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Vol. 9, Issue 6, 1479-1494, June 1998
and CCAAT/Enhancer Binding Protein
Isoform Synthesis in Control and LPS-Treated Livers
Department of Human Biological Chemistry and Genetics, University
of Texas Medical Branch, Galveston, Texas 77551
The CCAAT/enhancer binding protein 
(C/EBP) and
CCAAT/enhancer binding protein 
(C/EBP) mRNAs are templates for
the differential translation of several isoforms.
Immunoblotting detects C/EBPs with molecular masses
of 42, 38, 30, and 20 kDa and C/EBPs of 35, 20, and ~8.5 kDa. The
DNA-binding activities and pool levels of p42C/EBP
and
p30C/EBP in control nuclear extracts decrease
significantly whereas the binding activity and protein levels of the
20-kDa isoforms increase dramatically with LPS treatment. Our studies
suggest that the LPS response involves alternative translational
initiation at specific in-frame AUGs, producing specific C/EBP and
C/EBP isoform patterns. We propose that alternative translational
initiation occurs by a leaky ribosomal scanning mechanism. We find that
nuclear extracts from normal aged mouse livers have decreased
p42C/EBP levels and binding activity, whereas those of
p20C/EBP and p20C/EBP
are increased.
However, translation of 42-kDa C/EBP is not down-regulated on
polysomes, suggesting that aging may affect its nuclear translocation. Furthermore, recovery of the C/EBP- and C/EBP-binding activities and pool levels from an LPS challenge is delayed significantly in aged
mouse livers. Thus, aged livers have altered steady-state levels of
C/EBP and C/EBP isoforms. This result suggests that normal aging
liver exhibits characteristics of chronic stress and a severe inability
to recover from an inflammatory challenge.
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