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Identification of novel Nox4 splice variants with impact on ROS levels in A549 cells
Authors:Goyal Parag  Weissmann Norbert  Rose Frank  Grimminger Friedrich  Schäfers Hans J  Seeger Werner  Hänze Jörg
Institution:Department of Internal Medicine, Medical School University of Giessen, Klinikstr. 36, D-35392 Giessen, Germany.
Abstract:NAD(P)H oxidases (Nox) generate reactive oxygen species (ROS) that function in host defense and cellular signaling. While analyzing the expression of Nox4 at the protein and the mRNA levels, we identified four novel Nox4 splice-variants Nox4B, Nox4C, Nox4D, and Nox4E, which are expressed in human lung A549 cell line and lung tissues. One Nox4 isoform lacks the first NAD(P)H binding site (Nox4B) while another lacks all FADH and NAD(P)H binding sites (Nox4C). Cells over-expressing NoxB or Nox4C exhibited a decrease in ROS levels. Thus, these isoforms have dominant negative characteristics for ROS generation. Two other splice-variants (Nox4D, Nox4E) lack the transmembrane domains, suggesting these as non-membrane associated isoforms. Nox4D contains all FADH and NAD(P)H binding domains and shows the same rate of ROS generation as Nox4 prototype. Taken together, we suggest that Nox4 exists as several isoforms that may have different functions in ROS-related cell signaling.
Keywords:NAD(P)H oxidase  Nox4  Nox1  Splice variant  ROS signaling
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