title: Protein misfolding, aggregation, and autophagy after brain ischemia.
abstract: Ischemic brain injury is a common disorder linked to a variety of diseases. Significant progress has been made in our understanding of the underlying mechanisms. Previous studies show that protein misfolding, aggregation, and multiple organelle damage are major pathological events in postischemic neurons. The autophagy pathway is the chief route for bulk degradation of protein aggregates and damaged organelles. The latest studies suggest that impairment of autophagy contributes to abnormal protein aggregation and organelle damages after brain ischemia. This article reviews recent studies of protein misfolding, aggregation, and impairment of autophagy after brain ischemia.
authors: Shock, Trauma and Anesthesiology Research Center, Department of Anesthesiology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA.
authors: Tianfei
authors: T
authors: Luo
authors: Yujung
authors: Y
authors: Park
authors: Xin
authors: X
authors: Sun
authors: Chunli
authors: C
authors: Liu
authors: Bingren
authors: B
authors: Hu
mesh_terms: D000818:Animals; D001343:Autophagy / Q000502:physiology*; D001921:Brain / Q000378:metabolism* / Q000473:pathology; D002545:Brain Ischemia / Q000378:metabolism* / Q000473:pathology; D050956:HSP40 Heat-Shock Proteins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D051379:Mice; D009474:Neurons / Q000378:metabolism* / Q000473:pathology; D015388:Organelles / Q000378:metabolism*; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D051381:Rats
chemical_list: D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D011506:Proteins