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Detection of Mitochondria Membrane Potential to Study CLIC4 Knockdown-induced HN4 Cell Apoptosis In Vitro
Published on: July 17, 2018
Utilizing mitochondrial events as biomarkers for imaging apoptosis
N Yivgi-Ohana1, M Eifer, Y Addadi
1Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel.
Cell Death & Disease
|June 3, 2011
Summary
We developed a new method to visualize mitochondrial changes during apoptosis using split yellow fluorescent protein (YFP) complementation. This technique allows for live-cell imaging of Bax translocation and cytochrome c release, aiding in apoptosis research.
Area of Science:
- Cell Biology
- Molecular Imaging
- Apoptosis Research
Background:
- Apoptosis involves complex cellular changes, with existing imaging tools focusing on caspases or phosphatidylserine exposure.
- Visualizing mitochondrial events during apoptosis, such as Bax translocation and cytochrome c release, remains challenging.
Purpose of the Study:
- To develop a novel bimolecular fluorescence complementation (BiFC) method for detecting mitochondrial events during apoptosis.
- To enable live-cell imaging of Bax translocation and cytochrome c release in apoptotic cells.
Main Methods:
- Utilized split yellow fluorescent protein (YFP) fragments fused to Bax and cytochrome c (Cyt c).
- Employed BiFC to detect the proximity of Bax and Cyt c at the mitochondria.
- Performed in vivo imaging in liver hepatocytes and subcutaneous tumors.
Main Results:
- Robust YFP fluorescence was observed at the mitochondria of apoptotic cells with minimal background.
- Successfully visualized Bax translocation and Cyt c release in live cells.
- Demonstrated elevated YFP fluorescence in vivo upon apoptosis induction in liver and tumor models.
Conclusions:
- YFP complementation provides a sensitive method for imaging mitochondrial events during apoptosis.
- This novel approach facilitates high-throughput screening and in vivo molecular imaging of apoptosis.
- The technique offers a valuable tool for studying the dynamics of apoptosis in biological systems.
