title: Unfolded protein response and aggresome formation in hereditary reducing-body myopathy.
abstract: Reducing-body myopathy (RBM) is a rare myopathy characterized by the presence of unique sarcoplasmic inclusions called reducing bodies (RBs). We characterized the aggresomal features of RBs that contained gamma-tubulin, ubiquitin, and endoplasmic reticulum (ER) chaperones, together with a set of membrane proteins, in a family with hereditary RBM. Increased messenger ribonucleic acid and protein levels of a molecular chaperone, glucose-related protein 78, were also observed. These results suggest that the unfolded protein response caused by the accumulation of misfolded proteins in the endoplasmic reticulum plays an important role in the formation of RBs.
authors.affiliation: Department of Neuromuscular Research, National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawa-Higashi, Kodaira, Tokyo 187-8502, Japan.
authors.forename: Teerin
authors.initials: T
authors.lastname: Liewluck
authors.forename: Yukiko K
authors.initials: YK
authors.lastname: Hayashi
authors.forename: Maki
authors.initials: M
authors.lastname: Ohsawa
authors.forename: Rumi
authors.initials: R
authors.lastname: Kurokawa
authors.forename: Masako
authors.initials: M
authors.lastname: Fujita
authors.forename: Satoru
authors.initials: S
authors.lastname: Noguchi
authors.forename: Ikuya
authors.initials: I
authors.lastname: Nonaka
authors.forename: Ichizo
authors.initials: I
authors.lastname: Nishino
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics; D000328:Adult; D015415:Biomarkers / Q000032:analysis / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000235:genetics; D002648:Child; D004721:Endoplasmic Reticulum / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D000091342:Endoplasmic Reticulum Chaperone BiP; D005260:Female; D030342:Genetic Diseases, Inborn / Q000235:genetics / Q000378:metabolism / Q000473:pathology*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D002479:Inclusion Bodies / Q000235:genetics / Q000378:metabolism / Q000473:pathology*; D008297:Male; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism / Q000473:pathology* / Q000503:physiopathology*; D009135:Muscular Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology*; D017510:Protein Folding; D012333:RNA, Messenger / Q000378:metabolism; D035583:Rare Diseases; D014404:Tubulin / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism; D000074405:Valosin Containing Protein
chemical_list: D015415:Biomarkers; D018797:Cell Cycle Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D009124:Muscle Proteins; D012333:RNA, Messenger; D014404:Tubulin; D025801:Ubiquitin; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein