scholarly journals Do anti‐tumour necrosis factor‐α biologics affect subclinical measures of atherosclerosis and arteriosclerosis? A systematic review

2020 ◽  
Vol 86 (5) ◽  
pp. 837-851 ◽  
Author(s):  
Laurence Knowles ◽  
Nida Nadeem ◽  
Philip J. Chowienczyk
Keyword(s):  
Systematic Review ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals A systematic review and meta-analysis of biological treatments targeting tumour necrosis factor α for sciatica

2013 ◽  
Vol 22 (9) ◽  
pp. 1921-1935 ◽  
Author(s):  
Nefyn H. Williams ◽  
Ruth Lewis ◽  
Nafees Ud Din ◽  
Hosam E. Matar ◽  
Deborah Fitzsimmons ◽  
...  
Keyword(s):  
Systematic Review ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Meta Analysis ◽  
Tumour Necrosis Factor Α ◽  
Biological Treatments ◽  
Factor Α ◽  
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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