Increased cellular resistance to oxidative stress by expression of cyanobacterium catalase-peroxidase in animal cells.
To exploit prokaryotic antioxidant enzymes for protection of animal cells from oxidative damage, we expressed catalase-peroxidase of cyanobacterium Synechococcus PCC 7942 in 104C1 cells. The gene for this enzyme was inserted into the mammalian expression vector pRc/CMV. The stable transfectants obtained had higher specific activities of catalase and as a result became more resistant to H2O2 or paraquat than the parental cells. Subcellular fractionation and immunoblot analysis revealed that the expressed catalase-peroxidase was confined to the cytosol; this localization may be the basis for the effective protection of the transfectants from the oxidative cell damage.
Ishikawa
T
T
Department of Biochemistry, Wakayama Medical College, Japan.
Ohta
Y
Y
Takeda
T
T
Shigeoka
S
S
Nishikimi
M
M
D000818:Animals; D001426:Bacterial Proteins; D002460:Cell Line; D000458:Cyanobacteria / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology; D006168:Guinea Pigs; D006861:Hydrogen Peroxide / Q000494:pharmacology; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010269:Paraquat / Q000494:pharmacology; D010544:Peroxidases / Q000378:metabolism*; D011994:Recombinant Proteins; D014162:Transfection
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D006861:Hydrogen Peroxide; D010544:Peroxidases; C081610:catalase-peroxidase, bacteria; D010269:Paraquat