Bruton's tyrosine kinase is required for TLR-dependent heme oxygenase-1 gene activation via Nrf2 in macrophages

J Immunol. 2011 Jul 15;187(2):817-27. doi: 10.4049/jimmunol.1003631. Epub 2011 Jun 15.

Abstract

Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation and provides cytoprotection against oxidative stress by its products carbon monoxide and biliverdin. More recently, HO-1 has also been shown to exert immunomodulatory functions via cell type-specific anti-inflammatory effects in myeloid/macrophage cells. In the current study, it is demonstrated that Bruton's tyrosine kinase (Btk), the gene of which is mutated in the human immunodeficiency X-linked agammaglobulinemia, is involved in the upregulation of HO-1 gene expression via TLR signaling in macrophages. The specific Btk inhibitor LFM-A13 blocked HO-1 induction by the classical TLR4 ligand LPS in cell cultures of RAW264.7 monocytic cells and primary mouse alveolar macrophages. Moreover, upregulation of HO-1 gene expression was abrogated in LPS-stimulated alveolar macrophages from Btk(-/-) mice. Transfection studies with luciferase reporter gene constructs demonstrated that LPS-dependent induction of HO-1 promoter activity was attenuated by pharmacological Btk inhibition and by an overexpressed dominant-negative mutant of Btk. This induction was mediated by the transcription factor Nrf2, which is a master regulator of the antioxidant cellular defense. Accordingly, nuclear translocation of Nrf2 in LPS-treated macrophages was reduced by Btk inhibition. The generation of reactive oxygen species, but not that of NO, was involved in this regulatory pathway. Btk-dependent induction of HO-1 gene expression was also observed upon macrophage stimulation with ligands of TLR2, TLR6, TLR7, and TLR9, suggesting that Btk is required for HO-1 gene activation by major TLR pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agammaglobulinaemia Tyrosine Kinase
  • Agammaglobulinemia / enzymology
  • Agammaglobulinemia / genetics
  • Agammaglobulinemia / immunology
  • Amides / pharmacology
  • Animals
  • Cell Line
  • Cells, Cultured
  • Gene Expression Regulation, Enzymologic / drug effects
  • Gene Expression Regulation, Enzymologic / immunology
  • Genetic Diseases, X-Linked / enzymology
  • Genetic Diseases, X-Linked / genetics
  • Genetic Diseases, X-Linked / immunology
  • Heme Oxygenase-1 / antagonists & inhibitors
  • Heme Oxygenase-1 / biosynthesis
  • Heme Oxygenase-1 / genetics*
  • Lipopolysaccharides / physiology
  • Macrophages, Alveolar / drug effects
  • Macrophages, Alveolar / enzymology*
  • Macrophages, Alveolar / immunology*
  • Membrane Proteins / antagonists & inhibitors
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / genetics*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Mutation
  • NF-E2-Related Factor 2 / physiology*
  • Nitriles / pharmacology
  • Protein Kinase Inhibitors / pharmacology
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / deficiency
  • Protein-Tyrosine Kinases / physiology*
  • Signal Transduction / drug effects
  • Signal Transduction / immunology
  • Toll-Like Receptors / physiology*
  • Transcriptional Activation / drug effects
  • Transcriptional Activation / genetics
  • Transcriptional Activation / immunology*

Substances

  • Amides
  • LFM A13
  • Lipopolysaccharides
  • Membrane Proteins
  • NF-E2-Related Factor 2
  • NFE2L2 protein, human
  • Nitriles
  • Protein Kinase Inhibitors
  • Toll-Like Receptors
  • Heme Oxygenase-1
  • Hmox1 protein, mouse
  • Protein-Tyrosine Kinases
  • Agammaglobulinaemia Tyrosine Kinase
  • BTK protein, human
  • Btk protein, mouse

Supplementary concepts

  • Bruton type agammaglobulinemia