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• W2149293843 abstract "PU.1 is one of key regulators of hematopoietic cell development, a tightly-regulated lineage-specific process. Here we provide the first evidence that PU.1 protein is cleaved into two fragments of 24 kDa and 16 kDa during apoptosis progression in leukemic cell lines and primary leukemic cells. Further experiments with specific capase-3 inhibitor Z-DEVD-fmk and the in vitro proteolytic system confirmed that PU.1 is a direct target of caspase-3. Using site-directed mutagenesis analyses, the aspartic acid residues at positions 97 and 151 of PU.1 protein were identified as capsase-3 target sites. More intriguingly, the suppression of PU.1 expression by small interfering RNAs (siRNAs) significantly inhibits DNA-damaging agents NSC606985 and etoposide-induced apoptosis in leukemic cells, together with the up-regulated expression of anti-apoptotic bcl-2 gene. These results would provide new insights for understanding the mechanism of PU.1 protein in hematopoiesis and leukemogenesis." @default.
• W2149293843 created "2016-06-24" @default.
• W2149293843 creator A5017175637 @default.
• W2149293843 creator A5019912790 @default.
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• W2149293843 date "2009-05-01" @default.
• W2149293843 modified "2023-09-26" @default.
• W2149293843 title "PU.1, a novel capase-3 substrate, partially contributes to chemotherapeutic agents-induced apoptosis in leukemic cells" @default.
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• W2149293843 doi "https://doi.org/10.1016/j.bbrc.2009.03.024" @default.
• W2149293843 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19281794" @default.
• W2149293843 hasPublicationYear "2009" @default.
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