Share Email Print
cover

Proceedings Paper

Observation of interaction between bid and 14-3-3 proteins by FRET in living cell during TNF-a-induced apoptosis
Format Member Price Non-Member Price
PDF $14.40 $18.00

Paper Abstract

Caspase8 is activated and cleaves Bid into two fragments when cells are exposed to death-inducing molecules such as tumor necrosis factor-α (TNF-α). Then the C-terminal fragment relocates from cytosol to mitochondria and promotes the release of cytochrome c, in the final cellular apoptosis is induced. Despite recent progress in the study of Bid during apoptosis induction, it remains unclear how C-terminal fragment of Bid cleaved moves to mitochondria and then induces the release of cytochrome c and so on. The 14-3-3 proteins are known to sequester certain pro-apoptotic members of Bcl-2 family. In order to further study the biological action of Bid during apoptosis, especially under physiological condition of living cell, the plasmids pBid-CFP and pYFP-14-3-3 were constructed. By the transient transfection of pBid-CFP and pYFP-14-3-3, the dynamic process of interaction of Bid and 14-3-3 protein in individual living cell during the apoptosis was primarily investigated with FRET (fluorescent resonance energy transfer) technique by the use of fluorescence microscopy.

Paper Details

Date Published: 18 January 2005
PDF: 9 pages
Proc. SPIE 5630, Optics in Health Care and Biomedical Optics: Diagnostics and Treatment II, (18 January 2005); doi: 10.1117/12.572804
Show Author Affiliations
Jinjun Wang, South China Normal Univ. (China)
Tongsheng Chen, South China Normal Univ. (China)
Da Xing, South China Normal Univ. (China)
Fang Wang, South China Normal Univ. (China)


Published in SPIE Proceedings Vol. 5630:
Optics in Health Care and Biomedical Optics: Diagnostics and Treatment II
Britton Chance; Mingzhe Chen; Arthur E. T. Chiou; Qingming Luo, Editor(s)

© SPIE. Terms of Use
Back to Top