Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury.
作者： Neal A. Seidberg , Robert S. B. Clark , Xiaopeng Zhang , Yichen Lai , Minzhi Chen
DOI: 10.1046/J.1471-4159.2003.01547.X
关键词: Endocrinology 、 Western blot 、 Traumatic brain injury 、 Transcription factor 、 Pathology 、 Biology 、 Heat shock protein 、 Hsp70 、 Chaperone (protein) 、 Gene isoform 、 Human brain 、 Internal medicine
摘要: The stress response in injured brain is well characterized after experimental ischemic and traumatic injury (TBI); however, the induction regulation of humans TBI remains largely undefined. Accordingly, we examined tissue from adult patients (n = 8) that underwent emergent surgical decompression TBI, for alterations inducible 72-kDa heat shock protein (Hsp70), constitutive 73-kDa (Hsc70), isoforms chaperone cofactor BAG-1. Control samples 6) were obtained postmortem dying causes unrelated to CNS trauma. Western blot analysis showed Hsp70, but not Hsc70, was increased versus controls. Both Hsp70 Hsc70 coimmunoprecipitated with 33 46, 50-kDa BAG-1 ratio 46/33-kDa controls, suggesting negative modulation Hsp70/Hsc70 refolding activity brain. These data implicate its by Bcl-2 family member BAG-1, humans.
sci-hub.se 参考文章(52)
M Jäättelä, Dorte Wissing, Paul A Bauer, Gloria C Li, None, Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. The EMBO Journal. ,vol. 11, pp. 3507- 3512 ,(1992) , 10.1002/J.1460-2075.1992.TB05433.X
Stephen M. Massa, Raymond A. Swanson, Frank R Sharp, The stress gene response in brain. Cerebrovascular and brain metabolism reviews. ,vol. 8, pp. 95- 158 ,(1996)
K.-A. Hossmann, Chapter 11 Disturbances of cerebral protein synthesis and ischemic cell death Progress in Brain Research. ,vol. 96, pp. 161- 177 ,(1993) , 10.1016/S0079-6123(08)63265-3
Georg Schett, Carl-Walter Steiner, Marion Gröger, Stefan Winkler, Winfried Graninger, Josef Smolen, Qingbo Xu, Günter Steiner, None, Activation of Fas inhibits heat-induced activation of HSF1 and up-regulation of hsp70 The FASEB Journal. ,vol. 13, pp. 833- 842 ,(1999) , 10.1096/FASEBJ.13.8.833
RP Simon, H Cho, R Gwinn, DH Lowenstein, The temporal profile of 72-kDa heat-shock protein expression following global ischemia The Journal of Neuroscience. ,vol. 11, pp. 881- 889 ,(1991) , 10.1523/JNEUROSCI.11-03-00881.1991
Randall A. Ruppel, Patrick M. Kochanek, P.David Adelson, Marie E. Rose, Stephen R. Wisniewski, Michael J. Bell, Robert S.B. Clark, Donald W. Marion, Steven H. Graham, Excitatory amino acid concentrations in ventricular cerebrospinal fluid after severe traumatic brain injury in infants and children: the role of child abuse The Journal of Pediatrics. ,vol. 138, pp. 18- 25 ,(2001) , 10.1067/MPD.2001.110979
Hirokazu Tanno, Russ P. Nockels, Lawrence H. Pitts, Linda J. Noble, Immunolocalization of heat shock protein after fluid percussive brain injury and relationship to breakdown of the blood-brain barrier Journal of Cerebral Blood Flow and Metabolism. ,vol. 13, pp. 116- 124 ,(1993) , 10.1038/JCBFM.1993.14
Daniel H. Lowenstein, Ryder P. Gwinn, M.Serena Seren, Roger P. Simon, Tracy K. McIntosh, Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or the 72 kDA heat-shock protein in three models of acute CNS injury Molecular Brain Research. ,vol. 22, pp. 299- 308 ,(1994) , 10.1016/0169-328X(94)90058-2
G. C. Li, Z. Werb, Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 79, pp. 3218- 3222 ,(1982) , 10.1073/PNAS.79.10.3218
James S. Someren, Lee E. Faber, Janet D. Klein, James A. Tumlin, Heat Shock Proteins 70 and 90 Increase Calcineurin Activity in Vitro through Calmodulin-Dependent and Independent Mechanisms Biochemical and Biophysical Research Communications. ,vol. 260, pp. 619- 625 ,(1999) , 10.1006/BBRC.1999.0800