Activation of p38 MAPK Induced by a Multi-cycle Ischaemic Preconditioning Protocol is Associated with Attenuated p38 MAPK Activity During Sustained Ischaemia and Reperfusion

2001 ◽  
Vol 33 (4) ◽  
pp. 769-778 ◽  
Author(s):  
E. Marais ◽  
S. Genade ◽  
B. Huisamen ◽  
J.G. Strijdom ◽  
J.A. Moolman ◽  
...  
Keyword(s):  
P38 Mapk ◽  
Ischaemic Preconditioning ◽  
Mapk Activity ◽  
Ischaemia And Reperfusion

scholarly journals Interleukin-6 Inhibits Fas-Induced Apoptosis and Stress-Activated Protein Kinase Activation in Multiple Myeloma Cells

Blood ◽  
1997 ◽  
Vol 89 (1) ◽  
pp. 227-234 ◽  
Author(s):  
Dharminder Chauhan ◽  
Surender Kharbanda ◽  
Atsushi Ogata ◽  
Mitsuyoshi Urashima ◽  
Gerrard Teoh ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Protein Kinase ◽  
Dna Fragmentation ◽  
P38 Mapk ◽  
Interleukin 6 ◽  
Early Response ◽  
Mitogen Activated Protein Kinase ◽  
Serum Starvation ◽  
Mapk Activity ◽  
Induced Apoptosis

Abstract Fas belongs to the family of type-1 membrane proteins that transduce apoptotic signals. In the present studies, we characterized signaling during Fas-induced apoptosis in RPMI-8226 and IM-9 multiple myeloma (MM) derived cell lines as well as patient plasma cell leukemia cells. Treatment with anti-Fas (7C11) monoclonal antibody (MoAb) induced apoptosis, evidenced by internucleosomal DNA fragmentation and propidium iodide staining, and was associated with increased expression of c-jun early response gene. We also show that anti-Fas MoAb treatment is associated with activation of stress-activated protein kinase (SAPK) and p38 mitogen-activated protein kinase (MAPK); however, no detectable increase in extracellular signal-regulated kinases (ERK1 and ERK2) activity was observed. Because interleukin-6 (IL-6) is a growth factor for MM cells and inhibits apoptosis induced by dexamethasone and serum starvation, we examined whether IL-6 affects anti-Fas MoAb-induced apoptosis and activation of SAPK or p38 MAPK in MM cells. Culture of MM cells with IL-6 before treatment with anti-Fas MoAb significantly reduced both DNA fragmentation and activation of SAPK, without altering induction of p38 MAPK activity. These results therefore suggest that anti-Fas MoAb-induced apoptosis in MM cells is associated with activation of SAPK, and that IL-6 may both inhibit apoptosis and modulate SAPK activity.

scholarly journals Interleukin-13 affects the epithelial sodium channel in the intestine by coordinated modulation of STAT6 and p38 MAPK activity

2015 ◽  
Vol 593 (24) ◽  
pp. 5269-5282 ◽  
Author(s):  
Petra Dames ◽  
Theresa Bergann ◽  
Anja Fromm ◽  
Roland Bücker ◽  
Christian Barmeyer ◽  
...  
Keyword(s):  
Sodium Channel ◽  
P38 Mapk ◽  
Epithelial Sodium Channel ◽  
Interleukin 13 ◽  
Mapk Activity

scholarly journals Arsenite stimulated glucose transport in 3T3-L1 adipocytes involves both Glut4 translocation and p38 MAPK activity

2003 ◽  
Vol 270 (19) ◽  
pp. 3891-3903 ◽  
Author(s):  
Merlijn Bazuine ◽  
D. Margriet Ouwens ◽  
Daan S. Gomes de Mesquita ◽  
J. Antonie Maassen
Keyword(s):  
Glucose Transport ◽  
P38 Mapk ◽  
Glut4 Translocation ◽  
Mapk Activity

scholarly journals p38-MAPK mediated rRNA processing and translation regulation enables PrE differentiation during mouse blastocyst maturation

2020 ◽  
Author(s):  
Pablo Bora ◽  
Lenka Gahurova ◽  
Tomáš Mašek ◽  
Andrea Hauserova ◽  
David Potěšil ◽  
...  
Keyword(s):  
Cell Fate ◽  
P38 Mapk ◽  
Ribosomal Proteins ◽  
De Novo ◽  
Inner Cell Mass ◽  
Cell Mass ◽  
Translation Regulation ◽  
Placental Development ◽  
Mapk Activity ◽  
Live Embryo

AbstractBackgroundp38-MAPKs are stress-activated kinases necessary for placental development and nutrient and oxygen transfer during murine post-implantation development. In preimplantation development, p38-MAPK activity is required for blastocyst formation. Additionally, we have previously reported its role in regulating specification of inner cell mass (ICM) towards primitive endoderm (PrE), although a comprehensive mechanistic understanding is currently limited. Adopting live embryo imaging, proteomic and transcriptomic approaches, we report experimental data that directly address this deficit.ResultsChemical inhibition of p38-MAPK activity during blastocyst maturation causes impaired blastocyst cavity expansion, most evident between the third and tenth hours post inhibition onset. We identify an overlapping minimal early blastocyst maturation window of p38-MAPKi inhibition (p38-MAPKi) sensitivity, that is sufficient to impair PrE cell fate by the late blastocyst (E4.5) stage. Comparative proteomic analyses reveal substantial downregulation of ribosomal proteins, the mRNA transcripts of which are also significantly upregulated. Ontological analysis of the differentially expressed transcriptome during this developmental period reveals “translation” related gene transcripts as being most significantly, yet transiently, affected by p38-MAPKi. Moreover, combined assays consistently report concomitant reductions in de novo translation that are associated with accumulation of unprocessed rRNA precursors. Using a phosphoproteomic approach, ± p38-MAPKi, we identified Mybpp1a, an rRNA transcription and processing regulator gene, as a potential p38-MAPK effector. We report that siRNA mediated clonal knockdown of Mybpp1a is associated with significantly diminished PrE contribution. Lastly, we show that defective PrE specification caused by p38-MAPKi (but not MEK/ERK signalling inhibition) can be partially rescued by activating the archetypal mTOR mediated translation regulatory pathway.ConclusionsActivated p38-MAPK controls blastocyst maturation in an early and distinctly transient developmental window by regulating gene functionalities related to translation, that creates a permissive environment for appropriate specification of ICM cell fate.

