scholarly journals Lipopolysaccharide induces cytokine production and decreases extravillous trophoblast invasion through a mitogen-activated protein kinase-mediated pathway: possible mechanisms of first trimester placental dysfunction

2011 ◽  
Vol 27 (1) ◽  
pp. 61-72 ◽  
Author(s):  
L. Anton ◽  
A. G. Brown ◽  
S. Parry ◽  
M. A. Elovitz
Keyword(s):  
Protein Kinase ◽  
Cytokine Production ◽  
First Trimester ◽  
Mitogen Activated Protein Kinase ◽  
Extravillous Trophoblast ◽  
Trophoblast Invasion ◽  
Placental Dysfunction ◽  
Mitogen Activated Protein

scholarly journals The Balance between Sphingosine and Sphingosine-1-Phosphate Is Decisive for Mast Cell Activation after Fc∈ Receptor I Triggering

1999 ◽  
Vol 190 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Eva E. Prieschl ◽  
Robert Csonga ◽  
Veronica Novotny ◽  
Gary E. Kikuchi ◽  
Thomas Baumruker
Keyword(s):  
Mast Cells ◽  
Protein Kinase ◽  
Cytokine Production ◽  
Fc Receptor ◽  
Mitogen Activated Protein Kinase ◽  
Mast Cell Activation ◽  
Signaling Cascades ◽  
Mitogen Activated Protein ◽  
Sphingosine 1 Phosphate ◽  
Kinase Pathway

Over the last few years, sphingolipids have been identified as potent second messenger molecules modulating cell growth and activation. A newly emerging facet to this class of lipids suggests a picture where the balance between two counterregulatory lipids (as shown in the particular example of ceramide and sphingosine-1-phosphate in T lymphocyte apoptosis) determines the cell fate by setting the stage for various protein signaling cascades. Here, we provide a further example of such a decisive balance composed of the two lipids sphingosine and sphingosine-1-phosphate that determines the allergic responsiveness of mast cells. High intracellular concentrations of sphingosine act as a potent inhibitor of the immunoglobulin (Ig)E plus antigen–mediated leukotriene synthesis and cytokine production by preventing activation of the mitogen-activated protein kinase pathway. In contrast, high intracellular levels of sphingosine-1-phosphate, also secreted by allergically stimulated mast cells, activate the mitogen-activated protein kinase pathway, resulting in hexosaminidase and leukotriene release, or in combination with ionomycin, give cytokine production. Equivalent high concentrations of sphingosine-1-phosphate are dominant over sphingosine as they counteract its inhibitory potential. Therefore, it might be inferred that sphingosine-kinase is pivotal to the activation of signaling cascades initiated at the Fc∈ receptor I by modulating the balance of the counterregulatory lipids.

scholarly journals Mitogen activated protein kinase (MAPK) mediates non-genomic pathway of estrogen on T cell cytokine production following trauma-hemorrhage

Cytokine ◽  
2008 ◽  
Vol 42 (1) ◽  
pp. 32-38 ◽  
Author(s):  
Takao Suzuki ◽  
Huang-Ping Yu ◽  
Ya-Ching Hsieh ◽  
Mashkoor A. Choudhry ◽  
Kirby I. Bland ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Kinase ◽  
Cytokine Production ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Cell Cytokine Production

scholarly journals Mitogen-Activated Protein Kinase Phosphatase 2 Regulates the Inflammatory Response in Sepsis

2010 ◽  
Vol 78 (6) ◽  
pp. 2868-2876 ◽  
Author(s):  
Timothy T. Cornell ◽  
Paul Rodenhouse ◽  
Qing Cai ◽  
Lei Sun ◽  
Thomas P. Shanley
Keyword(s):  
Protein Kinase ◽  
Inflammatory Response ◽  
Map Kinase ◽  
Inflammatory Cytokines ◽  
Cytokine Production ◽  
Negative Regulator ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Anti Inflammatory ◽  
Dual Specific Phosphatase

ABSTRACT Sepsis results from a dysregulation of the regulatory mechanisms of the pro- and anti-inflammatory response to invading pathogens. The mitogen-activated protein (MAP) kinase cascades are key signal transduction pathways involved in the cellular production of cytokines. The dual-specific phosphatase 1 (DUSP 1), mitogen-activated protein kinase phosphatase-1 (MKP-1), has been shown to be an important negative regulator of the inflammatory response by regulating the p38 and Jun N-terminal protein kinase (JNK) MAP kinase pathways to influence pro- and anti-inflammatory cytokine production. MKP-2, also a dual-specific phosphatase (DUSP 4), is a phosphatase highly homologous with MKP-1 and is known to regulate MAP kinase signaling; however, its role in regulating the inflammatory response is not known. We hypothesized a regulatory role for MKP-2 in the setting of sepsis. Mice lacking the MKP-2 gene had a survival advantage over wild-type mice when challenged with intraperitoneal lipopolysaccharide (LPS) or a polymicrobial infection via cecal ligation and puncture. The MKP-2−/− mice also exhibited decreased serum levels of both pro-inflammatory cytokines (tumor necrosis factor alpha [TNF-α], interleukin-1β [IL-1β], IL-6) and anti-inflammatory cytokines (IL-10) following endotoxin challenge. Isolated bone marrow-derived macrophages (BMDMs) from MKP-2−/− mice showed increased phosphorylation of the extracellular signal-regulated kinase (ERK), decreased phosphorylation of JNK and p38, and increased induction of MKP-1 following LPS stimulation. The capacity for cytokine production increased in MKP-2−/− BMDMs following MKP-1 knockdown. These data support a mechanism by which MKP-2 targets ERK deactivation, thereby decreasing MKP-1 and thus removing the negative inhibition of MKP-1 on cytokine production.

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