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Cell death

A2B via p53

Nature Reviews Cancer volume 13, page 441 (2013)Cite this article

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Various stimuli are known to induce p53 stabilization and activation, and some (cisplatin, ultraviolet (UV) light and methotrexate) but not all (γ-irradiation and 5-fluorouracil) resulted in the p53-dependent transcription of ADORA2B. Further experiments revealed that, in response to cisplatin, p53-mediated transcription of ADORA2B occurred in cells expressing the adenoviral E1A oncogene and did not occur in control cells. Overexpression of genes such as E1A can both transform cells and make them more sensitive to certain stimuli that induce apoptosis. These findings hinted that the expression of A2B might be linked to cell death. Further experiments showed that, in Saos-2 human osteosarcoma cells expressing a regulatable ADORA2B gene, A2B expression induced apoptosis, which was increased by treating the cells with an adenosine analogue, adenosine 5′-N-ethylcarboximide (NECA), an A2B ligand. Moreover, NECA–A2B-induced apoptosis was shown to be regulated by members of the BCL-2 family of pro-apoptotic and anti-apoptotic proteins, and the BH3-only pro-apoptotic protein PUMA in particular was required to induce apoptosis downstream of A2B expression.

A2B functions as a cell death priming mechanism downstream of p53

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References

  1. Long, J. S. et al. Extracellular adenosine sensing — a metabolic cell death priming mechanism downstream of p53. Mol. Cell 50, 394–406 (2013)

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  1. Nicola McCarthy
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McCarthy, N. A2B via p53. Nat Rev Cancer 13, 441 (2013). https://doi.org/10.1038/nrc3548

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