|Citation||Bardet, P.L., Kolahgar, G.I., Mynett, A., Miguel-Aliaga, I., Briscoe, J., Meier, P., Vincent, J.P. (2008). A fluorescent reporter of caspase activity for live imaging. Proc. Natl. Acad. Sci. U.S.A. 105(37): 13901--13905. (Export to RIS)|
|Publication Type||Research paper|
|PubMed Abstract||There is a growing interest in the mechanisms that control the apoptosis cascade during development and adult life. To investigate the regulatory events that trigger apoptosis in whole tissues, we have devised a genetically encoded caspase sensor that can be detected in live and fixed tissue by standard confocal microscopy. The sensor comprises two fluorophores, mRFP, monomeric red fluorescent protein (mRFP) and enhanced green fluorescent protein (eGFP), that are linked by an efficient and specific caspase-sensitive site. Upon caspase activation, the sensor is cleaved and eGFP translocates to the nucleus, leaving mRFP at membranes. This is detected before other markers of apoptosis, including anti-cleaved caspase 3 immunoreactivity. Moreover, the sensor does not perturb normal developmental apoptosis and is specific, as cleavage does not occur in Drosophila embryos that are unable to activate the apoptotic cascade. Importantly, dying cells can be recognized in live embryos, thus opening the way for in vivo imaging. As expected from the high conservation of caspases, it is also cleaved in dying cells of chick embryos. It is therefore likely to be generally useful to track the spatiotemporal pattern of caspase activity in a variety of species.|
|Personal communication to FlyBase||UAS-Apoliner.
Vincent, 2010.9.7, UAS-Apoliner. [FBrf0211799]
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|All updates||Click here to see a list of all updates to this record from FB2010_08 and on.|
|Language of Publication||English|
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|Abbreviation||Proc. Natl. Acad. Sci. U.S.A.|
|Title||Proceedings of the National Academy of Sciences of the United States of America|
|Data from Reference|
|Natural transposons (1)|