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Ferritin is a ubiquitously distributed iron-binding protein that
plays a key role in cellular iron homeostasis. It is composed of two
subunits, termed H (heavy or heart) and L (light or liver). In
fibroblasts and other cells, the cytokine tumor necrosis factor-
Volume 270,
Number 25,
Issue of June 25, pp. 15285-15293, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
B in the Regulation of Ferritin H by Tumor Necrosis
Factor-
(TNF) specifically induces synthesis of the ferritin H subunit. Using
nuclear run-off assays, we demonstrate that this TNF-dependent increase
in ferritin H is mediated by a selective increase in ferritin H
transcription. Transfection of murine fibroblasts with chimeric genes
containing the 5`-flanking region of murine ferritin H fused to the
human growth hormone reporter gene reveals that the cis-acting
element that mediates this response is located 4.8 kilobases
distal to the start site of transcription. Deletion analyses delimit
the TNF-responsive region to a 40-nucleotide sequence located between
nucleotides -4776 and -4736, which we term FER-2.
Electrophoretic mobility shift assays and site-specific mutations
indicate that this region contains two independent elements: one
contains a sequence that binds a member of the NF-
B family of
transcription factors, and a second contains a novel sequence that
partially conforms to the NF-B consensus sequence and may bind a
different member of the NF-B/Rel transcription factor family.
Thus, effects of an inflammatory cytokine on ferritin are mediated by a
family of transcription factors responsive to oxidative stress.
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