Metallothionein prevention of arsenic trioxide-induced cardiac cell death is associated with its inhibition of mitogen-activated protein kinases activation in vitro and in vivo

2013 ◽  
Vol 220 (3) ◽  
pp. 277-285 ◽  
Author(s):  
Xiao Miao ◽  
Zefang Tang ◽  
Yonggang Wang ◽  
Guanfang Su ◽  
Weixia Sun ◽  
...  
Keyword(s):  
Cell Death ◽  
Arsenic Trioxide ◽  
Protein Kinases ◽  
Cardiac Cell ◽  
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.

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.

scholarly journals Neuroprotective Effects of Tetrahydrocurcumin against Glutamate-Induced Oxidative Stress in Hippocampal HT22 Cells

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 144 ◽  
Author(s):  
Chang-Hyun Park ◽  
Ji Hoon Song ◽  
Su-Nam Kim ◽  
Ji Hwan Lee ◽  
Hae-Jeung Lee ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Death ◽  
Protein Kinases ◽  
Apoptotic Cell ◽  
Curcuma Longa ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Ht22 Cells ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

In the central nervous system, glutamate is a major excitable neurotransmitter responsible for many cellular functions. However, excessive levels of glutamate induce neuronal cell death via oxidative stress during acute brain injuries as well as chronic neurodegenerative diseases. The present study was conducted to examine the effect of tetrahydrocurcumin (THC), a major secondary metabolite of curcumin, and its possible mechanism against glutamate-induced cell death. We prepared THC using curcumin isolated from Curcuma longa (turmeric) and demonstrated the protective effect of THC against glutamate-induced oxidative stress in HT22 cells. THC abrogated glutamate-induced HT22 cell death and showed a strong antioxidant effect. THC also significantly reduced intracellular calcium ion increased by glutamate. Additionally, THC significantly reduced the accumulation of intracellular oxidative stress induced by glutamate. Furthermore, THC significantly diminished apoptotic cell death indicated by annexin V-positive in HT22 cells. Western blot analysis indicated that the phosphorylation of mitogen-activated protein kinases including c-Jun N-terminal kinase, extracellular signal-related kinases 1/2, and p38 by glutamate was significantly diminished by treatment with THC. In conclusion, THC is a potent neuroprotectant against glutamate-induced neuronal cell death by inhibiting the accumulation of oxidative stress and phosphorylation of mitogen-activated protein kinases.

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