Suppression of macrophage interleukin-12 and tumour necrosis factor-α production in mice infected with Toxocara canis

2001 ◽  
Vol 23 (6) ◽  
pp. 305-311 ◽  
Author(s):  
Etsushi Kuroda ◽  
Yasuhiro Yoshida ◽  
Bao En Shan ◽  
Uki Yamashita
Immunology ◽  
1996 ◽  
Vol 87 (3) ◽  
pp. 467-474 ◽  
Author(s):  
N. A. GIESE ◽  
R. T. GAZZINELLI ◽  
J. K. ACTOR ◽  
R. A. MORAWETZ ◽  
M. SARZOTTI ◽  
...  

Author(s):  
Christopher Willy Schwarz ◽  
Nikolai Loft ◽  
Mads Kirchheiner Rasmussen ◽  
Christoffer V. Nissen ◽  
Tomas Norman Dam ◽  
...  

Identifying patient characteristics associated withachieving treatment response to biologics in patients with psoriasis could prevent expensive switching between biologics. The aim of this study was to identifypatient characteristics that predict the efficacy of treatment for biologics that inhibit tumour necrosis factor-α, interleukin-12/-23, and -17A. The study investigated biologic-naïve patients from the DERMBIO registry treated with adalimumab, etanercept, infliximab, secukinumab, or ustekinumab. Multivariable logistic models were conducted to assess associations between patient characteristics and treatment response. A total of 2,384 patients were included (adalimumab n = 911; etanercept n = 327; infliximab n = 152; secukinumab n = 323; ustekinumab n = 671). Smoking (odds ratio 0.74; 95% confidence interval (CI) 0.56–0.97; p = 0.03) and higher bodyweight (odds ratio 0.989; 95% CI 0.984–0.994; p < 0.001) reduced the odds of achieving response defined as Psoriasis Area and Severity Index ≤2.0 after 6 months of treatment. In conclusion, higher bodyweight and smoking were associated with a reduced probability of treatment response for tumour necrosis factor-α inhibitors, ustekinumab, and secukinumab.


2000 ◽  
Vol 129 (5) ◽  
pp. 909-914 ◽  
Author(s):  
György Haskó ◽  
David G Kuhel ◽  
Andrew L Salzman ◽  
Csaba Szabó

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  

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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