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Christoffersen, Christina; Obinata, Hideru; Kumaraswamy, Sunil B; Galvani, Sylvain; Ahnström, Josefin; Sevvana, Madhumati; Egerer-Sieber, Claudia; Muller, Yves A; Hla, Timothy; Nielsen, Lars B; Dahlbäck, Björn
Proceedings of the National Academy of Sciences - PNAS, 06/2011, Volume: 108, Issue: 23Journal Article
Protection of the endothelium is provided by circulating sphingosine-1-phosphate (S1P), which maintains vascular integrity. We show that HDL-associated S1P is bound specifically to both human and murine apolipoprotein M (apoM). Thus, isolated human ApoM⺠HDL contained S1P, whereas ApoMâ» HDL did not. Moreover, HDL in Apomâ»/â» mice contains no S1P, whereas HDL in transgenic mice overexpressing human apoM has an increased S1P content. The 1.7-à structure of the S1P-human apoM complex reveals that S1P interacts specifically with an amphiphilic pocket in the lipocalin fold of apoM. Human ApoM⺠HDL induced S1Pâ receptor internalization, downstream MAPK and Akt activation, endothelial cell migration, and formation of endothelial adherens junctions, whereas apoMâ» HDL did not. Importantly, lack of S1P in the HDL fraction of Apomâ»/â» mice decreased basal endothelial barrier function in lung tissue. Our results demonstrate that apoM, by delivering S1P to the S1Pâ receptor on endothelial cells, is a vasculoprotective constituent of HDL.
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