The role of p38 mitogen-activated protein kinase in IL-6 and IL-8 production from the TNF-α- or IL-1β-stimulated rheumatoid synovial fibroblasts

FEBS Letters ◽  
1999 ◽  
Vol 465 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Masaki Suzuki ◽  
Toshifumi Tetsuka ◽  
Shinichi Yoshida ◽  
Nobuyuki Watanabe ◽  
Masaaki Kobayashi ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Synovial Fibroblasts ◽  
Mitogen Activated Protein Kinase ◽  
Tnf Α ◽  
Mitogen Activated Protein

scholarly journals The Role of Mitogen-Activated Protein Kinase-Activated Protein Kinase 2 in the p38/TNF-α Pathway of Systemic and Cutaneous Inflammation

2010 ◽  
Vol 130 (2) ◽  
pp. 481-491 ◽  
Author(s):  
Arndt J. Schottelius ◽  
Ulrich Zügel ◽  
Wolf-Dietrich Döcke ◽  
Thomas M. Zollner ◽  
Lars Röse ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Cutaneous Inflammation ◽  
Tnf Α ◽  
Mitogen Activated Protein

Is MK2 (mitogen-activated protein kinase-activated protein kinase 2) the key for understanding post-transcriptional regulation of gene expression?

2002 ◽  
Vol 30 (6) ◽  
pp. 959-963 ◽  
Author(s):  
A. Kotlyarov ◽  
M. Gaestel
Keyword(s):  
Transcriptional Regulation ◽  
Cell Migration ◽  
Protein Kinase ◽  
Molecular Mechanisms ◽  
Cytokine Expression ◽  
Mitogen Activated Protein Kinase ◽  
Tnf Α ◽  
Mitogen Activated Protein ◽  
Post Transcriptional Regulation

The phenotype of mitogen-activated protein kinase-activated protein kinase-2 (MK2) knockout mice revealed the essential role of this enzyme in post-transcriptional regulation of lipopolysaccharide-induced expression of cytokines such as tumour necrosis factor (TNF)-α, interleukin-6 and interferon-γ, at the level of mRNA stability and translation. In the case of TNF-α, this regulation depends on the AU-rich element in TNF-α mRNA. In addition to cytokine expression, MK2 is also essential for cell migration in vitro. Although the role of MK2 in cytokine expression depends mainly on catalytic activity, its role in cell migration is also dependent on a proline-rich N-terminal motif. However, the molecular mechanisms involved and the relevant protein targets for MK2 are not completely defined. Here we discuss the possible mechanisms by which two potential target proteins of MK2, small heat-shock protein 25/27 (Hsp25/27) and tristetraprolin, could contribute to our understanding of the above regulation.

Role of p38 Mitogen-Activated Protein Kinase in Thrombus Formation

2004 ◽  
Vol 24 (4) ◽  
pp. 283-296 ◽  
Author(s):  
Kanako Sakurai ◽  
Yuji Matsuo ◽  
Tatsuhiko Sudo ◽  
Yoh Takuwa ◽  
Sadao Kimura ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Thrombus Formation ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Dual-mode regulation of the APC/C by CDK1 and MAPK controls meiosis I progression and fidelity

2014 ◽  
Vol 204 (6) ◽  
pp. 891-900 ◽  
Author(s):  
Ibtissem Nabti ◽  
Petros Marangos ◽  
Jenny Bormann ◽  
Nobuaki R. Kudo ◽  
John Carroll
Keyword(s):  
Protein Kinase ◽  
Spindle Assembly Checkpoint ◽  
Mitogen Activated Protein Kinase ◽  
Cyclin Dependent Kinase ◽  
Anaphase Promoting Complex ◽  
Female Meiosis ◽  
Dual Mode ◽  
Mitogen Activated Protein ◽  
Meiosis I

Female meiosis is driven by the activities of two major kinases, cyclin-dependent kinase 1 (Cdk1) and mitogen-activated protein kinase (MAPK). To date, the role of MAPK in control of meiosis is thought to be restricted to maintaining metaphase II arrest through stabilizing Cdk1 activity. In this paper, we find that MAPK and Cdk1 play compensatory roles to suppress the anaphase-promoting complex/cyclosome (APC/C) activity early in prometaphase, thereby allowing accumulation of APC/C substrates essential for meiosis I. Furthermore, inhibition of MAPK around the onset of APC/C activity at the transition from meiosis I to meiosis II led to accelerated completion of meiosis I and an increase in aneuploidy at metaphase II. These effects appear to be mediated via a Cdk1/MAPK-dependent stabilization of the spindle assembly checkpoint, which when inhibited leads to increased APC/C activity. These findings demonstrate new roles for MAPK in the regulation of meiosis in mammalian oocytes.

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