scholarly journals ADP Stimulates Human Endothelial Cell Migration via P2Y1Nucleotide Receptor–Mediated Mitogen-Activated Protein Kinase Pathways

2008 ◽  
Vol 102 (4) ◽  
pp. 448-456 ◽  
Author(s):  
Jianzhong Shen ◽  
Paul E. DiCorleto
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Endothelial Cell Migration ◽  
Human Endothelial Cell ◽  
Mitogen Activated Protein

scholarly journals Multiple Roles of Protein Kinase A in Arachidonic Acid–Mediated Ca2+ Entry and Tumor-Derived Human Endothelial Cell Migration

2010 ◽  
Vol 8 (11) ◽  
pp. 1466-1476 ◽  
Author(s):  
Alessandra Fiorio Pla ◽  
Tullio Genova ◽  
Emanuela Pupo ◽  
Cristiana Tomatis ◽  
Armando Genazzani ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Multiple Roles ◽  
Endothelial Cell Migration ◽  
Human Endothelial Cell ◽  
Kinase A

scholarly journals Specific Activation of Mitogen-activated Protein Kinase by Transforming Growth Factor-β Receptors in Lipid Rafts Is Required for Epithelial Cell Plasticity

2009 ◽  
Vol 20 (3) ◽  
pp. 1020-1029 ◽  
Author(s):  
Wei Zuo ◽  
Ye-Guang Chen
Keyword(s):  
Cell Migration ◽  
Growth Factor ◽  
Protein Kinase ◽  
Lipid Rafts ◽  
Transforming Growth Factor ◽  
Mitogen Activated Protein Kinase ◽  
Type I ◽  
Coated Pits ◽  
Mapk Activation ◽  
Mitogen Activated Protein

Transforming growth factor (TGF)-β regulates a spectrum of cellular events, including cell proliferation, differentiation, and migration. In addition to the canonical Smad pathway, TGF-β can also activate mitogen-activated protein kinase (MAPK), phosphatidylinositol 3-kinase (PI3K)/Akt, and small GTPases in a cell-specific manner. Here, we report that cholesterol depletion interfered with TGF-β–induced epithelial-mesenchymal transition (EMT) and cell migration. This interference is due to impaired activation of MAPK mediated by cholesterol-rich lipid rafts. Cholesterol-depleting agents specifically inhibited TGF-β–induced activation of extracellular signal-regulated kinase (ERK) and p38, but not Smad2/3 or Akt. Activation of ERK or p38 is required for both TGF-β–induced EMT and cell migration, whereas PI3K/Akt is necessary only for TGF-β–promoted cell migration but not for EMT. Although receptor heterocomplexes could be formed in both lipid raft and nonraft membrane compartments in response to TGF-β, receptor localization in lipid rafts, but not in clathrin-coated pits, is important for TGF-β–induced MAPK activation. Requirement of lipid rafts for MAPK activation was further confirmed by specific targeting of the intracellular domain of TGF-β type I receptor to different membrane locations. Together, our findings establish a novel link between cholesterol and EMT and cell migration, that is, cholesterol-rich lipid rafts are required for TGF-β–mediated MAPK activation, an event necessary for TGF-β–directed epithelial plasticity.

scholarly journals NICOTINE ENHANCES ENDOTHELIAL CELL (EC) ADHESION MOLECULE EXPRESSION VIA P38 MITOGEN-ACTIVATED PROTEIN KINASE (MAPK)

Shock ◽  
2003 ◽  
Vol 19 (Supplement) ◽  
pp. 30
Author(s):  
H. Ueno ◽  
S. Pradhan ◽  
D. Schlessel ◽  
H. Hirasawa ◽  
B. E. Sumpio
Keyword(s):  
Endothelial Cell ◽  
Protein Kinase ◽  
Adhesion Molecule ◽  
Mitogen Activated Protein Kinase ◽  
Adhesion Molecule Expression ◽  
Mitogen Activated Protein
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