title: Role of polyunsaturated fatty acids for misfolding protein aggregations: implication for neurodegenerative diseases.
abstract: Numerous neurodegenerative diseases are accompanied by highly insoluble inclusions of protein aggregates within characteristic neuronal populations. Recent in vitro studies have advanced new aspects of protein aggregates and their cytotoxicity. Aggregations of unfolded proteins escape the cellular quality-control system, such as chaperone and proteasome, which is a common feature of aggregates-associated neurodegeneration. Based on this idea, several factors may provide protein aggregates-favoring conditions that are closely involved in progression of diseases. In particular, we focused on polyunsaturated fatty acids as an important modulator for unfolded protein-aggregation in relation to disease pathogenesis.
authors.affiliation: Hirabayashi Research Unit, RIKEN Brain Science Institute, Wako-shi, Saitama 351-0198, Japan. yjkim@brain.riken.jp
authors.forename: Yeon-Jeong
authors.initials: YJ
authors.lastname: Kim
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Takahashi
mesh_terms: D000818:Animals; D002470:Cell Survival / Q000502:physiology; D005231:Fatty Acids, Unsaturated / Q000378:metabolism*; D006801:Humans; D045586:Intranuclear Inclusion Bodies / Q000378:metabolism / Q000473:pathology; D016631:Lewy Bodies / Q000378:metabolism / Q000473:pathology; D018832:Molecular Chaperones / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000473:pathology; D058225:Plaque, Amyloid / Q000378:metabolism / Q000473:pathology; D046988:Proteasome Endopeptidase Complex / Q000502:physiology; D011485:Protein Binding; D017510:Protein Folding
chemical_list: D005231:Fatty Acids, Unsaturated; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; D046988:Proteasome Endopeptidase Complex