scholarly journals 205 INVOLVEMENT OF P38 MAP KINASE PHOSPHORYLATION IN CHONDROCYTE APOPTOSIS INDUCED BY MECHANICAL STRESS AND HEAT STRESS

2009 ◽  
Vol 17 ◽  
pp. S117
Author(s):  
K. Takebe ◽  
T. Nishiyama ◽  
S. Hashimoto ◽  
T. Fujishiro ◽  
N. Kanzaki ◽  
...  
Keyword(s):  
Heat Stress ◽  
Map Kinase ◽  
Mechanical Stress ◽  
P38 Map Kinase ◽  
Chondrocyte Apoptosis ◽  
Kinase Phosphorylation

scholarly journals 275 INVOLVEMENT OF P38 MAP KINASE PHOSPHORYLATION IN CHONDROCYTES APOPTOSIS INDUCED BY HEAT STRESS

2010 ◽  
Vol 18 ◽  
pp. S123-S124
Author(s):  
K. Takebe ◽  
T. Nishiyama ◽  
S. Hayashi ◽  
T. Fujishiro ◽  
N. Kanzaki ◽  
...  
Keyword(s):  
Heat Stress ◽  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Phosphorylation

Functional Role of p38 Mitogen Activated Protein Kinase in Platelet Activation induced by a Thromboxane A2 Analogue and by 8-iso-prostaglandin F2 α

2002 ◽  
Vol 87 (05) ◽  
pp. 888-898 ◽  
Author(s):  
Stefania Gaino ◽  
Valeria Zuliani ◽  
Rosa Tommasoli ◽  
Donatella Benati ◽  
Riccardo Ortolani ◽  
...  
Keyword(s):  
Map Kinase ◽  
Platelet Activation ◽  
Tyrosine Kinases ◽  
Actin Polymerization ◽  
Shape Change ◽  
Specific Inhibitor ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation

SummaryWe investigated similarities in the signaling pathways elicited by the F2 isoprostane 8-iso-PGF2α and by low doses of U46619 to induce platelet activation. Both 0.01-0.1 µmol/L U46619 and 0.01-1 µmol/L 8-isoPGF2α triggered shape change and filopodia extension, as well as adhesion to immobilized fibrinogen of washed platelets. At these doses the two platelet agonists failed to trigger secretion and aggregation, which were however induced by higher doses of U46619 (0.1-1 µmol/L). SB203580 (1-10 µmol/L), a specific inhibitor of the p38 mitogen activated protein (MAP) kinase blunted platelet shape change and adhesion induced by 0.05-1 µmol/L 8-iso-PGF2α and by 0.01 µmol/L U46619. These platelet responses were also inhibited by 20 µmol/L cytochalasin D, an inhibitor of actin polymerization, and 50 µmol/L piceatannol, an inhibitor of the Syk tyrosine kinases. Both 8-iso-PGF2α and U46619-induced p38 MAP kinase phosphorylation in suspended platelets and this was inhibited by piceatannol, indicating that Syk activation occurs upstream p38 MAP kinase phosphorylation. These findings suggest that the signaling pathway triggered by both 8-iso-PGF2α and low concentrations of U46619 to induce platelet adhesion and shape change implicates Syk, the p38 MAP kinase, and actin polymerization.

p38 MAP kinase mediates mechanically induced COX-2 and PG EP4 receptor expression in podocytes: implications for the actin cytoskeleton

2004 ◽  
Vol 286 (4) ◽  
pp. F693-F701 ◽  
Author(s):  
Louis C. Martineau ◽  
Lyne I. McVeigh ◽  
Bernard J. Jasmin ◽  
Chris R. J. Kennedy
Keyword(s):  
Actin Cytoskeleton ◽  
Map Kinase ◽  
Mechanical Stress ◽  
P38 Map Kinase ◽  
Receptor Expression ◽  
Prostaglandin E ◽  
Glomerular Permeability ◽  
Ep4 Receptor ◽  
Filtration Barrier ◽  
Cox 2

A dynamic cytoskeleton allows podocytes to withstand significant mechanical stress on elevation of intraglomerular capillary pressure (Pgc). However, vasoactive hormones, such as prostaglandin E2 (PGE2), may challenge the integrity of the actin cytoskeleton, alter podocyte morphology, and compromise glomerular permeability. PGE2 synthesis correlates with the onset of proteinuria and increased Pgc following reduced nephron mass. We investigated the interplay among mechanical stress, cyclooxygenase (COX), E-prostanoid (EP) receptor expression, and the actin cytoskeleton, using an in vitro model of cell stretch. Immortalized mouse podocytes grown on flexible silicone membranes were cyclically stretched (5% elongation, 0.5 Hz) for 2 h. EP4 and COX-2 mRNA increased three- and sevenfold above nonstretched controls, whereas EP1 and COX-1 levels were unchanged. Six hours of stretch resulted in a threefold increase in PGE2-stimulated cAMP accumulation, a measure of EP4 receptor function, and an increase in COX-2 protein. The stretch-induced effects on COX-2/EP4 expression and EP4-induced cAMP production were attributable to p38 MAP kinase, as blockade of this pathway, but not of ERK or JNK, abrogated the response. These stretch-induced changes in expression were transcriptionally dependent as they were actinomycin D sensitive. Finally, we investigated the influence of enhanced EP4 signaling on the actin cytoskeleton. Addition of PGE2 resulted in actin filament depolymerization observable only in stretched cells. Our results indicate that key components of the eicosanoid pathway are upregulated by mechanically stimulated p38 MAP kinase in podocytes. Enhanced EP4 receptor signaling may undermine podocyte cytoskeletal dynamics and thereby compromise filtration barrier function under conditions of increased Pgc.

