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Abstract
TDP-43 is a ubiquitously expressed DNA/RNA binding protein that has recently attracted attention for its involvement in neurodegenerative diseases. While TDP-43 has been found to participate in various important cellular activities including stress and apoptosis, little is known about its role in cancer cells. Here we report that staurosporine (STS) induced apoptosis in U87 glioma cells is associated with rapid downregulation of TDP-43 at both mRNA and protein levels. The latter is dependent on activation of caspase 3. More importantly, we have shown that knockdown of TDP-43 by specific siRNA dramatically enhanced cytotoxicity of STS. These results suggest that normal level of TDP-43 may be protective for cancer cells under apoptotic insult.
Highlights
TAR-DNA-binding protein 43 (TDP-43) is a highly conserved heterogeneous nuclear ribonucleoprotein which consists of 414 amino acids
To ask whether transcriptional down-regulation by STS is the only mechanism for reduced levels of TDP43, we further looked at involvement of caspase-3 in TDP-43 proteolysis as it has been shown that TDP-43
Glioma is a certain kind of tumor which grows in brain or spine, it accounts for ~30% of central nervous system (CNS) tumors and 80% of malignant brain tumors (Goodenberger et al, 2012)
Summary
TAR-DNA-binding protein 43 (TDP-43) is a highly conserved heterogeneous nuclear ribonucleoprotein (hnRNP) which consists of 414 amino acids. It is encoded by the TARDBP gene on chromosome 1 (Ou et al, 1995). TDP-43 can interact with many other splicing related protein (Buratti et al, 2005; Freibaum et al, 2010) via the C-terminal glycine-rich domain of the protein (Wang et al, 2004; Ayala et al, 2005)
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