Mechanism of action of amiloride: A molecular prospective

Thomas R. Kleyman, Shaohu Sheng, Farhad Kosari, Thomas Kieber-Emmons

Research output: Contribution to journalReview article

23 Scopus citations

Abstract

Amiloride is a prototypic inhibitor of epithelial sodium channels. Rapid progress has been made in our understanding of the structure of the sodium channel and related cation-selective channels. This work, coupled with experiments examining how selected sodium channel mutations affect amiloride binding, provides critical clues towards defining sites within the channel that bind amiloride. Residues within the channel pore and within its extracellular domain participate in amiloride binding. These results suggest that sites that interact with amiloride within the channel's extracellular domain may be in close proximity to residues within the channel's pore.

Original languageEnglish (US)
Pages (from-to)524-532
Number of pages9
JournalSeminars in Nephrology
Volume19
Issue number6
StatePublished - Nov 17 1999

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ASJC Scopus subject areas

  • Nephrology

Cite this

Kleyman, T. R., Sheng, S., Kosari, F., & Kieber-Emmons, T. (1999). Mechanism of action of amiloride: A molecular prospective. Seminars in Nephrology, 19(6), 524-532.