scholarly journals Protective Effect of Dexmedetomidine on Acute Lung Injury via the Upregulation of Tumour Necrosis Factor-α-Induced Protein-8-like 2 in Septic Mice

Inflammation ◽  
2020 ◽  
Vol 43 (3) ◽  
pp. 833-846 ◽  
Author(s):  
Qian Kong ◽  
Xiaojing Wu ◽  
Zhen Qiu ◽  
Qin Huang ◽  
Zhongyuan Xia ◽  
...  
2004 ◽  
Vol 53 (8) ◽  
pp. 727-733 ◽  
Author(s):  
Chiharu Nara ◽  
Kazuhiro Tateda ◽  
Tetsuya Matsumoto ◽  
Akira Ohara ◽  
Shuichi Miyazaki ◽  
...  

2000 ◽  
Vol 99 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Chi-Huei CHIANG ◽  
Chin-Pyng WU ◽  
Wann-Cherng PERNG ◽  
Horng-Chin YAN ◽  
Cheng-Ping YU

Experimental interventions that reduce ischaemia/reperfusion (I/R) lung injury can be used to improve the properties of preservation solutions. We attempted to increase the attenuation of I/R injury by University of Wisconsin solution (UW) by adding an antibody against tumour necrosis factor-α (TNF-α), to neutralize TNF-α, and/or by adding 3-deaza-adenosine (c3-Ado), to inhibit leucocyte adhesion and the biosynthesis of ICAM-1 (intercellular cell-adhesion molecule 1). We examined I/R injury using an isolated rat lung model. Six different solutions were perfused individually, followed by evaluation of I/R injury: (1) 0.9% NaCl (normal saline; NS), (2) NS+anti-TNF-α antibody, (3) UW alone, (4) UW+anti-TNF-α, (5) UW+c3-Ado and (6) UW+anti-TNF-α+c3-Ado. Haemodynamic changes, lung weight gain, capillary filtration coefficient, TNF-α levels and lung pathology were analysed in order to evaluate I/R injury. Compared with lungs perfused with NS, lungs treated with NS+anti-TNF-α showed less I/R injury. The addition of anti-TNF-α and/or c3-Ado to UW reduced I/R injury compared with unmodified UW. Among the six solutions tested, UW containing anti-TNF-α antibody reduced I/R injury to the greatest extent. We conclude that addition of anti-TNF-α antibody or c3-Ado protects against I/R lung injury when using UW. Further investigation of the improved properties of modified UWs would be beneficial with regard to lung transplantation research.


2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.


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