scholarly journals A Study of Single Nucleotide Polymorphisms of Tumour Necrosis Factor α-1031 And Tumour Necrosis Factor β+ 252 in Chronic Rhinosinusitis

2017 ◽  
Vol 10 (3) ◽  
pp. 241-247 ◽  
Author(s):  
Khairunnisak Misron ◽  
Suzina Sheikh Ab Hamid ◽  
Azlina Ahmad ◽  
Ramiza Ramza Ramli
Keyword(s):  
Single Nucleotide Polymorphisms ◽  
Chronic Rhinosinusitis ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Nucleotide Polymorphisms ◽  
Tumour Necrosis Factor Α ◽  
Single Nucleotide ◽  
Factor Α ◽  
Necrosis Factor

Analysis of single nucleotide polymorphisms (SNPS) in the Tumour Necrosis Factor (TNF) gene in celiac disease

2000 ◽  
Vol 118 (4) ◽  
pp. A365
Author(s):  
Jacqueline S. Daly ◽  
Ross McManus ◽  
Rosemary Whelan ◽  
Barbara Ryan ◽  
Yeng Shiong Ang ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Single Nucleotide Polymorphisms ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Nucleotide Polymorphisms ◽  
Single Nucleotide ◽  
Tnf Gene ◽  
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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