Cytokine rescue of p53-dependent apoptosis and cell cycle arrest is mediated by distinct Jak kinase signaling pathways

Article Abstract:

Certain cytokines, erythropoietin and interleukin-3, keep gamma-IR-induced apoptosis and cell cycle arrest from occurring. Activation of the Jak kinase is necessary and sufficient as a cause. If hematopoietic progenitors are exposed to gamma-irradiation (IR), the result is p-53-dependent apoptosis and a p53-independent G2/M cell cycle arrest. The Jak signaling pathway can be functionally linked to suppression of p53-mediated cell death by cytokine action. Apoptotic and growth arrest that result from DNA damage in hematopoietic cells are altered by certain cytokine-specific signal transduction paths.

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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappaB activation

Article Abstract:

Yeast two-hybrid methods identified proteins, designated TRADD, that interact with the intracellular region of human TNFR1, a receptor mediating apoptosis or programmed cell death. Overexpression of TRADD in cells has been shown to induce apoptosis and activation of NF-kappaB, suggesting that two signal pathways are triggered. Activation of the crmA gene encoding the expression of 1beta-converting enzyme inhibited TRADD-mediated cell death, but had no effect on NF-kappaB. This suggests that the apoptotic signal pathway is distinct from the pathway signaling NF-kappaB activation.

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Contenders in FasL/TNF death signaling

Article Abstract:

The Fas ligand (FasL) and the tumor necrosis factors (TNFR) induce apoptosis or programmed cell death through interaction with receptors belonging to the TNFR superfamily, which forms the cell death pathway. FasL and TNFR sends signals that activate genes inducing cytoplasmic changes in the cell. The yeast two-hybrid method suggest that FasL and TNFR contain proteins that are homologous to the death domains of Fas and TNFR1. It was also shown that other receptors/reaper such as TRADD, FADD and RIP contains effector domains for apoptosis.

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