Galloyl benzamide-based compounds modulating tumour necrosis factor α-stimulated c-Jun N-terminal kinase and p38 mitogen-activated protein kinase signalling pathways

2015 ◽  
Vol 67 (10) ◽  
pp. 1380-1392 ◽  
Author(s):  
Valentina Leo ◽  
Angela Stefanachi ◽  
Carmela Nacci ◽  
Francesco Leonetti ◽  
Modesto de Candia ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Mitogen Activated Protein Kinase ◽  
Signalling Pathways ◽  
Tumour Necrosis Factor Α ◽  
Mitogen Activated Protein ◽  
Factor Α ◽  
Protein Kinase Signalling ◽  
Necrosis Factor

scholarly journals Phosphatidylcholine-specific phospholipase C and phospholipase D are respectively implicated in mitogen-activated protein kinase and nuclear factor κB activation in tumour-necrosis-factor-α-treated immature acute-myeloid-leukaemia cells

2000 ◽  
Vol 351 (2) ◽  
pp. 459-467 ◽  
Author(s):  
Isabelle PLO ◽  
Dominique LAUTIER ◽  
Thierry LEVADE ◽  
Hadef SEKOURI ◽  
JeanPierre JAFFRÉZOU ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Tumour Necrosis ◽  
Nuclear Factor Κb ◽  
Mitogen Activated Protein Kinase ◽  
Nuclear Factor ◽  
Tumour Necrosis Factor Α ◽  
Proliferative Effect ◽  
Mitogen Activated Protein ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor-α (TNFα) has been reported to induce potent growth inhibition of committed myeloid progenitor cells, whereas it is a potential growth stimulator of human CD34+CD38- multipotent haematopoietic cells. The present study was aimed at evaluating the respective role of two phospholipases, phosphatidylcholine-specific phospholipase C (PC-PLC) and phospholipase D (PLD) in the response of the CD34+ CD38- KG1a cells to TNFα. In these cells TNFα triggered phosphoinositide 3-kinase (PI3K)-dependent PC hydrolysis within 4–8min with concomitant production of both diacylglycerol (DAG) and phosphocholine (P-chol). DAG and P-chol production was accompanied by extracellular-signal-related protein kinase-1 (‘ERK-1’) activation and DNA-synthesis stimulation. PC-PLC stimulation was followed by PI3K-independent PLD activation with concomitant phosphatidic acid (PA) production followed by PA-derived DAG accumulation and sustained nuclear factor κB (NF-κB) activation. PLD/NF-κB signalling activation played no role in the TNFα proliferative effect and conferred no consistent protection of KG1a cells towards antileukaemic agents. Altogether these results suggest that, in KG1a cells, TNFα can stimulate in parallel PC-PLC and PLD, whose lipid products activate in turn mitogen-activated protein kinase (MAP kinase) and NF-κB signalling respectively. Finally, our study suggests that PC-PLC, but not PLD, plays a role in the TNFα proliferative effect in immature myeloid cells.

Protein kinase inhibitor attenuates an increase in endothelial monolayer permeability induced by tumour necrosis factor-α

Respirology ◽  
1997 ◽  
Vol 2 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Makoto YONEMARU ◽  
Ikuma KASUGA ◽  
Hiroshi KUSUMOTO ◽  
Hiroshi KIYOKAWA ◽  
Saburo KUWABARA ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Tumour Necrosis Factor Α ◽  
Endothelial Monolayer ◽  
Monolayer Permeability ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Tumour necrosis factor-induced activation of c-Jun N-terminal kinase is sensitive to caspase-dependent modulation while activation of mitogen-activated protein kinase (MAPK) or p38 MAPK is not

2002 ◽  
Vol 366 (1) ◽  
pp. 145-155 ◽  
Author(s):  
Ahmed A.A. MOHAMED ◽  
Orla J. JUPP ◽  
Helen M. ANDERSON ◽  
Alison F. LITTLEJOHN ◽  
Peter VANDENABEELE ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Tumour Necrosis Factor ◽  
P38 Mapk ◽  
Hela Cells ◽  
Tumour Necrosis ◽  
Mitogen Activated Protein Kinase ◽  
Downstream Target ◽  
Mitogen Activated Protein ◽  
Induced Apoptosis ◽  
Necrosis Factor

The activation of the extracellular signal-regulated kinases (ERKs) by tumour necrosis factor-α (TNF) receptors (TNFRs) is an integral part of the cytokine's pleiotropic cellular responses. Here we report differences in the caspase sensitivity and TNFR subtype activation of members of the ERK family. Inhibition in HeLa cells of caspase function by pharmacological inhibitors or the expression of CrmA (cytokine response modifier A), a viral modifier protein, blocks TNF-induced apoptosis or caspase-dependent protein kinase Cδ and poly(ADP-ribose) polymerase protein degradation. TNFR1- or TNFR2-stimulated c-Jun N-terminal kinase (JNK) activity was attenuated in cells in which caspase activity was inhibited either by pharmacological blockers or CrmA expression. Both TNFR1- and TNFR2-stimulated JNK activity was caspase-sensitive; however, only TNFR1 was capable of stimulating p42/44 mitogen-activated protein kinase (MAPK) and p38 MAPK activities. TNFR1-stimulated p42/44 MAPK and p38 MAPK activities were insensitive to pharmacological caspase inhibition or CrmA. These findings were supported when measuring TNF-induced cytosolic phospholipase A2 activation, which is a downstream target for MAPK and p38 MAPK. Profiling caspase enzymes activated by TNF in HeLa cells showed sequential caspase-8, −3, −7, −6 and −9 activation, with their inhibition characteristics suggesting a role for caspase-3 and/or caspase-6 in modulating JNK activity. Taken together these results show delineated ERK-activation pathways employed by TNFR subtypes.

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