scholarly journals The food contaminant deoxynivalenol activates the mitogen activated protein kinases in the intestine: Interest of ex vivo models as an alternative to in vivo experiments

Toxicon ◽  
2013 ◽  
Vol 66 ◽  
pp. 31-36 ◽  
Author(s):  
Joelma Lucioli ◽  
Philippe Pinton ◽  
Patrick Callu ◽  
Joëlle Laffitte ◽  
François Grosjean ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Ex Vivo ◽  
Mitogen Activated Protein Kinases ◽  
In Vivo Experiments ◽  
Food Contaminant ◽  
Mitogen Activated Protein

scholarly journals Dusp-5 and Snrk-1 coordinately function during vascular development and disease

Blood ◽  
2009 ◽  
Vol 113 (5) ◽  
pp. 1184-1191 ◽  
Author(s):  
Kallal Pramanik ◽  
Chang Zoon Chun ◽  
Maija K. Garnaas ◽  
Ganesh V. Samant ◽  
Keguo Li ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Vascular Development ◽  
Serine Threonine Kinase ◽  
Lateral Plate ◽  
Mitogen Activated Protein Kinases ◽  
Cellular Processes ◽  
Mitogen Activated Protein ◽  
Integral Role ◽  
Dual Specific Phosphatase

Abstract Mitogen-activated protein kinases play an integral role in several cellular processes. To regulate mitogen-activated protein kinases, cells express members of a counteracting group of proteins called phosphatases. In this study, we have identified a specific role that one member of this family of phosphatases, dual-specific phosphatase-5 (Dusp-5) plays in vascular development in vivo. We have determined that dusp-5 is expressed in angioblasts and in established vasculature and that it counteracts the function of a serine threonine kinase, Snrk-1, which also plays a functional role in angioblast development. Together, Dusp-5 and Snrk-1 control angioblast populations in the lateral plate mesoderm with Dusp-5 functioning downstream of Snrk-1. Importantly, mutations in dusp-5 and snrk-1 have been identified in affected tissues of patients with vascular anomalies, implicating the Snrk-1–Dusp-5 signaling pathway in human disease.

Amygdala depotentiation ex vivo requires mitogen-activated protein kinases and protein synthesis

Neuroreport ◽  
2009 ◽  
Vol 20 (5) ◽  
pp. 517-520 ◽  
Author(s):  
Jeongyeon Kim ◽  
Sungmo Park ◽  
Sukwon Lee ◽  
Sukwoo Choi
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Ex Vivo ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

Stress deprivation from the patellar tendon induces apoptosis of fibroblasts in vivo with activation of mitogen-activated protein kinases

2009 ◽  
Vol 42 (15) ◽  
pp. 2611-2615 ◽  
Author(s):  
Hideyuki Kawabata ◽  
Taro Katsura ◽  
Eiji Kondo ◽  
Nobuto Kitamura ◽  
Shin Miyatake ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Patellar Tendon ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

On the mode of action of thrombin-induced angiogenesis: thrombin peptide, TP508, mediates effects in endothelial cells via αvβ3 integrin

2004 ◽  
Vol 92 (10) ◽  
pp. 846-857 ◽  
Author(s):  
Nikos Tsopanoglou ◽  
Matthew Papaconstantinou ◽  
Christodoulos Flordellis ◽  
Michael Maragoudakis
Keyword(s):  
Endothelial Cells ◽  
Protein Kinases ◽  
Cell Attachment ◽  
Growth Factor Receptor ◽  
Αvβ3 Integrin ◽  
Mitogen Activated Protein Kinases ◽  
Rgd Sequence ◽  
Mitogen Activated Protein

