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Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.

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Knoops, Bernard [UCL] Clippe, André [UCL] Bogard, C Arsalane, K. Wattiez, R. Hermans, Cédric [UCL] Bernard, Alfred [UCL]

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+/O(2) 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.

Document type Article de périodique (Journal article) – Journal Article, Research Support, Non-U.S. Gov't
Access type Accès restreint
Publication date 1999
Journal information "The Journal of biological chemistry" - Vol. 274, no. 43, p. 30451-8 (1999)
Peer reviewed yes
issn 0021-9258
Publication status Publié
Affiliations UCL - SC/BIOL - Département de biologie
UCL - MD/ESP - Ecole de santé publique
MESH Subject Amino Acid Sequence ; Animals ; Antioxidants - metabolism ; Base Sequence ; Cell Line ; Chromosome Mapping ; Cloning, Molecular ; Consensus Sequence ; Conserved Sequence ; Escherichia coli - enzymology ; Escherichia coli Proteins ; Evolution, Molecular ; Humans ; Inflammation ; Kinetics ; Lung Diseases - enzymology ; Mammals ; Molecular Sequence Data ; Organ Specificity ; Peroxidases - chemistry ; Peroxiredoxins ; Phylogeny ; Rats ; Recombinant Proteins - chemistry - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Transcription, Genetic ; Tumor Cells, Cultured
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Bibliographic reference Knoops, Bernard ; Clippe, André ; Bogard, C ; Arsalane, K. ; Wattiez, R. ; et. al. Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.. In: The Journal of biological chemistry, Vol. 274, no. 43, p. 30451-8 (1999)
Permanent URL http://hdl.handle.net/2078.1/8371