Orphan designation: autologous human adipose perivascular stromal cells genetically modified to secrete soluble tumour necrosis factor-related apoptosis-inducing ligand, The treatment of pancreatic cancer

2019 ◽  
Author(s):  
Keyword(s):  
Pancreatic Cancer ◽  
Tumour Necrosis Factor ◽  
Stromal Cells ◽  
Tumour Necrosis ◽  
Genetically Modified ◽  
Orphan Designation ◽  
Necrosis Factor

Anti-Proliferative Effect on Human Pancreatic Cancer Cells of Natural Human Tumour Necrosis Factor-β Combined with Natural Human Interferon-α or Interferon-γ

1992 ◽  
Vol 20 (2) ◽  
pp. 112-120 ◽  
Author(s):  
T Watanabe ◽  
S Fuchimoto ◽  
N Matsubara ◽  
H Iwagaki ◽  
K Orita
Keyword(s):  
Pancreatic Cancer ◽  
Tumour Necrosis Factor ◽  
Cell Lines ◽  
Tumour Necrosis ◽  
Interferon Γ ◽  
Human Pancreatic Cancer ◽  
Human Interferon ◽  
Interferon Α ◽  
Proliferative Effect ◽  
Necrosis Factor

The anti-proliferative effects of natural cytokines, human tumour necrosis factor-β, natural human interferon-α and natural human interferon-γ, on three human pancreatic cancer cell lines (PANC-1, MIA PaCa-2 and BxPC-3) were investigated in vitro. The anti-proliferative effect was determined using the dye uptake method and analysed for synergism by the median effect principle. Tumour necrosis factor-β, as a single agent, had little anti-proliferative effect on any of the three cell lines, whereas interferon-α and interferon-γ exhibited a strong anti-proliferative effect against two cell lines (MIA PaCa-2 and BxPC-3) and one cell line (BxPC-3), respectively. When tumour necrosis factor-β and interferon-α were administered together (ratio 1:1), a synergistic effect was observed against PANC-1 cells. The combination of tumour necrosis factor-β and interferon-γ (ratio 10:1) was synergisic against both PANC-1 and MIA PaCa-2 cells. A synergistic anti-proliferative effect of tumour necrosis factor-β and interferons was, therefore, observed even for cell lines that showed little biological response to each cytokine alone. The data suggest that some future improvement in the treatment of pancreatic cancer may be obtained by using combination cytokine therapy.

scholarly journals Interleukin-6- and tumour necrosis factor α-mediated expression of hepatocyte growth factor by stromal cells and its involvement in the growth of endometriosis

2005 ◽  
Vol 20 (10) ◽  
pp. 2715-2723 ◽  
Author(s):  
Khaleque Newaz Khan ◽  
Hideaki Masuzaki ◽  
Akira Fujishita ◽  
Michio Kitajima ◽  
Koichi Hiraki ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tumour Necrosis Factor ◽  
Stromal Cells ◽  
Interleukin 6 ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Hepatocyte Growth ◽  
Necrosis Factor

scholarly journals Two polymorphisms of the tumour necrosis factor gene do not influence survival in pancreatic cancer

1999 ◽  
Vol 117 (3) ◽  
pp. 425-429 ◽  
Author(s):  
Barber ◽  
Powell ◽  
Lynch ◽  
Gough ◽  
Fearon ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Factor Gene ◽  
Necrosis Factor

Implantation: Tumour necrosis factor α inhibits in-vitro decidualization of human endometrial stromal cells

1994 ◽  
Vol 9 (12) ◽  
pp. 2411-2417 ◽  
Author(s):  
T. Inoue ◽  
H. Kanzaki ◽  
M. Iwai ◽  
K. Imai ◽  
S. Narukawa ◽  
...  
Keyword(s):  
Tumour Necrosis Factor ◽  
Stromal Cells ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Endometrial Stromal Cells ◽  
Factor Α ◽  
Necrosis Factor

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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