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J Biol Chem, Vol. 274, Issue 37, 26217-26224, September 10, 1999
,
From the HepG2 cells were transfected with vectors
containing human catalase cDNA and catalase cDNA with a
mitochondrial leader sequence to allow comparison of the effectiveness
of catalase overexpressed in the cytosolic or mitochondrial
compartments to protect against oxidant-induced injury. Overexpression
of catalase in cytosol and in mitochondria was confirmed by Western
blot, and activity measurement and stable cell lines were established.
The intracellular level of H2O2 induced
by exogenously added H2O2 or antimycin A was
lower in C33 cell lines overexpressing catalase in the cytosol and mC5
cell lines overexpressing catalase in the mitochondria as compared with
Hp cell lines transfected with empty vector. Cell death caused by
H2O2, antimycin A, and menadione was
considerably suppressed in both the mC5 and C33 cell lines. C33 and mC5
cells were also more resistant to apoptosis induced by
H2O2 and to the loss of mitochondrial membrane
potential induced by H2O2 and antimycin A. In
view of the comparable protection by catalase overexpressed in the
cytosol versus the mitochondria, catalase produced in both cellular compartments might act as a sink to decompose
H2O2 and move diffusable
H2O2 down its concentration gradient. The
present study suggests that catalase in cytosol and catalase in
mitochondria are capable of protecting HepG2 cells against cytotoxicity
or apoptosis induced by oxidative stress.
Department of Biochemistry and Molecular
Biology, Mount Sinai School of Medicine, New York, New York 10029 and
the § Department of Biochemistry and Molecular Biology,
Albany Medical College, Albany, New York 12208
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