Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury
Article first published online: 13 JAN 2003
Journal of Neurochemistry
Volume 84, Issue 3, pages 514–521, February 2003
How to Cite
Seidberg, N. A., Clark, R. S. B., Zhang, X., Lai, Y., Chen, M., Graham, S. H., Kochanek, P. M., Watkins, S. C. and Marion, D. W. (2003), Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury. Journal of Neurochemistry, 84: 514–521. doi: 10.1046/j.1471-4159.2003.01547.x
- Issue published online: 13 JAN 2003
- Article first published online: 13 JAN 2003
- Received August 31, 2002; revised manuscript received October 11, 2002; accepted October 17, 2002.
- head injury;
The stress response in injured brain is well characterized after experimental ischemic and traumatic brain injury (TBI); however, the induction and regulation of the stress response in humans after TBI remains largely undefined. Accordingly, we examined injured brain tissue from adult patients (n = 8) that underwent emergent surgical decompression after TBI, for alterations in the inducible 72-kDa heat shock protein (Hsp70), the constitutive 73-kDa heat shock protein (Hsc70), and isoforms of the chaperone cofactor BAG-1. Control samples (n = 6) were obtained postmortem from patients dying of causes unrelated to CNS trauma. Western blot analysis showed that Hsp70, but not Hsc70, was increased in patients after TBI versus controls. Both Hsp70 and Hsc70 coimmunoprecipitated with the cofactor BAG-1. The 33 and 46, but not the 50-kDa BAG-1 isoforms were increased in patients after TBI versus controls. The ratio of the 46/33-kDa isoforms was increased in TBI versus controls, suggesting negative modulation of Hsp70/Hsc70 protein refolding activity in injured brain. These data implicate induction of the stress response and its modulation by the chaperone cofactor and Bcl-2 family member BAG-1, after TBI in humans.