Evaluation of tumour necrosis factor-α, soluble P-selectin, γ-glutamyl transferase, glutathione S-transferase-π and α-fetoprotein in patients with hepatocellular carcinoma before and during chemotherapy

2006 ◽  
Vol 63 (2) ◽  
pp. 74-78 ◽  
Author(s):  
M.I. Morsi ◽  
A.E. Hussein ◽  
M. Mostafa ◽  
E. El-Abd ◽  
N.A. Abd El-Moneim
Keyword(s):  
Hepatocellular Carcinoma ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Glutathione S Transferase ◽  
Soluble P ◽  
Glutamyl Transferase ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Abscopal regression of hepatocellular carcinoma after radiotherapy for bone metastasis

Gut ◽  
1998 ◽  
Vol 43 (4) ◽  
pp. 575-577 ◽  
Author(s):  
K Ohba ◽  
K Omagari ◽  
T Nakamura ◽  
N Ikuno ◽  
S Saeki ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Bone Metastasis ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Serum Levels ◽  
Tumour Necrosis Factor Α ◽  
Vertebral Bone ◽  
Old Japanese ◽  
Factor Α ◽  
Necrosis Factor

Spontaneous regression of hepatocellular carcinoma is a rare phenomenon. Abscopal regression of tumours resulting from the effect of irradiation of a tissue on a remote non-irradiated tissue is also rare. The case of a 76 year old Japanese man with hepatocellular carcinoma that regressed after radiotherapy for thoracic vertebral bone metastasis is described. Serum levels of tumour necrosis factor-α increased after radiotherapy. The findings suggests that such abscopal related regression may be associated with host immune response, involving cytokines such as tumour necrosis factor-α.

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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