Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/104524
Title: Activation of Endothelial Nitric Oxide (eNOS) Occurs Through Different Membrane Domains in Endothelial Cells.
Author: Tran, Jason
Magenau, Astrid
Rodriguez, Macarena
Rentero Alfonso, Carles
Royo, Teresa
Enrich Bastús, Carles
Thomas, Shane R
Grewal, Thomas
Gaus, Katharina
Keywords: Membranes (Biologia)
Colesterol
Proteïnes de membrana
Fosforilació
Esteroides
Òxid nítric
Membranes (Biology)
Cholesterol
Membrane proteins
Phosphorylation
Steroids
Nitric oxide
Issue Date: 15-Mar-2016
Publisher: Public Library of Science (PLoS)
Abstract: Endothelial cells respond to a large range of stimuli including circulating lipoproteins, growth factors and changes in haemodynamic mechanical forces to regulate the activity of endo- thelial nitric oxide synthase (eNOS) and maintain blood pressure. While many signalling pathways have been mapped, the identities of membrane domains through which these sig- nals are transmitted are less well characterized. Here, we manipulated bovine aortic endo- thelial cells (BAEC) with cholesterol and the oxysterol 7-ketocholesterol (7KC). Using a range of microscopy techniques including confocal, 2-photon, super-resolution and electron microscopy, we found that sterol enrichment had differential effects on eNOS and caveolin- 1 (Cav1) colocalisation, membrane order of the plasma membrane, caveolae numbers and Cav1 clustering. We found a correlation between cholesterol-induced condensation of the plasma membrane and enhanced high density lipoprotein (HDL)-induced eNOS activity and phosphorylation suggesting that cholesterol domains, but not individual caveolae, mediate HDL stimulation of eNOS. Vascular endothelial growth factor (VEGF)-induced and shear stress-induced eNOS activity was relatively independent of membrane order and may be predominantly controlled by the number of caveolae on the cell surface. Taken together, our data suggest that signals that activate and phosphorylate eNOS are transmit- ted through distinct membrane domains in endothelial cells
Note: Reproducció del document publicat a: https://doi.org/10.1371/journal.pone.0151556
It is part of: PLoS One, 2016, vol. 11, num. 3, p. e0151556
Related resource: https://doi.org/10.1371/journal.pone.0151556
URI: http://hdl.handle.net/2445/104524
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Biomedicina)
Articles publicats en revistes (IDIBAPS: Institut d'investigacions Biomèdiques August Pi i Sunyer)

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