr Nacl Biotecnol, Dept Immunol & Oncol, E-28049 Madrid, Spain CSIC Madrid Spain E-28049 l, Dept Immunol & Oncol, E-28049 Madrid, Spain Univ Murcia, Fac Med, Dept Cellular Biol, E-30071 Murcia, Spain Univ Murcia Murcia Spain E-30071 pt Cellular Biol, E-30071 Murcia, Spain Hosp Princesa, Dept Endocrinol, Madrid, Spain Hosp Princesa Madrid Spain osp Princesa, Dept Endocrinol, Madrid, Spain
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 276, anno: 2001,
pagine: 23009 - 23017
SICI:
0021-9258(20010622)276:25<23009:BANRPO>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANS-GOLGI NETWORK; DARBY CANINE KIDNEY; APICAL TRANSPORT; PLASMA-MEMBRANE; MDCK CELLS; ANCHORED PROTEINS; CHOLESTEROL; EXPRESSION; COMPONENT; VESICLES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Alonso, MA Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 28049 Madrid, Spain
Citazione:
M.D. de Marco et al., "BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells", J BIOL CHEM, 276(25), 2001, pp. 23009-23017

Abstract

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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Documento generato il 09/07/20 alle ore 12:11:22