Channel induction by palytoxin in yeast cells expressing Na+,K+-ATPase or its chimera with sarco/endoplasmic reticulum Ca2+-ATPase
| Autor: | Toshiaki Ishii, Masato Higashiyama, Daisuke Uemura, Masa H. Sato, Katsuaki Ito, Isao Toyoda, Kunio Takeyasu, Shige H. Yoshimura |
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| Rok vydání: | 2003 |
| Předmět: |
Recombinant Fusion Proteins
Sarcoplasm Saccharomyces cerevisiae Biophysics Calcium-Transporting ATPases Biology Endoplasmic Reticulum Transfection Biochemistry Ouabain Sarcoplasmic Reticulum Calcium-Transporting ATPases chemistry.chemical_compound Cnidarian Venoms Structural Biology Palytoxin Catalytic Domain Genetics medicine Na+/K+-ATPase Enzyme Inhibitors Molecular Biology chemistry.chemical_classification Acrylamides Ion Transport Chimera Endoplasmic reticulum Cell Biology biology.organism_classification Channel Molecular biology Na+ K+-ATPase Yeast Enzyme chemistry Potassium Efflux Sodium-Potassium-Exchanging ATPase medicine.drug |
| Zdroj: | FEBS letters. 543(1-3) |
| ISSN: | 0014-5793 |
| Popis: | 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 alpha-subunit (NNN) or its chimera (NCN), in which the catalytic domain was replaced with that of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase, was co-expressed with beta-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. |
| Databáze: | OpenAIRE |
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