Interference of HIV-1 Nef in the sphingomyelin transduction pathway activated by tumour necrosis factor-α in human glial cells

AIDS ◽  
1997 ◽  
Vol 11 (1) ◽  
pp. F1-F7 ◽  
Author(s):  
Alain Richard ◽  
Gilles Robichaud ◽  
Réjean Lapointe ◽  
Sylvain Bourgoin ◽  
André Darveau ◽  
...  
Keyword(s):  
Tumour Necrosis Factor ◽  
Glial Cells ◽  
Tumour Necrosis ◽  
Transduction Pathway ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Hiv 1 ◽  
Necrosis Factor

Role of salivary tumour necrosis factor α in HIV-positive patients with oral manifestations

2007 ◽  
Vol 18 (8) ◽  
pp. 565-569 ◽  
Author(s):  
Tomoaki Ino ◽  
Akio Tada ◽  
Akira Tominaga ◽  
Yasuo Komori ◽  
Hiroshige Chiba ◽  
...  
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Oral Manifestations ◽  
Tumour Necrosis Factor Α ◽  
Cd4 Cells ◽  
Tnf Α ◽  
Factor Α ◽  
Hiv 1 ◽  
Necrosis Factor

In HIV-1-infected patients, oral manifestations such as recurrent apthous ulcers are often seen. A total of 29 HIV-infected patients were examined to determine salivary tumour necrosis factor α (TNF α) concentrations by enzyme-linked immunosorbent assay, the amount of HIV-1 RNA copy by Amplicor HIV-1 Monitor test, number of CD4 cells by flow cytometry and oral manifestations by oral examination. TNF α concentration was significantly correlated with the amount of HIV-1 RNA, however, not with the number of CD4 cells in HIV-1-infected patients. Further, patients with oral manifestations showed significantly higher concentrations of TNF α in saliva and HIV-1 RNA copies in serum than those without oral manifestations. Following recovery from oral ulcers, TNF α concentration was decreased by half to 20 times lower than the level of that during ulcer incidence. Our results suggest that salivary TNF α is a good indicator for oral manifestations and HIV RNA amounts in HIV-1-infected patients.

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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