Sensing endoplasmic reticulum stress by protein kinase RNA‐like endoplasmic reticulum kinase promotes adaptive mitochondrial DNA biogenesis and cell survival via heme oxygenase‐1/carbon monoxide activity

2012 ◽  
Vol 26 (6) ◽  
pp. 2558-2568 ◽  
Author(s):  
Min Zheng ◽  
Seul‐Ki Kim ◽  
Yeonsoo Joe ◽  
Sung Hoon Back ◽  
Hong R. Cho ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Endoplasmic Reticulum ◽  
Mitochondrial Dna ◽  
Protein Kinase ◽  
Endoplasmic Reticulum Stress ◽  
Cell Survival ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1

scholarly journals Endoplasmic Reticulum Stress Stimulates Heme Oxygenase-1 Gene Expression in Vascular Smooth Muscle

2004 ◽  
Vol 280 (2) ◽  
pp. 872-877 ◽  
Author(s):  
Xiao-ming Liu ◽  
Kelly J. Peyton ◽  
Diana Ensenat ◽  
Hong Wang ◽  
Andrew I. Schafer ◽  
...  
Keyword(s):  
Gene Expression ◽  
Endoplasmic Reticulum ◽  
Smooth Muscle ◽  
Endoplasmic Reticulum Stress ◽  
Vascular Smooth Muscle ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1

scholarly journals Heme, Heme Oxygenase, and Endoplasmic Reticulum Stress—A New Insight into the Pathophysiology of Vascular Diseases

2019 ◽  
Vol 20 (15) ◽  
pp. 3675 ◽  
Author(s):  
Gáll ◽  
Balla ◽  
Balla
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Er Stress ◽  
Heme Oxygenase ◽  
Molecular Mechanisms ◽  
Current Knowledge ◽  
Vascular Diseases ◽  
Heme Oxygenase 1 ◽  
Vascular Disorders ◽  
Ferroxidase Activity

The prevalence of vascular disorders continues to rise worldwide. Parallel with that, new pathophysiological pathways have been discovered, providing possible remedies for prevention and therapy in vascular diseases. Growing evidence suggests that endoplasmic reticulum (ER) stress is involved in a number of vasculopathies, including atherosclerosis, vascular brain events, and diabetes. Heme, which is released from hemoglobin or other heme proteins, triggers various pathophysiological consequence, including heme stress as well as ER stress. The potentially toxic free heme is converted by heme oxygenases (HOs) into carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is reduced to bilirubin (BR). Redox-active iron is oxidized and stored by ferritin, an iron sequestering protein which exhibits ferroxidase activity. In recent years, CO, BV, and BR have been shown to control cellular processes such as inflammation, apoptosis, and antioxidant defense. This review covers our current knowledge about how heme induced endoplasmic reticulum stress (HIERS) participates in the pathogenesis of vascular disorders and highlights recent discoveries in the molecular mechanisms of HO-mediated cytoprotection in heme stress and ER stress, as well as crosstalk between ER stress and HO-1. Furthermore, we focus on the translational potential of HIERS and heme oxygenase-1 (HO-1) in atherosclerosis, diabetes mellitus, and brain hemorrhage.

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