@article{oai:hirosaki.repo.nii.ac.jp:00003708,
 author = {Zhang, Hai-xin and Tanji, Kunikazu and Yoshida, Hidemi and Hayakari, Makoto and Mori, Fumiaki and Wakabayashi, Koichi},
 issue = {Supplement},
 journal = {弘前医学},
 month = {Jul},
 note = {TDP-43 proteinopathy （amyotrophic lateral sclerosis and frontotemporal lobar degeneration with ubiquitin-positive inclusions） is a newly categorized group of neurodegenerative disorders characterized by abnormal accumulation and mislocalization of nuclear TDP-43 protein in the neuronal cytoplasm. 15-deoxy-Δ12,14-prostaglandin J2 （15d-PGJ2） is non-enzymatically produced from PGD2, and plays roles in infl ammation and oxidative stress responses. Indeed, 15d-PGJ2 is up-regulated in the spinal motor neurons in ALS. In this study, biochemical and fluorescent staining analyses showed that 15d-PGJ2 modifi es expression, solubility, and subcellular localization of TDP-43. This alteration was at least partly related to a cyclopentenone ring structure containing an electrophilic carbon of 15d-PGJ2, because 15d-PGJ2 analogue, which lacks an cyclopentenone ring structure, had almost no eff ect on TDP-43 protein. Finally in vitro binding experiment indicated that 15d-PGJ2 is covalently bound to TDP-43 protein. These fi ndings suggest that a sustained high level of 15d-PGJ2 is involved in the pathogenesis of neurodegenerative disorders related to abnormal TDP-43 protein., 弘前医学. 61(Suppl.), 2010, p.S204-S210},
 pages = {S204--S210},
 title = {＜Poster＞15-Deoxy-Δ^12,14-prostaglandin J_2 modifi es profi les of nuclear TDP-43 protein through its direct binding : Implication for the pathogenesis of TDP-43 proteinopathy},
 volume = {61},
 year = {2010}
}