scholarly journals Inhibition by adenylyl cyclase-cAMP system of ET-1-induced HSP27 in osteoblasts

2001 ◽  
Vol 281 (6) ◽  
pp. E1260-E1266 ◽  
Author(s):  
Daijiro Hatakeyama ◽  
Osamu Kozawa ◽  
Masayuki Niwa ◽  
Hiroyuki Matsuno ◽  
Kanefusa Kato ◽  
...  
Keyword(s):  
Map Kinase ◽  
Adenylyl Cyclase ◽  
Mrna Level ◽  
P38 Map Kinase ◽  
Hsp 27 ◽  
Kinase C ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Camp System ◽  
Kinase Phosphorylation

We have previously reported that endothelin-1 (ET-1) stimulates heat shock protein (HSP) 27 induction in osteoblast-like MC3T3-E1 cells and that p38 mitogen-activated protein (MAP) kinase acts at a point downstream from protein kinase C (PKC) in HSP27 induction. In the present study, we investigated the effect of the adenylyl cyclase-cAMP system on ET-1-stimulated induction of HSP27 in MC3T3-E1 cells. Dibutyryl-cAMP (DBcAMP) dose dependently inhibited the HSP27 accumulation stimulated by ET-1. Forskolin and cholera toxin significantly suppressed the ET-1-stimulated accumulation of HSP27. However, dideoxyforskolin, a forskolin derivative that does not activate cAMP, failed to suppress the ET-1-induced HSP27 accumulation. Forskolin reduced the p38 MAP kinase phosphorylation induced by ET-1 or 12- O-tetradecanoylphorbol-13-acetate (TPA). PGE1, an extracellular agonist that activates cAMP production, reduced the ET-1-induced HSP27 accumulation. In addition, the phosphorylation of p38 MAP kinase induced by ET-1 or TPA was suppressed by PGE1. Forskolin, DBcAMP, and PGE1suppressed the ET-1-stimulated increase in the mRNA level for HSP27. These results indicate that the adenylyl cyclase-cAMP system has an inhibitory role in ET-1-stimulated HSP27 induction in osteoblasts and that the effect is exerted at the point between PKC and p38 MAP kinase in osteoblasts.

Gö6976 Protects Mesencephalic Neurons from Lipopolysaccharide-Elicited Death by Inhibiting p38 MAP Kinase Phosphorylation

2002 ◽  
Vol 962 (1) ◽  
pp. 347-359 ◽  
Author(s):  
GWANG-HO JEOHN ◽  
CYNTHIA L. COOPER ◽  
KYUNG-JIN JANG ◽  
HYOUNG-CHUN KIM ◽  
JAU-SHYONG HONG
Keyword(s):  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Phosphorylation

Leishmania mexicana lipophosphoglycan activates ERK and p38 MAP kinase and induces production of proinflammatory cytokines in human macrophages through TLR2 and TLR4

Parasitology ◽  
2014 ◽  
Vol 141 (6) ◽  
pp. 788-800 ◽  
Author(s):  
A. ROJAS-BERNABÉ ◽  
O. GARCIA-HERNÁNDEZ ◽  
C. MALDONADO-BERNAL ◽  
J. DELEGADO-DOMINGUEZ ◽  
E. ORTEGA ◽  
...  
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
P38 Map Kinase ◽  
Leishmania Mexicana ◽  
Human Macrophages ◽  
Parasite Survival ◽  
Causative Agents ◽  
Favourable Environment ◽  
Kinase Phosphorylation ◽  
Pro Inflammatory Cytokines

SUMMARYProtozoan parasites of genus Leishmania are the causative agents of leishmaniasis. Leishmania promastigotes primarily infect macrophages in the host, where they transform into amastigotes and multiply. Lipophosphoglycan (LPG), the most abundant surface molecule of the parasite, is a virulence determinant that regulates the host immune response. Promastigotes are able to modulate this effect through LPG, creating a favourable environment for parasite survival, although the mechanisms underlying this modulation remain unknown. We analysed the participation of TLR2 and TLR4 in the production of cytokines and explored the possible phosphorylation of ERK and/or p38 MAP kinase signalling cascades in human macrophages stimulated with Leishmania mexicana LPG. The results show that LPG induced the production of TNF-α, IL-1β, IL-12p40, IL-12p70 and IL-10 and led to phosphorylation of ERK and p38 MAP kinase. Specific inhibitors of ERK or p38 MAP kinases and mAbs against TLR2 and TLR4 reduced cytokine production and phosphorylation of both kinases. Our results suggest that L. mexicana LPG binds TLR2 and TLR4 receptors in human macrophages, leading to ERK and MAP kinase phosphorylation and production of pro-inflammatory cytokines.

Regulation of p38 MAP kinase phosphorylation by estradiol in endometrial stromal cells in vitro

2004 ◽  
Vol 82 ◽  
pp. S317-S318
Author(s):  
Y. Seval ◽  
H. Cakmak ◽  
U.A. Kayisli ◽  
R. Demir ◽  
A. Arici
Keyword(s):  
Map Kinase ◽  
Stromal Cells ◽  
P38 Map Kinase ◽  
Endometrial Stromal Cells ◽  
Kinase Phosphorylation
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