title: Hsp70 molecular chaperones and Parkinson's disease.
abstract: Because over expression of Hsp70 molecular chaperones suppresses the toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and various polyQ-diseases (Huntington's disease and ataxias), Hsp70 is garnering attention as a possible therapeutic agent for these various diseases. Here, I review progress in this fascinating field of molecular chaperones and neurodegeneration and describe our current understanding of the mechanisms by which Hsp70 protects cells from the PD-related protein called alpha-synuclein (alpha-syn).
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130-3932, USA. switt1@lsuhsc.edu
authors.forename: Stephan N
authors.initials: SN
authors.lastname: Witt
mesh_terms: D000682:Amyloid / Q000378:metabolism; D000818:Animals; D001343:Autophagy / Q000502:physiology; D015415:Biomarkers / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D009410:Nerve Degeneration / Q000139:chemically induced / Q000378:metabolism / Q000473:pathology; D010300:Parkinson Disease / Q000188:drug therapy / Q000378:metabolism* / Q000473:pathology; D011387:Prokaryotic Cells / Q000378:metabolism; D011487:Protein Conformation; D051844:alpha-Synuclein / Q000378:metabolism / Q000633:toxicity
chemical_list: D000682:Amyloid; D015415:Biomarkers; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D051844:alpha-Synuclein