Detection of programmed cell death using fluorescence energy transfer
Open Access
- 15 April 1998
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 26 (8) , 2034-2035
- https://doi.org/10.1093/nar/26.8.2034
Abstract
Fluorescence energy transfer (FRET) can be generated when green fluorescent protein (GFP) and blue fluorescent protein (BFP) are covalently linked together by a short peptide. Cleavage of this linkage by protease completely eliminates FRET effect. Caspase-3 (CPP32) is an important cellular protease activated during programmed cell death. An 18 amino acid peptide containing CPP32 recognition sequence, DEVD, was used to link GFP and BFP together. CPP32 activation can be monitored by FRET assay during the apoptosis process.Keywords
This publication has 8 references indexed in Scilit:
- Applications of the green fluorescent protein in cell biology and biotechnologyNature Biotechnology, 1997
- Fluorescent indicators for Ca2+based on green fluorescent proteins and calmodulinNature, 1997
- Apoptosis by Death FactorCell, 1997
- Activation of actin-cleavable interleukin 1beta-converting enzyme (ICE) family protease CPP-32 during chemotherapeutic agent-induced apoptosis in ovarian carcinoma cells.1996
- Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosisNature, 1996
- Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transferCurrent Biology, 1996
- Protease activation during apoptosis: Death by a thousand cuts?Cell, 1995
- RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell deathCell, 1995