@article{oai:miyazaki-u.repo.nii.ac.jp:00000266.2,
 author = {伊藤, 勝昭 and Ito, Katsuaki and Toyoda, Isao and Higashiyama, Masato and Uemura, Daisuke and Sato, Masa H. and Yoshimura, Shige H. and Ishii, Toshiaki and Takeyasu, Kunio},
 issue = {1-3},
 journal = {FEBS letters : for the rapid publication of short reports in biochemistry, biophysics and molecular biology},
 month = {May},
 note = {Palytoxin （PTX） induces a cation channel through interaction
with Na+,K+-ATPase. It is unclear how this action relates to the enzyme
catalytic activity. We examined whether the action of PTX depends on
the catalytic domain specific for Na+,K+-ATPase. Wild-type
Na+,K+-ATPase α-subunit （NNN） or its chimera （NCN）, in which the
catalytic domain was replaced with that of SERCA, was co-expressed with
β-subunit in the yeast Saccharomyces cerevisiae. PTX （0.1-100 nM）
increased K+ efflux in NNN- or NCN-transfected cells to a similar degree
but not in non-transfected cells. When ouabain-resistant NNN and NCN
were expressed, PTX also increased K+ efflux. Ouabain inhibited the
effect of PTX in NNN- or NCN-cells but not in ouabain-resistant cells.
These data suggest that the channel-forming action of PTX does not depend
on the catalytic domain species., <a href="http://www.febsletters.com/" target="_blank">Journal HP</a>},
 pages = {108--112},
 title = {Channel induction by palytoxin in yeast cells expressing Na+,K+-ATPase or its chimera with sarco/endoplasmic reticulum Ca2+-ATPase},
 volume = {543},
 year = {2003},
 yomi = {イトウ, カツアキ}
}