Plasma Inhibitory Activity against Tumour Necrosis Factor in Fulminant Hepatic Failure

1996 ◽  
Vol 90 (1) ◽  
pp. 77-80 ◽  
Author(s):  
Helen M. Keane ◽  
Nick Sheron ◽  
John Goka ◽  
Robin D. Hughes ◽  
Roger Williams
Keyword(s):  
Tumour Necrosis Factor ◽  
Normal Control ◽  
Fulminant Hepatic Failure ◽  
Hepatic Failure ◽  
Tumour Necrosis ◽  
Neutralization Capacity ◽  
Control Subjects ◽  
Significant Difference ◽  
Necrosis Factor

1. Soluble tumour necrosis factor receptors released into the circulation inhibit the effects of excess tumour necrosis factor-α and represent an important protective response. 2. In this study we have measured the levels of tumour necrosis factor and soluble tumour necrosis factor receptors p55 and p75 in the plasma of 10 patients with fulminant hepatic failure and 10 healthy control subjects. The capacity of the plasmas at varying dilutions to inhibit the biological activity of 1000 pg/ml of recombinant tumour necrosis factor in a tumour necrosis factor cytotoxicity assay in vitro was also determined. 3. The mean plasma levels of tumour necrosis factor in patients with fulminant hepatic failure (48.4 ± 10.9 pg/ml) were significantly increased compared with normal control subjects (6.1 ± 1.04 pg/ml, P < 0.01). Plasma soluble tumour necrosis factor receptors p55 and p75 were also significantly elevated in patients with fulminant hepatic failure (18.16 ± 9.94 ng/ml and 16.06 ± 9.93 ng/ml respectively) when compared with normal control subjects (1.28 ± 0.24 ng/ml and 1.62 ± 0.91 ng/ml, P < 0.001). 4. Fulminant hepatic failure plasma had a much lower capacity to inhibit tumour necrosis factor bioactivity in vitro, with a statistically significant difference between the inhibitory capacity of the fulminant hepatic failure and normal plasma seen at plasma dilutions of 1:5 and 1:20 (P < 0.05). 5. The reduced tumour necrosis factor neutralization capacity observed in fulminant hepatic failure, despite the increased levels of soluble tumour necrosis factor receptors, suggests enhanced susceptibility to the potential deleterious effects of tumour necrosis factor in fulminant hepatic failure.

ENHANCED TUMOUR NECROSIS FACTOR AND INTERLEUKIN-1 IN FULMINANT HEPATIC FAILURE

The Lancet ◽  
1988 ◽  
Vol 332 (8602) ◽  
pp. 72-74 ◽  
Author(s):  
Yasutoshi Muto ◽  
Anthony Meager ◽  
KayhanT. Nouri-Aria ◽  
GraemeJ.M. Alexander ◽  
AdrianL.W.F. Eddleston ◽  
...  
Keyword(s):  
Tumour Necrosis Factor ◽  
Fulminant Hepatic Failure ◽  
Hepatic Failure ◽  
Tumour Necrosis ◽  
Interleukin 1 ◽  
Necrosis Factor

scholarly journals Assessment Of Tumour Necrosis Factor-Alpha (Tnf- Α) And Creatinine Levels In Echis Ocellatus Bite Victims In Jos Metropolis, Nigeria

2016 ◽  
Vol 12 (21) ◽  
pp. 70
Author(s):  
Manafa P.O. ◽  
Osmond E.O. ◽  
Onyenekwe C.C. ◽  
Okeke C.O. ◽  
Chukwuma G.O. ◽  
...  
Keyword(s):  
Serum Level ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Alpha ◽  
Control Group ◽  
Necrosis Factor Alpha ◽  
Significant Difference ◽  
Factor Alpha ◽  
The Mean ◽  
Necrosis Factor

