Redox-based endoplasmic reticulum dysfunction in neurological diseases

作者: Gábor Bánhegyi , József Mandl , Miklós Csala

DOI: 10.1111/J.1471-4159.2008.05571.X

关键词:

摘要: The redox homeostasis of the endoplasmic reticulum lumen is characteristically different from that other subcellular compartments. concerted action membrane transport processes and oxidoreductase enzymes maintain oxidized state thiol-disulfide reducing pyridine nucleotide systems, which are prerequisites for normal functions organelle. powerful thiol-oxidizing machinery allows oxidative protein folding but continuously challenges local antioxidant defense. Alterations cellular environment either in oxidizing or direction affect processing may induce stress unfolded response. activated signaling pathways attempt to restore balance between loading apoptosis if fails. Recent findings strongly support involvement this mechanism brain ischemia, neuronal degenerative diseases traumatic injury. changes integral parts pathomechanism neurological diseases, as causative agents, complications.

参考文章(158)
Christoph Aufenberg, Simone Wenkel, Angelika Mautes, Wulf Paschen, Spinal cord trauma activates processing of xbp1 mRNA indicative of endoplasmic reticulum dysfunction. Journal of Neurotrauma. ,vol. 22, pp. 1018- 1024 ,(2005) , 10.1089/NEU.2005.22.1018
Alex Odermatt, Atanas G. Atanasov, Zoltan Balazs, Roberto A.S. Schweizer, Lyubomir G. Nashev, Daniela Schuster, Thierry Langer, Why is 11β-hydroxysteroid dehydrogenase type 1 facing the endoplasmic reticulum lumen?: Physiological relevance of the membrane topology of 11β-HSD1 Molecular and Cellular Endocrinology. ,vol. 248, pp. 15- 23 ,(2006) , 10.1016/J.MCE.2005.11.040
Bernhard Gess, Karl-Heinz Hofbauer, Roland H. Wenger, Christiane Lohaus, Helmut E. Meyer, Armin Kurtz, The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. FEBS Journal. ,vol. 270, pp. 2228- 2235 ,(2003) , 10.1046/J.1432-1033.2003.03590.X
Wulf Paschen, Ido Yatsiv, Shai Shoham, Esther Shohami, Brain trauma induces X‐box protein 1 processing indicative of activation of the endoplasmic reticulum unfolded protein response Journal of Neurochemistry. ,vol. 88, pp. 983- 992 ,(2004) , 10.1046/J.1471-4159.2003.02218.X
Michio Tamatani, Tomohiro Matsuyama, Atsushi Yamaguchi, Noriaki Mitsuda, Yoshitane Tsukamoto, Manabu Taniguchi, Yong Ho Che, Kentaro Ozawa, Osamu Hori, Hiroyuki Nishimura, Atsuko Yamashita, Masaru Okabe, Hideki Yanagi, David M. Stern, Satoshi Ogawa, Masaya Tohyama, ORP150 protects against hypoxia/ischemia-induced neuronal death. Nature Medicine. ,vol. 7, pp. 317- 323 ,(2001) , 10.1038/85463
Y F Yang, W W Wells, D P Xu, P A Rocque, Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. Journal of Biological Chemistry. ,vol. 265, pp. 15361- 15364 ,(1990) , 10.1016/S0021-9258(18)55401-6
Sonja Althausen, Thorsten Mengesdorf, Günter Mies, Laszlo Oláh, Angus C. Nairn, Christopher G. Proud, Wulf Paschen, Changes in the phosphorylation of initiation factor eIF‐2α, elongation factor eEF‐2 and p70 S6 kinase after transient focal cerebral ischaemia in mice Journal of Neurochemistry. ,vol. 78, pp. 779- 787 ,(2001) , 10.1046/J.1471-4159.2001.00462.X
B. R. Hu, M. E. Martone, Y. Z. Jones, C. L. Liu, Protein aggregation after transient cerebral ischemia. The Journal of Neuroscience. ,vol. 20, pp. 3191- 3199 ,(2000) , 10.1523/JNEUROSCI.20-09-03191.2000
I. Braakman, J. Helenius, A. Helenius, Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. The EMBO Journal. ,vol. 11, pp. 1717- 1722 ,(1992) , 10.1002/J.1460-2075.1992.TB05223.X
Anissa Belkaid, Jean-Christophe Currie, Julie Desgagnés, Borhane Annabi, The chemopreventive properties of chlorogenic acid reveal a potential new role for the microsomal glucose-6-phosphate translocase in brain tumor progression Cancer Cell International. ,vol. 6, pp. 7- 7 ,(2006) , 10.1186/1475-2867-6-7