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J. Biol. Chem., Vol. 277, Issue 45, 43309-43318, November 8, 2002
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From the Mitochondrial transcription factor A is a
key regulator involved in mitochondrial DNA transcription and
replication. In a poorly differentiated rat hepatoma, Morris hepatoma
3924A, the mRNA and protein levels of this factor were elevated
about 10- and 11-fold, respectively, relative to the host liver. The
mRNA levels for the hepatoma cytochrome c oxidase I,
II, and NADH dehydrogenase 5, 6, the downstream targets of Tfam, were
augmented 10-, 8-, 5-, and 3-fold, respectively. Interestingly, Tfam
was also found in the hepatoma nucleus. The mRNA levels for nuclear
respiratory factor 1 and 2 (NRF-1 and -2), the proteins that are known
to interact with specific regulatory elements on human TFAM
promoter, were 5- and 3-fold higher, respectively, in the hepatoma
relative to the host liver. Unlike the human promoter, the rat
Tfam promoter did not form a specific complex with the
NRF-1 in the liver or hepatoma nuclear extracts, which is consistent
with the absence of an NRF-1 consensus sequence in the proximal rat
promoter. A single specific complex formed between the rat promoter and
the NRF-2 protein was comparable in the two extracts. The DNA binding activity of Sp1 in the hepatoma nuclear extract was 4-fold greater than
that in the liver extract. In vivo genomic footprinting
showed occupancy of NRF-2 and Sp1 consensus sites on the promoter of rat Tfam gene. Tfam was also up-regulated in other hepatoma
cells. Together, these results show up-regulation of Tfam in some
tumors, particularly the liver tumors. Further, the relatively high
level of Sp1 binding to the promoter in the hepatoma could play a major role in the up-regulation of
Tfam in these tumor cells.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF377866.
Mitochondrial Transcription Factor A and Its Downstream Targets
Are Up-regulated in a Rat Hepatoma*
,,,¶
Department of Molecular and
Cellular Biochemistry, College of Medicine, The Ohio State University,
Columbus, Ohio 43210, and § Molecular Biotechnology Core,
Cleveland Clinic Foundation, Lerner Research Institute,
Cleveland, Ohio 44195
*
This work was supported in part by United States Public
Service Grants CA 81024 and ES 10874 (to S. T. J.) from NCI (National Institutes of Health (NIH)) and NIEHS (NIH), respectively. This research was performed in partial fulfillment of the requirement for
the Ph.D. degree in the Molecular, Cellular, and Developmental Biology
Program of the Ohio State University (X. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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