Erythropoietin activates caspase-3 and downregulates CAD during erythroid differentiation in TF-1 cells - a protection mechanism against DNA fragmentation |
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Authors: | Lui Julian Chun-Kin Kong Siu-Kai |
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Affiliation: | Department of Biochemistry, The Chinese University of Hong Kong, Shatin, NT, Hong Kong, China. |
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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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Keywords: | CAD, caspase-activated DNase EPO, erythropoietin GPA, glycophorin A GADPH, glyceraldehyde-3-phosphate dehydrogenase GM-CSF, granulocyte-macrophage colony stimulating factor Hb, hemoglobin ICAD, inhibitor of the caspase-activated DNase MAb, monoclonal antibody PARP, poly (ADP-ribose) polymerase PI, propidium iodide PS, phosphatidylserine STS, staurosporine TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick-end labeling |
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