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Heme oxygenase 1 expression induced by IL‐10 requires STAT‐3 and phosphoinositol‐3 kinase and is inhibited by lipopolysaccharide

Heme‐oxygenase 1 (HO‐1) is a stress‐response protein with anti‐inflammatory activity. This study has examined the regulation of HO‐1 expression by the anti‐inflammatory factor, interleukin (IL)‐10 and whether HO‐1 could account for the function of the cytokine. IL‐10‐induced expression of HO‐1 required the activation of signal transducer and activator of transcription (STAT)‐3 but not p38 mitogen‐activated protein kinase. However, expression of HO‐1 also required the activation of the phosphatidylinositol‐3 kinase pathway, a signaling mechanism not required for the anti‐inflammatory activity of IL‐10. Moreover, induction of HO‐1 expression was not restricted to IL‐10, as IL‐6, a cytokine known to activate STAT‐3, could also induce the protein. In human macrophages, lipopolysaccharide inhibited HO‐1 expression induced by IL‐10 Also, inhibition of HO‐1 activity by the specific inhibitor zinc‐II‐protoporphyrin‐IX had no effect on the anti‐inflammatory function of IL‐10. In summary, although IL‐10 does regulate HO‐1 expression, it does not appear to play a significant role in the anti‐inflammatory activity of the cytokine.