Multiple activation of mitogen-activated protein kinases by purified independent CCN2 modules in vascular endothelial cells and chondrocytes in culture

Biochimie ◽  
2006 ◽  
Vol 88 (12) ◽  
pp. 1973-1981 ◽  
Author(s):  
S. Kubota ◽  
H. Kawaki ◽  
S. Kondo ◽  
G. Yosimichi ◽  
M. Minato ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinases ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

scholarly journals Confluence of Vascular Endothelial Cells Induces Cell Cycle Exit by Inhibiting p42/p44 Mitogen-Activated Protein Kinase Activity

1999 ◽  
Vol 19 (4) ◽  
pp. 2763-2772 ◽  
Author(s):  
Francesc Viñals ◽  
Jacques Pouysségur
Keyword(s):  
Cell Cycle ◽  
Endothelial Cells ◽  
Growth Factors ◽  
Vascular Endothelial Cells ◽  
Mitogen Activated Protein Kinase ◽  
Vascular Endothelial ◽  
Cell Cycle Exit ◽  
Mapk Activation ◽  
Mapk Activity ◽  
Mitogen Activated Protein

ABSTRACT Like other cellular models, endothelial cells in cultures stop growing when they reach confluence, even in the presence of growth factors. In this work, we have studied the effect of cellular contact on the activation of p42/p44 mitogen-activated protein kinase (MAPK) by growth factors in mouse vascular endothelial cells. p42/p44 MAPK activation by fetal calf serum or fibroblast growth factor was restrained in confluent cells in comparison with the activity found in sparse cells. Consequently, the induction of c-fos, MAPK phosphatases 1 and 2 (MKP1/2), and cyclin D1 was also restrained in confluent cells. In contrast, the activation of Ras and MEK-1, two upstream activators of the p42/p44 MAPK cascade, was not impaired when cells attained confluence. Sodium orthovanadate, but not okadaic acid, restored p42/p44 MAPK activity in confluent cells. Moreover, lysates from confluent 1G11 cells more effectively inactivated a dually phosphorylated active p42 MAPK than lysates from sparse cells. These results, together with the fact that vanadate-sensitive phosphatase activity was higher in confluent cells, suggest that phosphatases play a role in the down-regulation of p42/p44 MAPK activity. Enforced long-term activation of p42/p44 MAPK by expression of the chimera ΔRaf-1:ER, which activates the p42/p44 MAPK cascade at the level of Raf, enhanced the expression of MKP1/2 and cyclin D1 and, more importantly, restored the reentry of confluent cells into the cell cycle. Therefore, inhibition of p42/p44 MAPK activation by cell-cell contact is a critical step initiating cell cycle exit in vascular endothelial cells.

scholarly journals Role of mitogen-activated protein kinases in pulmonary endothelial cells exposed to cyclic strain

2000 ◽  
Vol 89 (6) ◽  
pp. 2391-2400 ◽  
Author(s):  
Hiroyuki Kito ◽  
Emery L. Chen ◽  
Xiujie Wang ◽  
Masataka Ikeda ◽  
Nobuyoshi Azuma ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinases ◽  
Cyclic Strain ◽  
Cell Alignment ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Pulmonary Arterial ◽  
And Migration ◽  
Sb 203580

The aim of this study was to examine the role of mitogen-activated protein kinases (MAPKs) activation in bovine pulmonary arterial endothelial cells (EC) exposed to cyclic strain. EC were subjected to 10% average strain at 60 cycles/min. Cyclic strain induced activation of extracellular signal-regulated kinase (ERK; 1.5-fold), c-Jun NH2-terminal protein kinase (JNK; 1.9-fold), and p38 (1.5-fold) with a peak at 30 min. To investigate the functional role of the activated MAPKs, we analyzed cells after treatment with PD-98059, a specific ERK kinase inhibitor, or SB-203580, a catalytic inhibitor for p38, and after transient transfection with JNK(K-R), and MEKK(K-M) the respective catalytically inactive mutants of JNK1 and MAPK kinase kinase-1. Cyclic strain increased activator protein-1 (AP-1) binding activity, which was blocked by PD-98059 and SB-203580. Activity of AP-1-dependent luciferase reporter driven by 12- O-tetradecanoyl-phorbol-13-acetate-responsive element (TRE) was induced by cyclic strain, and this was attenuated by PD-98059, MEKK(K-M), JNK(K-R), and SB-203580. PD-98059 and SB-203850 did not inhibit cell alignment and migration induced by cyclic strain. MEKK(K-M) and JNK(K-R) transfection did not block cyclic strain-induced cell alignment. In conclusion, cyclic strain activates ERK, JNK, and p38, and their activation plays a role in transcriptional activation of AP-1/TRE but not in cell alignment and migration changes in bovine pulmonary arterial EC.

scholarly journals E-Selectin-Dependent Signaling Via the Mitogen-Activated Protein Kinase Pathway in Vascular Endothelial Cells

2000 ◽  
Vol 165 (4) ◽  
pp. 2142-2148 ◽  
Author(s):  
Yenya Hu ◽  
Jeanne-Marie Kiely ◽  
Brian E. Szente ◽  
Anthony Rosenzweig ◽  
Michael A. Gimbrone
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Vascular Endothelial Cells ◽  
Mitogen Activated Protein Kinase ◽  
Vascular Endothelial ◽  
Mitogen Activated Protein ◽  
Kinase Pathway

scholarly journals Thrombomodulin Regulation of Mitogen-Activated Protein Kinases

2019 ◽  
Vol 20 (8) ◽  
pp. 1851 ◽  
Author(s):  
Hemant Giri ◽  
Xiaofeng Cai ◽  
Sumith R. Panicker ◽  
Indranil Biswas ◽  
Alireza R. Rezaie
Keyword(s):  
Protein Kinases ◽  
Intracellular Signaling ◽  
Vascular Endothelial Cells ◽  
Coagulation Factors ◽  
Regulatory Relationship ◽  
Signaling Mechanism ◽  
Mitogen Activated Protein Kinases ◽  
Inflammatory Conditions ◽  
Mitogen Activated Protein ◽  
Protective Signaling

The multifaceted role of mitogen-activated protein kinases (MAPKs) in modulating signal transduction pathways in inflammatory conditions such as infection, cardiovascular disease, and cancer has been well established. Recently, coagulation factors have also emerged as key players in regulating intracellular signaling pathways during inflammation. Among coagulation factors, thrombomodulin, as a high affinity receptor for thrombin on vascular endothelial cells, has been discovered to be a potent anti-inflammatory and anti-tumorigenic signaling molecule. The protective signaling function of thrombomodulin is separate from its well-recognized role in the clotting cascade, which is to function as an anti-coagulant receptor in order to switch the specificity of thrombin from a procoagulant to an anti-coagulant protease. The underlying protective signaling mechanism of thrombomodulin remains largely unknown, though a few published reports link the receptor to the regulation of MAPKs under different (patho)physiological conditions. The goal of this review is to summarize what is known about the regulatory relationship between thrombomodulin and MAPKs.

Sign in / Sign up

Export Citation Format

Share Document