This study was designed to assess tumour necrosis factor-alpha and creatinine levels in Echis ocellatus bite victims. A total of 50 subjects were recruited. Out of this number, 40 were victims of E. ocellatus bite and the remaining 10 were non-victims of snake bite who served as the control group. Blood samples were collected from the victims within 24 hours of the snake bite and EchiTAb-G antivenom administered within the same period. Another batch of blood sample was collected 48 hours post-administration of the anti-venom. Tumour necrosis factor-alpha (TNF-alpha) levels were estimated by the Enzyme Linked Immunosorbent Assay technique while creatinine levels were determined using kinetic-spectrophotometric procedure. The mean serum levels of tumour necrosis factor-alpha and creatinine were significantly increased in E. ocellatus bite victims compared with the control group (P<0.05). Furthermore, the mean serum level of TNFalpha was significantly lower in E. ocellatus bite victims, post-administration of anti-venom, compared with the pre-administration of anti-venom (P<0.05). In contrast, no significant difference was observed in the mean serum level of creatinine in E. ocellatus bite victims, post-administration of anti-venom, compared with the pre-administration of anti-venom (P>0.05). Moreover, the mean serum level of creatinine was found to be significantly increased in E. ocellatus bite victims, post-administration of anti-venom, compared with the control group (P<0.05), while no significant difference was observed in the mean serum level of tumour necrosis factor-alpha in E. ocellatus bite victims, post-administration of anti-venom, compared with the control group(P>0.05). A positive correlation existed between tumour necrosis factor-alpha and creatinine levels in E. ocellatus bite subjects (r= 0.782). Echis ocellatus bite is a risk factor for renal damage indicated by an elevated serum creatinine, thus health authorities should make EchiTAb-G anti-venom freely available in health facilities and administered as quickly as possible to reduce the risk of renal damage in Echis ocellatus bite-prone areas.

scholarly journals Tumour necrosis factor-α induces hyperreactivity in tracheal smooth muscle of the guinea-pig in vitro

1998 ◽  
Vol 12 (1) ◽  
pp. 45-49 ◽  
Author(s):  
H-J. Pennings ◽  
K. Kramer ◽  
A. Bast ◽  
W.A. Buurman ◽  
E.F.M. Wouters
Keyword(s):  
Smooth Muscle ◽  
Guinea Pig ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tracheal Smooth Muscle ◽  
Factor I ◽  
Necrosis Factor

scholarly journals Association of a RING finger protein with the cytoplasmic domain of the human type-2 tumour necrosis factor receptor

1995 ◽  
Vol 309 (3) ◽  
pp. 825-829 ◽  
Author(s):  
H Y Song ◽  
D B Donner
Keyword(s):  
Tumour Necrosis Factor ◽  
Hybrid System ◽  
Tumour Necrosis ◽  
Ring Finger ◽  
Tnf Receptor ◽  
Intracellular Domain ◽  
Two Hybrid ◽  
Necrosis Factor

A human gene encoding a protein that specifically binds to the intracellular domain of the 75 kDa type-2 tumour necrosis factor (TNF) receptor (TNFR-2IC) has been identified using the yeast-based two-hybrid system. The N-terminal half of the TNF receptor-associated protein (TRAP) contains RING finger and zinc finger motifs often found in DNA-binding proteins including transcription factors. The 2.4 kb TRAP mRNA was barely detectable, if present at all, in lung, and variably expressed in heart, liver, placenta, brain, skeletal muscle, kidney and the pancreas; interestingly, the TRAP was more highly expressed in transformed cell lines than in normal tissues. This observation may be consistent with a role for this TRAP in promoting or regulating cellular proliferation. After in vitro transcription/translation and 35S labelling the TRAP was precipitated using a fusion protein consisting of glutathione S-transferase and the intracellular domain of TNFR-2 (TNFR-2IC), which showed that the two proteins directly interact in a mammalian cell-free system and also that identification of the TRAP was not an artifact of the two-hybrid system. By using truncated TNFR-2ICs for in vitro precipitation of 35S-TRAP, it was shown that the C-terminal half of the TNFR-2IC contains the domain necessary for interaction with TRAP. The TRAP identified in the present study shares considerable homology with, and may be the human homologue of, a mouse protein, TNF receptor-associated factor 2 (TRAF2), that binds mouse TNFR-2.

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