期刊
ANTIOXIDANTS & REDOX SIGNALING
卷 11, 期 10, 页码 2409-2427出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2009.2625
关键词
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资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
- CNPq-INCT de Processos Redox em Biomedicina-Redoxoma
- Financiadora de Estudos e Projetos
- Fundacao EJ Zerbini
Cellular mechanisms governing redox homeostasis likely involve their integration with other stresses. Endoplasmic reticulum (ER) stress triggers complex adaptive or proapoptotic signaling defined as the unfolded protein response (UPR), involved in several pathophysiological processes. Since protein folding is highly redoxdependent, convergence between ER stress and oxidative stress has attracted interest. Evidence suggests that ROS production and oxidative stress are not only coincidental to ER stress, but are integral UPR components, being triggered by distinct types of ER stressors and contributing to support proapoptotic, as well as proadaptive UPR signaling. Thus, ROS generation can be upstream or downstream UPR targets and may display a UPR-specific plus a nonspecific component. Enzymatic mechanisms of ROS generation during UPR include: (a) Multiple thioldisulfide exchanges involving ER oxidoreductases including flavooxidase Ero1 and protein disulfide isomerase (PDI); (b) Mitochondrial electron transport; (c) Nox4 NADPH oxidase complex, particularly Nox4. Understanding the roles of such mechanisms and how they interconnect with the UPR requires more investigation. Integration among such ROS sources may depend on Ca2+ levels, ROS themselves, and PDI, which associates with NADPH oxidase and regulates its function. Oxidative stress may frequently integrate with a background of ER stress/UPR in several diseases; here we discuss a focus in the vascular system. Antioxid. Redox Signal. 11, 2409-2427.
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