scholarly journals Tumour necrosis factor‐α promotes liver ischaemia‐reperfusion injury through the PGC ‐1α/Mfn2 pathway

2014 ◽  
Vol 18 (9) ◽  
pp. 1863-1873 ◽  
Author(s):  
Jun Li ◽  
Wenbo Ke ◽  
Qi Zhou ◽  
Yongzhong Wu ◽  
Hong Luo ◽  
...  
Keyword(s):  
Reperfusion Injury ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Ischaemia Reperfusion Injury ◽  
Ischaemia Reperfusion ◽  
Factor Α ◽  
Necrosis Factor ◽  
Liver Ischaemia

scholarly journals The involvement of tumour necrosis factor-α in the protective effects of 17β oestradiol in splanchnic ischaemia-reperfusion injury

1997 ◽  
Vol 121 (8) ◽  
pp. 1782-1788 ◽  
Author(s):  
Francesco Squadrito ◽  
Domenica Altavilla ◽  
Giovanni Squadrito ◽  
Giuseppe M. Campo ◽  
Mariarita Arlotta ◽  
...  
Keyword(s):  
Reperfusion Injury ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Protective Effects ◽  
Tumour Necrosis Factor Α ◽  
Ischaemia Reperfusion Injury ◽  
Ischaemia Reperfusion ◽  
Factor Α ◽  
Necrosis Factor

Use of anti-(tumour necrosis factor-α) antibody or 3-deaza-adenosine as additives to promote protection by University of Wisconsin solution in ischaemia/reperfusion injury

2000 ◽  
Vol 99 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Chi-Huei CHIANG ◽  
Chin-Pyng WU ◽  
Wann-Cherng PERNG ◽  
Horng-Chin YAN ◽  
Cheng-Ping YU
Keyword(s):  
Lung Injury ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
University Of Wisconsin ◽  
Ischaemia Reperfusion ◽  
Tnf Α ◽  
Factor Α ◽  
Wisconsin Solution ◽  
Necrosis Factor

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.

Tumour necrosis factor mediates e-selectin production and leukocyte accumulation in myocardial ischaemia-reperfusion injury

1995 ◽  
Vol 31 (5) ◽  
pp. 281-288 ◽  
Author(s):  
Mariapatrizia Ioculano ◽  
Domenica Altavilla ◽  
Francesco Squadrito ◽  
Patrizia Canals ◽  
Giovanni Squadrito ◽  
...  
Keyword(s):  
Reperfusion Injury ◽  
Tumour Necrosis Factor ◽  
Myocardial Ischaemia ◽  
Tumour Necrosis ◽  
Ischaemia Reperfusion Injury ◽  
Leukocyte Accumulation ◽  
Ischaemia Reperfusion ◽  
Necrosis Factor

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

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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