Erythropoietin activates caspase-3 and downregulates CAD during erythroid differentiation in TF-1 cells - a protection mechanism against DNA fragmentation

FEBS Letters
Julian Chun-Kin Lui, Siu-Kai Kong

Abstract

The involvement of caspase-3 and its failure in the induction of DNA fragmentation during erythropoiesis were investigated with TF-1 cells. During erythroid differentiation, caspase-3 activation and cleavage of caspase-3 substrates such as ICAD (inhibitor of caspase-activated DNase) were detected without concomitant phosphatidyl-serine (PS) externalization and DNA fragmentation. These observations are in contrast to our understanding that DNA is degraded by CAD (caspase-activated DNase) when ICAD is cleaved by caspase-3. Our study demonstrates that CAD is downregulated at the mRNA and protein level during the erythroid differentiation in TF-1 cells. This provides a mechanism for the first time how cells avoid DNA fragmentation with activated caspase-3.

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Citations

Mar 24, 2007·Cancer Letters·Crystal Sao-Fong CheungShannon Wing-Ngor Au
Oct 15, 2014·British Journal of Haematology·MinJung KimCurt I Civin
Oct 19, 2016·Nucleus·Baobing ZhaoPeng Ji
Feb 18, 2017·Cell Death and Differentiation·Stéphanie SolierEric Solary

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