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Caspase cleavage of Mcl-1 impairs its anti-apoptotic activity and proteasomal degradation in non-small lung cancer cells.

Apoptosis. 2018-01; 
WangTing,YangZhiwei,ZhangYimeng,ZhangXiang,WangLei,ZhangShengli,JiaLi
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PCR and Cloning … R050A, Takara). Full-length (FL) Mcl-1 and truncated Mcl-1 (amino acids 1-270 deleted, Mcl-1TC) were amplified by PCR and inserted into the HindIII/XbaI site of the pcDNA3.1 + /C-HA expression vector (GenScript, Piscataway, NJ, USA) … Get A Quote

摘要

Global cleavage of cellular proteins by activated caspases is a hallmark of apoptosis, which causes biochemical collapse of the cell. Recent studies suggest that, rather than completely destroying a protein, caspase cleavage can confer novel characteristics or functions. In this respect, the post-caspase role of Bcl-2 family proteins remains uncharacterized. Here, we showed that Mcl-1, a pro-survival member of the Bcl-2 family, was cleaved by caspase-3 in non-small cell lung cancer (NSCLC) cells undergoing chemotherapeutic agent-triggered apoptosis. Caspase cleavage partially impaired the anti-apoptotic activity of Mcl-1 by reducing its mitochondrial localization and impeding its association with ... More

关键词

Bak,Chemotherapy,Lung cancer,Mcl-1,Proteasomal degrada
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