Nucleic Acids Research, Vol 26, Issue 14 3418-3423, Copyright © 1998 by Oxford University Press
LE Rajagopalan, CJ Westmark, JA Jarzembowski and JS Malter
We have previously shown that heterogeneous nuclear ribonucleoprotein C
(hnRNP C) and nucleolin bound specifically to a 29 nt sequence in the
3'-untranslated region of amyloid precursor protein (APP) mRNA. Upon
activation of peripheral blood mononuclear cells, hnRNP C and nucleolin
acquired APP mRNA binding activity, concurrent with APP mRNA stabilization.
These data suggested that the regulated interaction of hnRNP C and
nucleolin with APP mRNA controlled its stability. Here we have directly
examined the role of the cis element and trans factors in the turnover and
translation of APP mRNA in vitro . In a rabbit reticulocyte lysate (RRL)
translation system, a mutant APP mRNA lacking the 29 nt element was
3-4-fold more stable and synthesized 2-4-fold more APP as wild-type APP
mRNA. Therefore, the 29 nt element functioned as an APP mRNA destabilizer.
RNA gel mobility shift assays with the RRL suggested the presence of
endogenous nucleolin, but failed to show hnRNP C binding activity. However,
wild-type APP mRNA was stabilized and coded for 6-fold more APP when
translated in an RRL system supplemented with exogenous active hnRNP C.
Control mRNAs lacking the 29 nt element were unaffected by hnRNP C
supplementation. Therefore, occupancy of the 29 nt element by hnRNP C
stabilized APP mRNA and enhanced its translation.
ARTICLES
hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA
Neuroscience Program, Institute on Aging and Department of Pathology and Laboratory Medicine,University of Wisconsin-Medical School, Madison, WI 53792, USA.
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