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Continuous presence of phorbol ester is required for its IL‐1β mRNA stabilizing effect
Author(s) -
Siljander Pia,
Hurme Mikko
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81138-p
Subject(s) - protein kinase c , phorbol , messenger rna , protein biosynthesis , phorbol ester , rna , chemistry , microbiology and biotechnology , tetradecanoylphorbol acetate , gene expression , biochemistry , biology , kinase , gene
The protein kinase C (PKC) activating phorbol esters are known to prevent the decay of mRNA of several cytokines and proto‐oncogenes. To examine whether the phorbol ester signal is continuously required for this stabilizing effect, THP‐1 monocytic cells were stimulated either with phorbol 12,13‐dibutyrate (PDBu), which can be removed from the cells by washings, or with the more hydrophobic phorbol 12‐myristate 13‐acetate (PMA). Both of these stimuli induced high levels of interleukin‐1β (IL‐1β) mRNA. When the cells were washed at the peak of the IL‐1β mRNA expression, this mRNA decayed rapidly in the PDBu stimulated cells while in PMA stimulated cells the mRNA levels were not affected. Moreover, this mRNA degradation induced by the removal of PDBu could be inhibited by readdition of the phorbol ester. This restabilization could be prevented by pharmacologie inhibitors of PKC, but not by inhibiting protein or RNA synthesis. Thus these data suggest that the phorbol ester must be continuously present to exert its mRNA stabilizing effect and that its effect is PKC‐mediated but does not require active protein or RNA synthesis.