Initial Characterization of Human Dual Oxidase 2 (DUOX2) in a Baculovirus System

Abstract

As members of the NOX/DUOX family, the DUOX protein subfamily is responsible for hydrogen peroxide generation in human epithelial cells. The reactive oxygen species produced is utilized for cellular functions including innate immunity, hormone production, and signaling. Two highly conserved DUOX isoforms are encoded in the H. sapiens genome; hDUOX1 and hDUOX2. These membrane bound proteins have garnered much attention for their unique N‐terminal peroxidase‐like domain(s). Initial studies on the hDUOX1 peroxidase‐like domain have failed to demonstrate heme binding; whereas the C. elegans DUOX1 isoform co‐purifies with heme bound. To further characterize the heme‐binding potential and function of the hDUOX2 protein, both the full‐length protein and N‐terminal peroxidase domain have been expressed in a baculovirus system for investigation. Evaluation of these proteins will be presented. This work was partially supported by NIH Grant DK30297.