IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

• Published in: European Journal of Immunology 2007-06, Vol.37 (6), p.1642-1652
• Main Authors: Berry, Antoine, Balard, Patricia, Coste, Agnès, Olagnier, David, Lagane, Céline, Authier, Hélène, Benoit‐Vical, Françoise, Lepert, Jean‐Claude, Séguéla, Jean‐Paul, Magnaval, Jean‐François, Chambon, Pierre, Metzger, Daniel, Desvergne, Béatrice, Wahli, Walter, Auwerx, Johan, Pipy, Bernard
• Format: Article
• Language: English
• Subjects: CD36; Human monocytes; IL‐13; Nuclear receptors; Phagocytosis; Plasmodium
• ISSN: 0014-2980; 1521-4141; 1365-2567
• DOI: 10.1002/eji.200636625

The class B scavenger receptor CD36 is a component of the pattern recognition receptors on monocytes that recognizes a variety of molecules. CD36 expression in monocytes depends on exposure to soluble mediators. We demonstrate here that CD36 expression is induced in human monocytes following exposure to IL‐13, a Th2 cytokine, via the peroxisome proliferator‐activated receptor (PPAR)γ pathway. Induction of CD36 protein was paralleled by an increase in CD36 mRNA. The PPARγ pathway was demonstrated using transfection of a PPARγ expression plasmid into the murine macrophage cell line RAW264.7, expressing very low levels of PPARγ, and in peritoneal macrophages from PPARγ‐conditional null mice. We also show that CD36 induction by IL‐13 via PPARγ is dependent on phospholipase A2 activation and that IL‐13 induces the production of endogenous 15‐deoxy‐Δ12,14‐prostaglandin J2, an endogenous PPARγ ligand, and its nuclear localization in human monocytes. Finally, we demonstrate that CD36 and PPARγ are involved in IL‐13‐mediated phagocytosis of Plasmodium falciparum‐parasitized erythrocytes. These results reveal a novel role for PPARγ in the alternative activation of monocytes by IL‐13, suggesting that endogenous PPARγ ligands, produced by phospholipase A2 activation, could contribute to the biochemical and cellular functions of CD36.