title: Nuclear transfer of perchloric acid-soluble protein by endoplasmic reticulum stressors.
abstract: Perchloric acid-soluble protein (PSP) is highly conserved during evolution from bacteria to mammals. Although PSP has been recognized as an inhibitor of translation and proliferation in vitro, its precise biological role has not yet been elucidated. Since we previously found similar distributions for PSP and the endoplasmic reticulum (ER) and Golgi complex, the intracellular distribution of PSP was analyzed in more detail. Immunofluorescence studies indicated that PSP co-localized with the ER and Golgi complex, since the distribution pattern of PSP was well matched to both of these organelles. An immunoelectron microscopic study revealed PSP was located not only in the cytosol but also on the surface of the outer ER membrane. Since PSP was present on the ER, we speculated that it may be associated with ER function. Therefore, we analyzed whether or not the ER stress response, which is one of the ER functions, affected PSP expression. The results showed that various ER stressors (thapsigargin, A23187, tunicamycin, brefeldin A, and cisplatin) provoked a dramatic change in the localization of PSP from outside of the nucleus to inside the nucleus within 3 h. Moreover, the ER stressors induced PSP expression. These results suggest that PSP is involved in the cellular response to ER stressors, and that the change in localization of PSP from the ER to the nucleus may be associated with ER stress responses.
authors.affiliation: Department of Biochemistry, Kawasaki Medical School, 577 Matsushima, Kurashiki-city, Okayama, 701-0192, Japan. kanouchihiroaki@mac.com
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Kanouchi
authors.forename: Mitsuharu
authors.initials: M
authors.lastname: Matsumoto
authors.forename: Masaki
authors.initials: M
authors.lastname: Taga
authors.forename: Koji
authors.initials: K
authors.lastname: Yamada
authors.forename: Tatsuzo
authors.initials: T
authors.lastname: Oka
authors.forename: Shigenobu
authors.initials: S
authors.lastname: Toné
authors.forename: Yohsuke
authors.initials: Y
authors.lastname: Minatogawa
mesh_terms: D021581:Active Transport, Cell Nucleus; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology; D000001:Calcimycin / Q000494:pharmacology; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism; D002945:Cisplatin / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000187:drug effects* / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000187:drug effects / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D008297:Male; D051381:Rats; D017207:Rats, Sprague-Dawley; D012260:Ribonucleases / Q000187:drug effects / Q000378:metabolism*; D019284:Thapsigargin / Q000494:pharmacology; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D006360:Heat-Shock Proteins; C097211:Rida protein, rat; D014415:Tunicamycin; D020126:Brefeldin A; D000001:Calcimycin; D019284:Thapsigargin; D012260:Ribonucleases; D002945:Cisplatin