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- W4313356695 abstract "Abstract We have previously shown that the RNA binding protein, polypyrimidine tract-binding protein (PTB) plays a crucial role in regulating the expression of CD40L in activated CD4 T cells. Regulation occurs through stabilizing the message at late times of activation as well as changing the distribution of CD40L mRNA within distinct cellular compartments. Further experiments were designed to assess how PTB affects global CD4 T cell activation by using shRNA introduced into primary human CD4 T cells. Specifically, we found that PTB is critical for the proliferation and viability of activated T cells. The propensity to undergo cell death was evident in both infected and uninfected CD4 T cells within the same population suggesting that either soluble and/or cognate interactions were being affected by decreased PTB. Accordingly, PTB was found to be required for optimal expression of CD25, CD69, TNF-α and IL-2 but not CD38 or IFN-γ. When the decay rates were assessed in anti-CD3/anti-CD28-stimulated CD4 T cells, the pattern of IL-2, TNF-α and CD69 mRNA decay did not change over a time course of activation whereas CD25 showed a pattern of mRNA decay that was highly similar to CD40L. Evaluation of signaling pathways using phosphoflow analysis revealed PTB-specific changes in the NF-κB and MAPK-ERK pathways. Together, these findings support a role for PTB in the control of CD4 T cell activation through processes that are both dependent on and independent of PTB-regulated mRNA stability." @default.
- W4313356695 created "2023-01-06" @default.
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- W4313356695 date "2015-05-01" @default.
- W4313356695 modified "2023-09-23" @default.
- W4313356695 title "The RNA-binding protein, polypyrimidine tract-binding protein, affects multiple events in CD4 T cell activation through distinct processes (IRM7P.717)" @default.
- W4313356695 doi "https://doi.org/10.4049/jimmunol.194.supp.61.18" @default.
- W4313356695 hasPublicationYear "2015" @default.
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