scholarly journals Activation of Akt Rescues Endoplasmic Reticulum Stress-Impaired Murine Cardiac Contractile Function via Glycogen Synthase Kinase-3β-Mediated Suppression of Mitochondrial Permeation Pore Opening

2011 ◽  
Vol 15 (9) ◽  
pp. 2407-2424 ◽  
Author(s):  
Yingmei Zhang ◽  
Zhi Xia ◽  
Karissa H. La Cour ◽  
Jun Ren
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Glycogen Synthase ◽  
Contractile Function ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β ◽  
Cardiac Contractile Function ◽  
Cardiac Contractile ◽  
Pore Opening

scholarly journals Activated Protein C Induces Endoplasmic Reticulum Stress and Attenuates Lipopolysaccharide-Induced Apoptosis Mediated by Glycogen Synthase Kinase-3β

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Liang Luo ◽  
Tangfeng Lv ◽  
Qian Wang ◽  
Ting Zhang ◽  
Xiaoling Gu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Protein C ◽  
Glycogen Synthase ◽  
Umbilical Vein ◽  
Activated Protein C ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

This study investigated the relationship between antiapoptotic activities induced by activated protein C and endoplasmic reticulum stress. In this study, it was observed that activated protein C elicited a rise in glucose-regulated protein 78 and glycogen synthase kinase-3βand inhibited apoptosis in human umbilical vein endothelial cells induced by lipopolysaccharide. Calcium inhibition did not alter the antiapoptotic effect of activated protein C. The antiapoptotic efficiency of activated protein C was reduced in human umbilical vein endothelial cells following treatment with glycogen synthase kinase-3β-siRNA. In summary, activated protein C induced endoplasmic reticulum stress and attenuated lipopolysaccharide-induced human umbilical vein endothelial cell apoptosis mediated by glycogen synthase kinase-3β.

scholarly journals Endoplasmic Reticulum Stress Accelerates p53 Degradation by the Cooperative Actions of Hdm2 and Glycogen Synthase Kinase 3β

2005 ◽  
Vol 25 (21) ◽  
pp. 9392-9405 ◽  
Author(s):  
Olivier Pluquet ◽  
Li-Ke Qu ◽  
Dionissios Baltzis ◽  
Antonis E. Koromilas
Keyword(s):  
Endoplasmic Reticulum ◽  
Tumor Suppressor ◽  
Er Stress ◽  
Nuclear Export ◽  
Glycogen Synthase ◽  
Nucleocytoplasmic Transport ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β ◽  
Cooperative Action ◽  
In Cells

ABSTRACT Inactivation of the tumor suppressor p53 by degradation is a mechanism utilized by cells to adapt to endoplasmic reticulum (ER) stress. However, the mechanisms of p53 destabilization by ER stress are not known. We demonstrate here that the E3 ubiquitin-ligase Hdm2 is essential for the nucleocytoplasmic transport and proteasome-dependent degradation of p53 in ER-stressed cells. We also demonstrate that p53 phosphorylation at S315 and S376 is required for its nuclear export and degradation by Hdm2 without interfering with the ubiquitylation process. Furthermore, we show that p53 destabilization in unstressed cells utilizes the cooperative action of Hdm2 and glycogen synthase kinase 3β, a process that is enhanced in cells exposed to ER stress. In contrast to other stress pathways that stabilize p53, our findings further substantiate a negative role of ER stress in p53 activation with important implications for the function of the tumor suppressor in cells with a dysfunctional ER.

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