Nuclear transfer of perchloric acid-soluble protein by endoplasmic reticulum stressors.
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.
Kanouchi
Hiroaki
H
Department of Biochemistry, Kawasaki Medical School, 577 Matsushima, Kurashiki-city, Okayama, 701-0192, Japan. kanouchihiroaki@mac.com
Matsumoto
Mitsuharu
M
Taga
Masaki
M
Yamada
Koji
K
Oka
Tatsuzo
T
Toné
Shigenobu
S
Minatogawa
Yohsuke
Y
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
D006360:Heat-Shock Proteins; C097211:Rida protein, rat; D014415:Tunicamycin; D020126:Brefeldin A; D000001:Calcimycin; D019284:Thapsigargin; D012260:Ribonucleases; D002945:Cisplatin