scholarly journals Fas-Induced Apoptosis of Human Neutrophils is Promoted by Phosphatidyl Inositol 3-Kinase but Suppressed by P38-MAPK Activity

2001 ◽  
Vol 1 ◽  
pp. 116-116
Author(s):  
Maria Alvarado-Kristensson ◽  
M. Isabella Poumlrn-Ares ◽  
Simone Grethe ◽  
David Smith ◽  
Limin Zheng ◽  
...  
Keyword(s):  
P38 Mapk ◽  
Phosphatidyl Inositol ◽  
Human Neutrophils ◽  
Mapk Activity ◽  
Induced Apoptosis

scholarly journals Oxalate upregulates expression of IL-2Rβ and activates IL-2R signaling in HK-2 cells, a line of human renal epithelial cells

2014 ◽  
Vol 306 (9) ◽  
pp. F1039-F1046 ◽  
Author(s):  
Sweaty Koul ◽  
Lakshmipathi Khandrika ◽  
Thomas J. Pshak ◽  
Naoko Iguchi ◽  
Mintu Pal ◽  
...  
Keyword(s):  
Gene Expression ◽  
Signaling Pathway ◽  
P38 Mapk ◽  
Mapk Pathway ◽  
Interleukin 2 ◽  
Stone Disease ◽  
Downstream Signaling ◽  
Protein Levels ◽  
Mapk Activity ◽  
P38 Mapk Inhibitor

The role of inflammation in oxalate-induced nephrolithiasis is debated. Our gene expression study indicated an increase in interleukin-2 receptor β (IL-2Rβ) mRNA in response to oxalate (Koul S, Khandrika L, Meacham RB, Koul HK. PLoS ONE 7: e43886, 2012). Herein, we evaluated IL-2Rβ expression and its downstream signaling pathway in HK-2 cells in an effort to understand the mechanisms of oxalate nephrotoxicity. HK-2 cells were exposed to oxalate for various time points in the presence or absence of SB203580, a specific p38 MAPK inhibitor. Gene expression data were analyzed by Ingenuity Pathway Analysis software. mRNA expression was quantitated via real-time PCR, and changes in protein expression/kinase activation were analyzed by Western blotting. Exposure of HK-2 cells to oxalate resulted in increased transcription of IL-2Rβ mRNA and increased protein levels. Oxalate treatment also activated the IL-2Rβ signaling pathway (JAK1/STAT5 phosphorylation). Moreover, the increase in IL-2Rβ protein was dependent upon p38 MAPK activity. These results suggest that oxalate-induced activation of the IL-2Rβ pathway may lead to a plethora of cellular changes, the most common of which is the induction of inflammation. These results suggest a central role for the p38 MAPK pathway in mediating the effects of oxalate in renal cells, and additional studies may provide the key to unlocking novel biochemical targets in stone disease.

scholarly journals Inhibition of p38 MAPK reverses hypoxia-induced pulmonary artery endothelial dysfunction

2009 ◽  
Vol 296 (5) ◽  
pp. H1312-H1320 ◽  
Author(s):  
Roshan P. Weerackody ◽  
David J. Welsh ◽  
Roger M. Wadsworth ◽  
Andrew J. Peacock
Keyword(s):  
Pulmonary Hypertension ◽  
Endothelial Dysfunction ◽  
Pulmonary Artery ◽  
P38 Mapk ◽  
Hypoxic Exposure ◽  
Sprague Dawley ◽  
Hypoxia Exposure ◽  
Mapk Activity ◽  
Novel Target ◽  
Endothelium Dependent Relaxation

Hypoxia-induced endothelial dysfunction plays a crucial role in the pathogenesis of hypoxic pulmonary hypertension. p38 MAPK expression is increased in the pulmonary artery following hypoxic exposure. Recent evidence suggests that increased p38 MAPK activity is associated with endothelial dysfunction. However, the role of p38 MAPK activation in pulmonary artery endothelial dysfunction is not known. Sprague-Dawley rats were exposed to 2 wk hypobaric hypoxia, which resulted in the development of pulmonary hypertension and vascular remodeling. Endothelium-dependent relaxation of intrapulmonary vessels from hypoxic animals was impaired due to a reduced nitric oxide (NO) generation. This was despite increased endothelial NO synthase immunostaining and protein expression. Hypoxia exposure increased superoxide generation and p38 MAPK expression. The inhibition of p38 MAPK restored endothelium-dependent relaxation, increased bioavailable NO, and reduced superoxide production. In conclusion, the pharmacological inhibition of p38 MAPK was effective in increasing NO generation, reducing superoxide burden, and restoring hypoxia-induced endothelial dysfunction in rats with hypoxia-induced pulmonary hypertension. p38 MAPK may be a novel target for the treatment of pulmonary hypertension.

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