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Mitochondria-Regulated Death Pathway Mediates (DIPP-L-Leu)2-LLysOCH3- Induced K562 Cells Apoptosis.

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(DIPP-L-Leu)2-L-LysOCH3 is A diisopropylphosphoryl dipeptide which is known to induce apoptosis of human leukemia K562 cells. The molecular and cellular mechanisms involved in this process remain to be clarified. Herein, we show that (DIPP-L-Leu)2-L-LysOCH3-induced apoptosis is associated with cytosolic accumulation of cytochrome c, sustained loss of mitochondrial transmembrane potential (MMP), transient generation of reactive oxygen species (ROS) and elevation of intracellular Ca2+ concentration. A specific caspase assay reveals an increase in caspase-9 and caspase-3 activity but no change in caspase-8 activity. Immunofluorescence analysis indicates that (DIPP-L-Leu)2-L-LysOCH3 induced upregulation of pro-apoptotic Bax and downregulation of anti-apoptotic Bcl-2 and Bcl-xL. These results suggest that the mitochondria-regulated death pathway mediates (DIPP-L-Leu)2-L-LysOCH3-induced K562 cells apoptosis.

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Keywords: Phosphoryl dipeptide; apoptosis; caspase; mitochondria

Document Type: Research Article

Affiliations: The Key Laboratory of Chemical Biology, Guangdong Province, Graduate School at Shenzhen, Tsinghua University, Shenzhen 518055 P. R. China.

Publication date: 2006-02-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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