Autophagy in ischemic stroke. (April 2018)

• Record Type: Journal Article
• Authors: Wang, Pei; Shao, Bo-Zong; Deng, Zhiqiang; Chen, Shi; Yue, Zhenyu; Miao, Chao-Yu
• Is Part Of: Progress in neurobiology. Volume 163/164(2018)
• Page Start: 98
• Page End: 117
• Publication Date: 2018-04
• Subjects: 3-MA 3-methyladenine -- Aβ amyloid β -- AIF apoptosis-inducing factor -- Akt protein kinase B -- AMPK AMP-activated protein kinase -- ATF6 activating transcription factor 6 -- Atg autophagy-related genes -- ATP adenosine 5′-triphosphate -- BBB blood-brain barrier -- BCCAO bilateral carotid artery occlusion -- BFA bafilomycin A1 -- BH Bcl-2 homology -- BMVECs brain microvascular endothelial cells -- BNIP3L BNIP3-like -- CaMKK calcium-dependent protein kinase kinase -- CK2 casein kinase 2 -- CREB cAMP-response element binding protein -- DAPK death-associated protein kinase -- DALYs disability-adjusted life years -- DISC death-inducing signaling complex -- DRAM damage-regulated autophagy modulator -- eIF2α eukaryotic initiation factor 2α -- ER endoplasmic reticulum -- FADD Fas-associated death domain -- FasL Fas ligand -- FOXO3 forkhead box O 3 -- FIP200 focal adhesion kinase family interacting protein of 200 kD -- FUNDC1 FUN 14 domain-containing protein 1 -- FXR farnesoid X receptor -- GFP green fluorescent protein -- GRP78 glucose-regulated protein 78 -- HIF1 hypoxia-inducible factor 1 -- HSP70 heat shock protein 70 -- IKK IκB kinase -- IL-6 interleukin-6 -- IP3R inositol trisphosphate receptor -- IRE1α inositol-requiring enzyme 1α -- JNK1 c-Jun N-terminal protein kinase 1 -- LAMP2 lysosome-associated membrane protein 2 -- LC3-PE light chain 3-phosphatidylethanolamine -- MAPK mitogen activated protein kinases -- MCAO middle cerebral artery occlusion -- MLKL mixed lineage kinase domain-like protein -- MnSOD manganese superoxide dismutase -- mTOR mammalian target of rapamycin -- mTORC1 mTOR complex 1 -- NAD nicotinamide adenine dinucleotide -- Nampt nicotinamide phosphoribosyltransferase -- NEMO NF-κB essential modulator -- NF-κB nuclear factor-κB -- NLRP3 NLR family pyrin domain containing 3 -- NMDA N-methyl-d-aspartate -- NMN nicotinamide mononucleotide -- NOX NADPH oxidase -- NRF2 NF-E2-related factor 2 -- OGD oxygen-glucose deprivation -- PARP-1 poly(ADP-ribose) polymerase-1 -- PERK protein kinase (PKR)-like ER kinase -- PGAM5 phosphoglycerate mutase family member 5 -- PI3K phosphatidylinositol 3-kinase -- PI3KC3 class III phosphatidylinositol 3-kinase -- PINK1 PTEN-induced putative kinase 1 -- PKR RNA-activated protein kinase -- PPAR-γ peroxisome proliferator-activated receptor-γ -- RIP1 receptor-interacting serine/threonine-protein 1 -- ROS reactive oxygen species -- siRNA small interfering RNA -- SOD superoxide dismutase -- TFEB transcription factor EB -- TIGAR TP53-induced glycolysis and apoptosis regulator -- TNFR1 TNF-α receptor 1 -- TNF-α tumor necrosis factor-α -- TRADD TNF-α receptor-associated death domain -- TRAIL TNF-related apoptosis-inducing ligand -- TSC2 tuberous sclerosis complex 2 -- ULK Unc-51-like kinase -- UPR unfolded protein response -- WHO World Health Organization -- XBP1s X box-binding protein 1 spliced -- ZO-1 zonula occludens-1; Autophagy -- Ischemic stroke -- Apoptosis -- Necrosis -- Necroptosis -- Oxidative stress; Neurobiology -- Periodicals; Neurology -- Periodicals; Neurology -- Periodicals; Neurobiologie -- Périodiques; 612.8
• DOI: 10.1016/j.pneurobio.2018.01.001
• Languages: English
• ISSNs: 0301-0082

Abstract

Highlights: A comprehensive view of regulation of autophagy in neurons, glia cells and brain microvascular cells in response to ischemia stress is provided. Autophagy is involved in the pathological process during cerebral ischemic preconditioning, perconditioning and postconditioning. We propose a crosstalk between autophagy, necroptosis, and apoptosis that contribute to ischemic stroke. We discuss the interactions between autophagy and oxidative stress, mitochondrial dysfunction and endoplasmic reticulum stress. Abstract: Autophagy is a self-eating cellular catabolic pathway, through which long-lived proteins, damaged organelles and misfolded proteins are degraded and recycled for the maintenance of cellular homeostasis and normal cellular functions. Autophagy plays an important homeostatic role in the regulation of cell survival. Accumulating evidence shows that autophagy is activated in various cell types in the brain such as neurons, glia cells, and brain microvascular cells upon ischemic stroke. However, the exact role and molecular mechanisms of autophagy process that is implicated in ischemic stroke have yet to be elucidated. This review aims to provide a comprehensive view of the regulation of autophagy in neurons, glia cells, and brain microvascular cells in response to ischemia stress. We also review the recent advance on the understanding of the involvement of autophagy in the pathological process during cerebral ischemic preconditioning, perconditioning and postconditioning. We propose a crosstalk between autophagy, necroptosis, and apoptosis that contribute to ischemic stroke. In addition, we discuss the interactions between autophagy and oxidative stress, mitochondrial dysfunction and endoplasmic reticulum stress.