PMID- 10521424
OWN - NLM
STAT- MEDLINE
DCOM- 19991123
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 43
DP  - 1999 Oct 22
TI  - Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of 
      the peroxiredoxin family.
PG  - 30451-8
AB  - 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.
FAU - Knoops, B
AU  - Knoops B
AD  - Laboratory of Cell Biology, Department of Biology, Universite Catholique de
      Louvain, 1348 Louvain-la-Neuve, Belgium. knoops@bani.ucl.ac.be
FAU - Clippe, A
AU  - Clippe A
FAU - Bogard, C
AU  - Bogard C
FAU - Arsalane, K
AU  - Arsalane K
FAU - Wattiez, R
AU  - Wattiez R
FAU - Hermans, C
AU  - Hermans C
FAU - Duconseille, E
AU  - Duconseille E
FAU - Falmagne, P
AU  - Falmagne P
FAU - Bernard, A
AU  - Bernard A
LA  - eng
SI  - GENBANK/AF110731
SI  - GENBANK/AF110732
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antioxidants)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 1.11.1.- (Peroxidases)
RN  - EC 1.11.1.15 (Peroxiredoxins)
RN  - EC 1.11.1.15 (ahpC protein, E coli)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antioxidants/metabolism
MH  - Base Sequence
MH  - Cell Line
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - Consensus Sequence
MH  - Conserved Sequence
MH  - Escherichia coli/enzymology
MH  - Escherichia coli Proteins
MH  - Evolution, Molecular
MH  - Humans
MH  - Inflammation
MH  - Kinetics
MH  - Lung Diseases/enzymology
MH  - Mammals
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Peroxidases/*chemistry
MH  - Peroxiredoxins
MH  - Phylogeny
MH  - Rats
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transcription, Genetic
MH  - Tumor Cells, Cultured
EDAT- 1999/10/16 00:00
MHDA- 1999/10/16 00:01
CRDT- 1999/10/16 00:00
PHST- 1999/10/16 00:00 [pubmed]
PHST- 1999/10/16 00:01 [medline]
PHST- 1999/10/16 00:00 [entrez]
AID - 10.1074/jbc.274.43.30451 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 22;274(43):30451-8. doi: 10.1074/jbc.274.43.30451.