Measurement of caspase-2 activation during different anti-tumor drugs induced apoptosis by FRET technique

Juqiang Lin; Shaoqun Zeng; Qingming Luo; Chen Rong; Zhihong Zhang

doi:10.1117/12.757313

8 January 2008 Measurement of caspase-2 activation during different anti-tumor drugs induced apoptosis by FRET technique

Juqiang Lin, Shaoqun Zeng, Qingming Luo, Chen Rong, Zhihong Zhang

Author Affiliations +

Proceedings Volume 6826, Optics in Health Care and Biomedical Optics III; 682630 (2008) https://doi.org/10.1117/12.757313
Event: Photonics Asia 2007, 2007, Beijing, China

Abstract

Caspase-2 is important for the engagement of the mitochondrial apoptotic pathway, in the presence of DNA-damaging agents, such as cisplatin; however, the mechanism by which caspase-2 executes apoptosis remains obscure. In this study, we carried out the measurements of the dynamics of caspase-2 activation in a single living cell by a FRET (fluorescence resonance energy transfer) probe. A FRET probe was constructed that encoded a CRS (caspase-2 recognition site) fused with a cyan fluorescent protein (CFP) and a red fluorescent protein (DsRed) (CFP-CRS-DsRed). Using this probe, we found that during TRAIL-induced apoptosis, caspase-2 was not activated, and caspase-2 activation occurred in etoposide and cisplatin treated cells. However, during cisplatin-induced apoptosis caspase-2 activation was initiated much earlier than that of etoposide. Cisplatin and etoposide is one of the most broadly used drugs in the Clinical applications of cancer chemotherapy, and TRAIL, which belongs to the TNF family proteins, can selectively induce apoptosis in many transformed cells but not in normal cells. Most of anticancer drugs can induce apoptosis mediated by the activation of caspase pathway. Thus, the perfect synergistic effect group of multi-drug can be selected by using our FRET probe.

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Juqiang Lin, Shaoqun Zeng, Qingming Luo, Chen Rong, and Zhihong Zhang "Measurement of caspase-2 activation during different anti-tumor drugs induced apoptosis by FRET technique", Proc. SPIE 6826, Optics in Health Care and Biomedical Optics III, 682630 (8 January 2008); https://doi.org/10.1117/12.757313

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KEYWORDS

Fluorescence resonance energy transfer

Cell death

Fluorescent proteins

Cancer

Biomedical optics

Proteins

Imaging systems

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