Abstract
A modified method of multiphoton fluorescence resonance energy transfer (FRET) for investigation of traumatic brain injury (TBI) is discussed. The method allows for the direct assessment of protein-protein interactions in tissue sections through the use of a dual-label immunofluorescent approach. It was found that the bcl-2-related proteins BAD and Bcl-xL heterodimerize in a pro-apoptotic fashion within traumatically injured axons following TBI. The results further define the activation of a calcineurin mediated, BAD/Bcl-xL apoptic pathway as a secondary mechanism of injury in TBI.
Original language | English |
---|---|
Pages (from-to) | 52-62 |
Number of pages | 11 |
Journal | Proceedings of SPIE - The International Society for Optical Engineering |
Volume | 5323 |
DOIs | |
State | Published - 2004 |
Externally published | Yes |
Event | Progress in Biomedical Optics and Imaging - Multiphoton Microscopy in the Biomedical Sciences IV - San Jose, CA, United States Duration: 25 Jan 2004 → 27 Jan 2004 |
Keywords
- BAD
- Bcl-xL
- Caspase 3
- Cytochrome c
- Fluorescent Resonance Energy Transfer (FRET)
- Traumatic axonal injury