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Abstract On A Research Article

            Tumor necrosis factor á (TNFá) - a pro-inflammatory cytokine - causes pleiotropic effects on numerous cell types. Excessive production of TNFá results in systemic inflammatory response syndrome (SIRS), which eventually leads to a circulatory collapse and multiple organ failure. Recent studies have shown that TNFá is controlled post-transcriptionally by the regulation of both the mRNA stability and translational efficacy. AU-rich elements (AREs) in the 3'- untranslated region of mRNA are known to be the recognition sequences for several RNA-binding proteins. RNase protection and RNA gel shift assays have enabled the mapping of two protein binding regions of TNFá mRNA necessary for binding of macrophage proteins to the 3'-UTR. The first binding region is present within the ARE, whereas the second is located 147 base pairs downstream of the first ARE. The goal of this study was to investigate whether GAU trinucleotide insertions in the main ARE of the 3'-UTR of TNFá mRNA has an effect on the binding of macrophage proteins to this element. It is shown that trinucleotide insertions in the main ARE of the 3'-UTR of TNFá mRNA alters the binding of complexes B and C (protein HuR is part of one of these complexes) to the region. These complexes are involved in the transport of TNFá mRNA from the nucleus of a cell to the cytoplasm. NZW mice are reported to be low producers of TNFá protein when stimulated with interferon a (INFa) and lipopolysaccharide (LPS) which normally cause increased production of TNFá. It has been demonstrated that NZW mice contain a trinucleotide (GAU) mutation in the main ARE of TNFá mRNA 3'-UTR, which affects the post-transcriptional regulation of TNFá production. B10.A mice do not have this mutation. Cells were stimulated with LPS and/or INFa and extracted from the two genotypic mice.


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