Duox2 exhibits potent heme peroxidase activity in human respiratory tract epithelium

Richart W Harper, Changhong Xu, Michael McManus, Amy Heidersbach, Jason P. Eiserich

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

The dual oxidase isozymes Duox1 and Duox2 exhibit functional NADPH:O2 oxidoreductase activity in thyroid and respiratory tract cells and are thought to be essential for H2O2 generation in these tissues. However, it is not universally accepted that the heme peroxidase domains of the Duox isozymes are functional. To address this question, we modulated Duox2 expression in human tracheobronchial epithelial (TBE) cell culture systems and quantified peroxidase activity. We discovered that interferon-gamma (IFN-γ) induced robust peroxidase activity in TBE cells that paralleled Duox2 expression. IFN-γ-induced peroxidase activity was abolished in the presence of sodium azide, which implicated the activation of a heme peroxidase. IFN-γ-induced peroxidase activity was abolished in TBE cell lines expressing anti-Duox2 short hairpin RNA transcripts. Together, these data unequivocally demonstrated that Duox2 contains a functional heme peroxidase in intact respiratory tract epithelium.

Original languageEnglish (US)
Pages (from-to)5150-5154
Number of pages5
JournalFEBS Letters
Volume580
Issue number22
DOIs
StatePublished - Oct 2 2006

Keywords

  • Duox
  • Duox2
  • Heme peroxidase
  • Human
  • Respiratory tract

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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