Hsp70 molecular chaperones and Parkinson's disease.
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).
Witt
Stephan N
SN
Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130-3932, USA. switt1@lsuhsc.edu
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
D000682:Amyloid; D015415:Biomarkers; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D051844:alpha-Synuclein