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            <funder>This work was supported by grants from the Nouvelle Société Française d'Athérosclérose/Sanofi-Aventis (to M.A.Bouhlel), the Région Nord-Pas de Calais/FEDER (ChoMetAlt project), the Fondation Coeur et Artères and theAgence Nationale de la Recherche (AlMHA project). G. Chinetti-Gbaguidi is a recipient of aContrat d'Interface from the CHRU de Lille.</funder>
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                <term xml:lang="sv">11beta-HSDI</term>
                <term xml:lang="sv">PPARgamma</term>
                <term xml:lang="sv">human alternative macrophages</term>
                <term xml:lang="sv">inflammation</term>
                <term xml:lang="sv">GR</term>
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              <classCode scheme="mesh">11-beta-Hydroxysteroid Dehydrogenase Type 1</classCode>
              <classCode scheme="mesh">Cells, Cultured</classCode>
              <classCode scheme="mesh">PPAR gamma</classCode>
              <classCode scheme="mesh">RNA Interference</classCode>
              <classCode scheme="mesh">Receptors, Glucocorticoid</classCode>
              <classCode scheme="mesh">Thiazolidinediones</classCode>
              <classCode scheme="mesh">Time Factors</classCode>
              <classCode scheme="mesh">Transfection</classCode>
              <classCode scheme="mesh">Cortisone</classCode>
              <classCode scheme="mesh">Enzyme Induction</classCode>
              <classCode scheme="mesh">Genes, Reporter</classCode>
              <classCode scheme="mesh">Humans</classCode>
              <classCode scheme="mesh">Hydrocortisone</classCode>
              <classCode scheme="mesh">Inflammation</classCode>
              <classCode scheme="mesh">Interleukin-4</classCode>
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              <p>OBJECTIVE: 11β-Hydroxysteroid dehydrogenase type 1 (11β-HSD1) catalyzes the intracellular reduction of inactive cortisone to active cortisol, the natural ligand activating the glucocorticoid receptor (GR). Peroxisome proliferator- activated receptor-γ (PPARγ) is a nuclear receptor controlling inflammation, lipid metabolism, and the macrophage polarization state. In this study, we investigated the impact of macrophage polarization on the expression and activity of 11β-HSD1 and the role of PPARγ therein. METHODS AND RESULTS: 11β-HSD1 gene expression is higher in proinflammatory M1 and anti-inflammatory M2 macrophages than in resting macrophages, whereas its activity is highest in M2 macrophages. Interestingly, PPARγ activation induces 11β-HSD1 enzyme activity in M2 macrophages but not in resting macrophages or M1 macrophages. Consequently, human M2 macrophages displayed enhanced responsiveness to the 11β-HSD1 substrate cortisone, an effect amplified by PPARγ induction of 11β-HSD1 activity, as illustrated by an increased expression of GR target genes. CONCLUSION: Our data identify a positive cross-talk between PPARγ and GR in human M2 macrophages via the induction of 11β-HSD1 expression and activity.</p>
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