scholarly journals Apoptosis induced by pneumolysin in human endothelial cells involves mitogen-activated protein kinase phosphorylation

2012 ◽  
Author(s):  
Jun Yuan
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Human Endothelial Cells ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation

Lysophosphatidylcholine induces apoptosis in human endothelial cells through a p38-mitogen-activated protein kinase-dependent mechanism

2002 ◽  
Vol 161 (2) ◽  
pp. 387-394 ◽  
Author(s):  
Masafumi Takahashi ◽  
Hitoaki Okazaki ◽  
Yukiyo Ogata ◽  
Koichi Takeuchi ◽  
Uichi Ikeda ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Human Endothelial Cells ◽  
Mitogen Activated Protein ◽  
Dependent Mechanism

The proximal serum response element in the Egr-1 promoter mediates response to thrombin in primary human endothelial cells

Blood ◽  
2002 ◽  
Vol 100 (13) ◽  
pp. 4454-4461 ◽  
Author(s):  
Sheng-Qian Wu ◽  
Takashi Minami ◽  
Diana J. Donovan ◽  
William C. Aird
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Serum Response Factor ◽  
Core Promoter ◽  
Mitogen Activated Protein Kinase ◽  
Human Endothelial Cells ◽  
Mobility Shift ◽  
Nuclear Extracts ◽  
Mitogen Activated Protein ◽  
Serum Response

Thrombin signaling in endothelial cells provides an important link between coagulation and inflammation. We report here that thrombin induces endogenous Egr-1 mRNA and Egr-1 promoter activity in primary human endothelial cells by approximately 6-fold and 3-fold, respectively. In transient transfection assays, deletion of the 3′ cluster of serum response elements (SREs), but not the 5′ cluster of SREs, resulted in a loss of thrombin response. When coupled to a heterologous core promoter, a region spanning the 3′ SRE cluster contained information for thrombin response, whereas a region spanning the 5′ SRE cluster had no such effect. A point mutation of the most proximal SRE (SRE-1), but not of the proximal Ets motif or upstream SREs, abrogated the response to thrombin. In electrophoretic mobility shift assays, nuclear extracts from thrombin-treated cells displayed increased binding of total and phosphorylated serum response factor (SRF) to SRE-1. Thrombin-mediated induction of Egr-1 was blocked by inhibitors of MEK1/2, but not by inhibitors of protein kinase C, phosphatidylinositol 3-kinase, or p38 mitogen-activated protein kinase (MAPK). Taken together, these data suggest that thrombin induces Egr-1 expression in endothelial cells by a MAPK-dependent mechanism that involves an interaction between SRF and SRE-1.

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