@article{oai:miyazaki-u.repo.nii.ac.jp:00000266,
 author = {伊藤, 勝昭 and Ito, Katsuaki and 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 and イトウ, カツアキ}
}