Premium
Role of Polyunsaturated Fatty Acids for Misfolding Protein Aggregations
Author(s) -
KIM YEONJEONG,
TAKAHASHI RYOSUKE
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1377.021
Subject(s) - polyunsaturated fatty acid , neurodegeneration , protein aggregation , protein folding , proteasome , chaperone (clinical) , protein quality , in vitro , inclusion bodies , biology , chemistry , pathogenesis , microbiology and biotechnology , biochemistry , disease , fatty acid , gene , medicine , immunology , pathology , escherichia coli
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.