Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2001-5-22
pubmed:abstractText
Translational regulation of ornithine decarboxylase (ODC), which catalyses the first step in the biosynthesis of polyamines, appears to be an important mechanism in the strong feedback control as well as in the hypotonic induction of the enzyme. However, the exact mechanisms are not yet understood. The ODC mRNA has long 5' and 3' untranslated regions (UTRs) which may be involved in the translational control of the enzyme. In the present study we have used a series of stable transfectants of Chinese Hamster ovary cells expressing ODC mRNAs with various truncations in the 5' and 3' UTRs to investigate the importance of these regions. It is demonstrated that neither the 5' UTR nor the 3' UTR appears to be involved in the polyamine-mediated feedback control of ODC synthesis. The hypotonic induction of ODC, on the other hand, was shown to be highly dependent on the presence of the 3' UTR, but not on the 5' UTR, of ODC mRNA. Cells expressing ODC mRNAs lacking the 3' UTR showed no, or only a very slight, induction of ODC whether the 5' UTR was present or not, whereas the cell lines expressing ODC mRNAs containing the 3' UTR (with or without the 5' UTR) markedly induced ODC after a hypotonic shock. The present finding of a role for the ODC mRNA 3' UTR in the hypotonic induction of ODC is the first demonstration of a specific effect of the 3' UTR in the regulation of ODC.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
356
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
627-34
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Importance of the 3' untranslated region of ornithine decarboxylase mRNA in the translational regulation of the enzyme.
pubmed:affiliation
Department of Physiological Sciences, Lund University, Sölvegatan 19, S-223 62 Lund, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't