Corrigendum to “The crystal structure of FdxA, a 7Fe ferredoxin from Mycobacterium smegmatis” [Biochem. Biophys. Res. Commun. 360 (2007) 97–102]

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• 作者：Stefano Ricagno ; Matteo de Rosa ; Aless ; ro Aliverti ; Giuliana Zanetti ; Martino Bolognesi
• 关键词：Proteasome ; Ubiquitin ; Ubiquitin– ; protein conjugates ; Ubiquitylation ; Heart transplantation ; Hypothermic organ preservation ; Cold ischemia ; Reperfusion
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2008
• 出版时间：25 January 2008
• 年：2008
• 卷：365
• 期：4
• 页码：890
• 全文大小：61 K

文摘

Recent observations suggest that the ubiquitin–proteasome system (UPS) contributes to the pathophysiology of myocardial ischemia–reperfusion injury. Since its regulation during cold ischemia–reperfusion is unknown, we evaluated the cardiac UPS in a model of heart transplantation in mice. Cardiac ubiquitylation rates and ubiquitin–protein conjugates increased after 3 h of cold ischemia (CI) and normalized post-transplant. 20S proteasome content and proteasome peptidase activities were unchanged after CI. 4 h/24 h post-transplant 20S proteasome concentrations decreased and chymotryptic-like but not tryptic-like proteasome peptidase activity was inactivated. Epoxomicin sensitivity of the proteasome increased 5.7-fold during CI and normalized 4 h/24 h post-transplant. This was accompanied by the disappearance of a 13.5 kDa-ubiquitin-conjugate during CI that could be attenuated by addition of epoxomicin to the preservation fluid. We conclude that substrate specificity of the proteasome changes during cold ischemia and that proteasome inhibition preserves the physiological ubiquitin–protein conjugate pool during organ preservation. Reduced proteasome activity during reperfusion is caused by a decrease in proteasome content and enzyme inhibition.