Document Type
Article
Language
eng
Format of Original
9 p.
Publication Date
10-2016
Publisher
Springer
Source Publication
Amino Acids
Source ISSN
0939-4451
Abstract
Ornithine decarboxylase (ODC) is the first and usually rate-limiting enzyme in the polyamine biosynthetic pathway. In a normal physiological state, ODC is tightly regulated. However, during neoplastic transformation, ODC expression becomes upregulated. The studies described here show that the ODC mRNA transcript is destabilized by the RNA-binding protein tristetraprolin (TTP). We show that TTP is able to bind to the ODC mRNA transcript in both non-transformed RIE-1 cells and transformed Ras12V cells. Moreover, using mouse embryonic fibroblast cell lines that are devoid of a functional TTP protein, we demonstrate that in the absence of TTP both ODC mRNA stability and ODC enzyme activity increase when compared to wild-type cells. Finally, we show that the ODC 3′ untranslated region contains cis acting destabilizing elements that are affected by, but not solely dependent on, TTP expression. Together, these data support the hypothesis that TTP plays a role in the post-transcriptional regulation of the ODC mRNA transcript.
Recommended Citation
Nowotarski, Shannon L.; Origanti, Sofia; Sass-Kuhn, Suzanne; and Shantz, Lisa M., "Destabilization of The Ornithine Decarboxylase mRNA Transcript by the RNA-Binding Protein Tristetraprolin" (2016). Biological Sciences Faculty Research and Publications. 536.
https://epublications.marquette.edu/bio_fac/536
Comments
Accepted version. Amino Acids, Vol. 48, No. 10 (October 2016): 2303-2311. DOI. © 2016 Springer. Used with permission.