Overexpression of the truncated form of Livin reveals a complex interaction with caspase-3.

Disruption in apoptosis are involved in cancer development and progression. Livin-β, has been identified as a critical modulator for cell death in several tumor cell lines. It was demonstrated that a truncated fragment of Livin-β (tLivin) without its N-terminal 52 amino acids is produced in cells through protein cleavage. However, ...
the biological consequence of the cleavage remains largely ignored. In the present study, we report that tLivin exerted a pro-apoptotic effect on cells. The subcellular localization of tLivin was mainly restricted to the cytoplasm. To explore the underlying mechanism, we observed an elevated caspase-3 activity which may account for the apoptosis. Furthermore, we observed that tLivin was further cleaved into a smaller fragment in cells. This second cleavage was possibly related to activated caspase-3. The resulted C-terminal fragment (livC) was an anti-apoptotic factor. Our study may help to deepen our understanding of the role of Livin in the regulation of cell death.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Antineoplastic Agents, Apoptosis, Caspase 3, Cell Line, Tumor, Cisplatin, Cytoplasm, Enzyme Activation, HEK293 Cells, Humans, Inhibitor of Apoptosis Proteins, Neoplasm Proteins, Recombinant Proteins
Int. J. Oncol.
Date: Jun. 01, 2013
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