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J. Biol. Chem., Vol. 269, Issue 39, 24000-24006, 09, 1994
SH Zaidi, R Denman and JS Malter
Growing evidence suggests that Alzheimer's disease results from
dysregulated production and deposition of beta-amyloid in the central
nervous system. beta-Amyloid is derived from proteolytic processing of one
of multiple amyloid precursor protein (APP) isoforms. The production of APP
in many somatic tissues and tumor cell lines provides a more accessible
model to study the regulation of APP gene expression. Recent data suggest
that APP mRNAs accumulate in activated lymphocytes and neuronal tumor
lines. We are interested in defining the contribution of alterations in
stability to changes in steady-state APP mRNA levels in these model
systems. Herein we demonstrate by mobility shift assay that the
3'-untranslated region of APP RNAs which contain a contiguous 29-base
region interacts in vitro with multiple mRNA-binding proteins found in
cytosolic lysates prepared from normal and transformed human cells. UV
cross-linking of radiolabeled APP RNAs to cytosolic protein extracts
followed by sodium dodecyl sulfate- polyacrylamide gel electrophoresis
identified six distinct RNA-protein complexes of 42, 47, 65, 73, 84, and
104 kDa. Competition assays with APP, AU-rich, or irrelevant RNAs
demonstrated that binding was specific and in some cases preferential for
AU- or U-rich sequences by which we tentatively place the binding site of
the proteins along the 29-base region. APP mRNA-binding proteins were
constitutively active in all tumor lines examined as well as at diminished
levels in whole human brain cytosolic lysates. The core element is AU-rich
and highly conserved between human and some murine APP mRNAs. In the
accompanying paper (Zaidi, S. H. E. and Malter, J. S. (1994) J. Biol. Chem.
269, 24007-24013) we show that this 29-base element in the 3'-untranslated
region regulates the stability of APP mRNA. Cumulatively these data suggest
that steady-state APP mRNA levels are modulated by cytosolic protein-RNA
interactions.
Multiple proteins interact at a unique cis-element in the 3'- untranslated region of amyloid precursor protein mRNA
Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison 53792-2472.
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