SummaryIn a previous report we have presented evidence that thrombin interacts with αvβ3 integrin in endothelial cells at the molecular and cellular level. This interaction was shown to be of functional significance in vitro and in vivo and contributed to activation of angiogenesis by thrombin. In the present study, we have used a synthetic thrombin peptide, TP508, which represents residues 183 to 200 of human thrombin. This peptide lacks the catalytic site of thrombin but contains the thrombin RGD sequence. Immobilized (surface-coated) TP508 peptide, like thrombin, supported αvβ3 integrin-dependent endothelial cell attachment and haptotactic migration. These effects were specific (a scrambled TP508 peptide was without effect), and dosedependent. The RGD sequence was essential since a modified TP508 peptide, which contained RAD sequence instead of RGD, was inactive. Immobilized TP508 peptide stimulated phosphorylation of mitogen-activated protein kinases and focal adhesion kinase, the signal transduction pathways characteristic for integrin activation. On the other hand, TP508 peptide, when in solution, did not mimic other thrombin-promoted angiogenic effects, such as that of activation gelatinase A, upregulation of expression of vascular endothelial growth factor receptor mRNA or prostacyclin PGI2 release in endothelial cells. On the contrary, soluble TP508 acted as an antagonist for the aforementioned effects of thrombin. TP508 peptide inhibited these thrombin-induced effects through a RGD and α. vβ3-related mechanism. The antagonism with thrombin or thrombin receptor activating peptide was specific and involved at least in part mitogen-activated protein kinases activation. These results point to the importance of RGD sequence of thrombin in mediating effects on endothelial cells and angiogenesis.

M-Phase Promoting Factor (MPF) and Mitogen Activated Protein Kinases (MAPK) Activities of Domestic Cat Oocytes Matured In Vitro and In Vivo

2004 ◽  
Vol 6 (1) ◽  
pp. 15-23 ◽  
Author(s):  
L. Bogliolo ◽  
G. Leoni ◽  
S. Ledda ◽  
M.T. Zedda ◽  
P. Bonelli ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Domestic Cat ◽  
Mitogen Activated Protein Kinases ◽  
M Phase ◽  
Mitogen Activated Protein

scholarly journals Mitogen-activated protein kinases are carbon dioxide receptors in plants

2020 ◽  
Author(s):  
Hanna Gałgańska ◽  
Łukasz Gałgański
Keyword(s):  
Protein Kinases ◽  
Stomatal Response ◽  
Mitogen Activated Protein Kinases ◽  
Environmental Signals ◽  
Know How ◽  
Mapk Signalling ◽  
Mitogen Activated Protein ◽  
Upstream Regulators

AbstractThe amount of CO2 in the atmosphere is increasing continuously in the industrial era, posing a threat to the ecological balance on Earth. There are two ways to reduce elevated CO2 concentrations ([CO2]high): reducing human emissions or increasing their absorption by oceans and plants. However, in response to [CO2]high, plants diminish gas exchange and CO2 uptake by closing stomata. Surprisingly, we do not know how plants sense CO2 in their environment, and the basic mechanisms of the plant response to [CO2]high are very poorly understood. Here, we show that mitogen-activated protein kinases (MAPKs) are plant CO2 receptors. We demonstrate that MPK4, a prominent MAPK that is known to be involved in the stomatal response to [CO2]high1–3, is capable of binding CO2 and is directly activated by a very low increase in [CO2] in vivo and in vitro. Unlike MPK4 activation by infections4, stress and hormones within known MAPK signalling cascades, [CO2]high-induced MPK4 activation is independent of the upstream regulators MKK1 and MKK2. Moreover, once activated, MPK4 is prone to inactivation by bicarbonate. The identification of stress-responsive MPK4 as a CO2 receptor sheds new light on the integration of various environmental signals in guard cells, setting up MPK4 as the main hub regulating CO2 availability for photosynthesis. This result could help to find new ways to increase CO2 uptake by plants.

Activation of Mitogen-activated Protein Kinases in in vivo Ischemia/Reperfused Myocardium in Rats

1999 ◽  
Vol 31 (6) ◽  
pp. 1269-1279 ◽  
Author(s):  
Takashi Omura ◽  
Minoru Yoshiyama ◽  
Takehiro Shimada ◽  
Naruhito Shimizu ◽  
Shokei Kim ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Reperfused Myocardium
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