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J Biol Chem, Vol. 273, Issue 5, 2917-2925, January 30, 1998
From the Department of Pathology, School of Medicine, University of
Pittsburgh, Pittsburgh, Pennsylvania 15261
A novel cDNA was partially isolated from a
HepG2 cell expression library by screening with the promoter-linked
coupling element (PCE), a site from the 
-fetoprotein (AFP) gene
promoter. The remainder of the cDNA was cloned from fetal liver RNA
using random amplification of cDNA ends. The cDNA encodes a
239-amino acid peptide with domains closely related to the
Drosophila factor nk-2. The new factor is the
eighth vertebrate factor related to nk-2, hence
nkx-2.8. Northern blot and reverse transcriptase polymerase chain reaction analysis demonstrated mRNA in HepG2, two other AFP-expressing human cell lines, and human fetal liver. Transcripts were not detected in adult liver. Cell-free translation produced DNA
binding activity that gel shifted a PCE oligonucleotide. Cotransfection of nkx-2.8 expression and PCE reporter plasmids into HeLa
cells demonstrated transcriptional activation; NH2-terminal
deletion eliminated this activity. Cotransfection into AFP-producing
hepatocytic cells repressed AFP reporter expression, suggesting that
endogenous activity was already present in these cells. In contrast,
cotransfection into an AFP-negative hepatocytic line produced moderate
activation of the AFP gene. The cardiac developmental factor
nkx-2.5 could substitute for nkx-2.8 in all
transfection assays, whereas another related factor, thyroid
transcription factor 1, showed a more limited range of substitution.
Although the studies have yet to establish definitively that
nkx-2.8 is the AFP gene regulator PCF, the two factors
share a common DNA binding site, gel shift behavior, migration on
SDS-acrylamide gels, and cellular distribution. Moreover, the
nk-2-related genes are developmental regulators, and
nkx-2.8 is the first such factor associated with liver
development.
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