Slow rise of Ca2+and slow release of reactive oxygen species are two cross-talked events important in tumour necrosis factor-α-mediated apoptosis

2000 ◽  
Vol 33 (3) ◽  
pp. 295-304 ◽  
Author(s):  
Samuel Ko ◽  
T.T. Kwok ◽  
K.P. Fung ◽  
Y.M. Choy ◽  
C.Y. Lee ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Slow Release ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Tumour Necrosis Factor Α ◽  
Slow Rise ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α

1989 ◽  
Vol 263 (2) ◽  
pp. 539-545 ◽  
Author(s):  
B Meier ◽  
H H Radeke ◽  
S Selle ◽  
M Younes ◽  
H Sies ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Interleukin 1 ◽  
Human Fibroblasts ◽  
Spectral Characteristics ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Necrosis Factor Alpha ◽  
Necrosis Factor

Human fibroblasts in primary culture released reactive oxygen species upon stimulation with cytokines such as interleukin-1 alpha (IL-1) or tumour necrosis factor-alpha (TNF). The primary radical produced was O2.- as determined by e.s.r. spin trapping and cytochrome c reduction. In contrast to the oxidative burst in granulocytes and monocytes, radical formation took place continuously for at least 4 h. Low-level chemiluminescence was increased by stimulation with IL-1 and TNF. Spectral characteristics and tests with azide led to the conclusion that the photoemissive species were excited carbonyls and not singlet oxygen. Further, there was a liberation of ethane from the cells. Radical production and light emission were not altered by either xanthine or allopurinol, nor by azide, cyanide or rotenone. O2.- production increased in the presence of NADH or NADPH, making an NAD(P)H oxidase a likely source.

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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