Upregulation of pentraxin-3 in human endothelial cells after lysophosphatidic acid exposure

Cindy Gustin, Edouard Delaive, Marc Dieu, Damien Calay, Martine Raes

Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs


Objective: The earliest event in atherogenesis appears to be endothelium dysfunction. Lysophosphatidic acid (LPA), one of the major bioactive lipid components of oxidized low-density lipoproteins (oxLDL), can cause the activation of endothelial cells (ECs), which start to secrete multiple proinflammatory polypeptides/proteins. The purpose of this study was to better document the proatherogenic properties of LPA using a subproteomic approach focused on the secretome of LPA-treated ECs. Methods and Results: The secretome of LPA-treated ECs was analyzed using the 2D-DIGE approach. Among the 20 spots displaying significant variations of abundance compared with the control cells, we identified pentraxin-3 by mass spectrometry. Pentraxin-3 upregulation was confirmed at the mRNA and protein level, both on immortalized and primary ECs. LPA- but also oxLDL-induced pentraxin-3 upregulation was reduced in the presence of an antagonist of the LPA-receptors and largely dependent on NFkB activation. Finally, we demonstrated, for the first time, the chemotactic activity of pentraxin-3 on human THP-1 monocytes by using a chemotaxis assay. Conclusions: Our findings favor the proatherogenic role of LPA, a bioactive lipid produced by activated platelets and present in oxLDL, because it enhances pentraxin-3 secretion that could contribute to the accumulation of monocytes in the atherosclerotic lesion. © 2008 American Heart Association, Inc.

langue originaleAnglais
Pages (de - à)491-497
Nombre de pages7
journalArteriosclerosis, Thrombosis, and Vascular Biology
Numéro de publication3
Les DOIs
Etat de la publicationPublié - 1 mars 2008

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