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J Biol Chem, Vol. 274, Issue 43, 30451-30458, October 22, 1999
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From the Using two-dimensional electrophoresis, we have
recently identified in human bronchoalveolar lavage fluid a novel
protein, termed B166, with a molecular mass of 17 kDa. Here, we report the cloning of human and rat cDNAs encoding B166, which has been renamed AOEB166 for antioxidant
enzyme B166. Indeed, the deduced amino acid
sequence reveals that AOEB166 represents a new mammalian subfamily of
AhpC/TSA peroxiredoxin antioxidant enzymes. Human AOEB166 shares 63%
similarity with Escherichia coli AhpC22 alkyl hydroperoxide
reductase and 66% similarity with a recently identified Saccharomyces cerevisiae alkyl hydroperoxide
reductase/thioredoxin peroxidase. Moreover, recombinant AOEB166
expressed in E. coli exhibits a peroxidase activity, and an
antioxidant activity comparable with that of catalase was
demonstrated with the glutamine synthetase protection assay against
dithiothreitol/Fe3+/O2 oxidation. The analysis of AOEB166
mRNA distribution in 30 different human tissues and in 10 cell
lines shows that the gene is widely expressed in the body. Of interest,
the analysis of N- and C-terminal domains of both human and rat AOEB166
reveals amino acid sequences presenting features of mitochondrial and
peroxisomal targeting sequences. Furthermore, human AOEB166 expressed
as a fusion protein with GFP in HepG2 cell line is sorted to these
organelles. Finally, acute inflammation induced in rat lung by
lipopolysaccharide is associated with an increase of AOEB166 mRNA
levels in lung, suggesting a protective role for AOEB166 in oxidative
and inflammatory processes.
Laboratory of Cell Biology, Department of
Biology, Université Catholique de Louvain, 1348 Louvain-la-Neuve,
Belgium, the § Unit of Industrial Toxicology and
Occupational Medicine, School of Medecine, Université Catholique
de Louvain, 1200 Brussels, Belgium, and the Department of
Biological Chemistry, Université de Mons-Hainaut,
B-7000 Mons, Belgium
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