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PMID: 10845103 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Structure and regulation of amiloride-sensitive sodium channels.

Annual review of physiology ·Vol. 62 ·2000-00-00 ·Pages 573-94

Alvarez de la Rosa D, Canessa CM, Fyfe GK, Zhang P

Abstract

Amiloride-sensitive Na+ channels constitute a new class of proteins known as the ENaC-Deg family of ion channels. All members in this family share a common protein structure but differ in their ion selectivity, their affinity for the blocker amiloride, and in their gating mechanisms. These channels are expressed in many tissues of invertebrate and vertebrate organisms where they serve diverse functions varying from Na+ absorption across epithelia to being the receptors for neurotransmitters in the nervous system. Here, we review progress made during the last years in the characterization, regulation, and cloning of new amiloride-sensitive Na+ channels.

MeSH Terms
Amiloride/pharmacology Animals Diuretics/pharmacology Epithelial Sodium Channels Humans Sodium Channels/chemistry,drug effects,metabolism
Chemicals
Diuretics Epithelial Sodium Channels Sodium Channels Amiloride
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Alvarez de la Rosa D
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520-8026, USA.
Canessa C M
Fyfe G K
Zhang P
Article Info
Journal
Annual review of physiology
Abbr.
Annu Rev Physiol
ISSN
0066-4278
Published
2000-00-00
Pages
573-94
Language
English
Region
United States
NLM ID
0370600
Subset
IM
Grants
NHLBI NIH HHS · HL 56163 · United States
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