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Altered phosphorylation of RRXS*/T* motif in ouabain-treated renal epithelial cells is not mediated by inversion of the [Na+](i)/[K+](i) ratioстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 31 октября 2014 г.
- Авторы: Akimova Olga A., Lopina Olga D., Tremblay Johanne, Hamet Pavel, Orlov Sergei N.
- Журнал: Cellular Physiology and Biochemistry
- Том: 21
- Номер: 4
- Год издания: 2008
- Издательство: S. Karger AG
- Местоположение издательства: Switzerland
- Первая страница: 315
- Последняя страница: 324
- DOI: 10.1159/000129390
- Аннотация: Recently, we reported that the death of ouabain-treated C7-MDCK cells resembling principal cells from collecting ducts of the Madin-Darby canine kidney (MDCK) is caused by ouabain interaction with Na+, K+-ATPase but is not mediated by inversion of the [Na+](i)/[K+](i) ratio. The mechanism of this intriguing phenomenon remains unknown. We therefore examined the action of ouabain on serine/threonine phosphoproteins as possible intermediates of cell death signaling. The death of ouabain-treated C7-MDCK cells proceeded by altered phosphorylation of the RRXS*/T*-motif in 4 proteins with Mr from 80 to 25 kDa. Similarly to cell death, inversion of the [ Na+] i/ [ K+](i) ratio evoked by Na+, K+-ATPase inhibition in K+-free medium did not affect the phosphorylation of RRXS*/T*-proteins but increased their sensitivity to ouabain. The action of ouabain was preserved in the presence of activators of protein kinases A ( forskolin), G ( sodium nitroprusside) and C (PMA) as well as inhibitors of protein kinase C (Go 6983, Go 6976) and serine-threonine phosphatases ( okadaic acid). Phosphorylation of RRXS*/T*-proteins was also noted in ouabain-sensitive C11-MDCK cells resembling intercalated cells from collecting ducts, but was absent in ouabain-resistant smooth muscle cells from the rat aorta. Our results show that altered phosphorylation of RRXS*/T*-proteins in ouabain-treated C7-MDCK cells is mediated by its interaction with Na+, K+-ATPase but is not caused by inversion of the [ Na+](i)/[K+](i) ratio. The molecular origin of serine-threonine kinases and/or phosphatases involved in phosphorylation of ouabain-sensitive proteins and their role in cell death signaling should be examined further.
- Добавил в систему: Лопина Ольга Дмитриевна