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Prepublished online as a Blood First Edition Paper on December 12, 2002; DOI 10.1182/blood-2002-04-1212.
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Blood, 15 April 2003, Vol. 101, No. 8, pp. 3274-3280
RED CELLS
Involvement of ABC7 in the biosynthesis of heme in erythroid
cells: interaction of ABC7 with ferrochelatase
Shigeru Taketani,
Kazuhiro Kakimoto,
Hiromi Ueta,
Ryuichi Masaki, and
Takako Furukawa
From the Department of Biotechnology, Kyoto Institute
of Technology, Japan; First Department of Physiology,
Kansai Medical University, Japan; and Biomedical Imaging
Research Center, Fukui Medical University, Japan.
A mitochondrial half-type ATP-binding cassette (ABC) protein, ABC7,
plays a role in iron homeostasis in mitochondria, and defects in human
ABC7 were shown to be responsible for the inherited disease X-linked
sideroblastic anemia/ataxia. We examined the role of ABC7 in the
biosynthesis of heme in erythroid cells where hemoglobin is a major
product of iron-containing compounds. RNA blots showed that the amount
of ABC7 mRNA in dimethylsulfoxide (Me2SO)-treated mouse
erythroleukemia (MEL) cells increased markedly in parallel with the
induction of the mRNA expression of ferrochelatase, the last enzyme in
the pathway to synthesize heme. The transfection of the antisense
oligonucleotide to mouse ABC7 mRNA into Me2SO-treated MEL
cells led to a decrease of heme production, as compared with sense
oligonucleotide-transfected cells. ABC7 protein was shown to be
colocalized with ferrochelatase in mitochondria, as assessed by
immunostaining. Furthermore, in vitro and in vivo pull-down assays
revealed that ABC7 protein is interacted with the carboxy-terminal region containing the iron-sulfur cluster of ferrochelatase. The transient expression of ABC7 in mouse embryo liver BNL-CL2 cells resulted in an increase in the activity and level of ferrochelatase and
thioredoxin, a cytosolic protein containing iron-sulfur. These increases were also observed in MEL cells stably expressing ABC7. When
ABC7 transfectants were treated with Me2SO, an increase in cellular heme concomitant with a marked induction of the expression of
ferrochelatase was observed. The extent of these increases was 3-fold
greater than in control cells. The results indicated that ABC7
positively regulates not only the expression of extramitochondrial thioredoxin but also that of an intramitochondrial
iron-sulfur-containing protein, ferrochelatase. Then, the expression
of ABC7 contributes to the production of heme during the
differentiation of erythroid cells.
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