Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
Pflugers Arch
2019 Feb 01;4712:329-336. doi: 10.1007/s00424-018-2223-z.
Show Gene links
Show Anatomy links
Comparative electrophysiological analysis of the bile acid-sensitive ion channel (BASIC) from different species suggests similar physiological functions.
Lenzig P
,
Wirtz M
,
Wiemuth D
.
???displayArticle.abstract???
Despite the identification of cholangiocytes in the liver and unipolar brush cells in the cerebellum as sites of expression, the physiological function of the bile acid-sensitive ion channel (BASIC) remains unknown. Rat BASIC (rBASIC) and mouse BASIC (mBASIC) share 97% of their amino acid sequence but show strikingly different biophysical properties. rBASIC is inactive at rest while mBASIC is constitutively active, when expressed in Xenopus oocytes. This conundrum rendered the identification of the physiological function even more difficult. In this study, we investigated the electrophysiological and pharmacological properties of BASIC from rat, mouse, and human in Hek293 cells using the patch clamp technique. Surprisingly, in Hek293 cells, rBASIC and mBASIC showed almost completely identical properties. Both are blocked by extracellular Ca2+ and thus are inactive at rest; both are selective for Na+, show similar affinities for extracellular Ca2+, were inhibited by diminazene, and activated by various bile acids. This is in contrast to previous results derived from Xenopus oocytes as expression system and suggests that the cell type is important for shaping the biophysical properties of BASIC. Furthermore, we compared hBASIC with rBASIC and mBASIC and observed similar properties between these channels with one exception: the bile acid sensitivity profile of hBASIC is different from rBASIC and mBASIC; hBASIC is more sensitive to bile acids which are abundant in human bile but not in rodent bile. Taken together, these results suggest similar physiological roles for BASIC in different species.
Assmann,
The comprehensive analysis of DEG/ENaC subunits in Hydra reveals a large variety of peptide-gated channels, potentially involved in neuromuscular transmission.
2014, Pubmed
Assmann,
The comprehensive analysis of DEG/ENaC subunits in Hydra reveals a large variety of peptide-gated channels, potentially involved in neuromuscular transmission.
2014,
Pubmed
Bianchi,
Mechanotransduction: touch and feel at the molecular level as modeled in Caenorhabditis elegans.
2007,
Pubmed
Boiko,
Restrictive expression of acid-sensing ion channel 5 (asic5) in unipolar brush cells of the vestibulocerebellum.
2014,
Pubmed
Canessa,
Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits.
1994,
Pubmed
Chen,
Diarylamidines: high potency inhibitors of acid-sensing ion channels.
2010,
Pubmed
Driscoll,
The mec-4 gene is a member of a family of Caenorhabditis elegans genes that can mutate to induce neuronal degeneration.
1991,
Pubmed
Dürrnagel,
Three homologous subunits form a high affinity peptide-gated ion channel in Hydra.
2010,
Pubmed
Fisher,
Sex differences in the bile acid composition of human bile: studies in patients with and without gallstones.
1973,
Pubmed
Ilyaskin,
Bile acids potentiate proton-activated currents in Xenopus laevis oocytes expressing human acid-sensing ion channel (ASIC1a).
2017,
Pubmed
Ilyaskin,
Activation of the Human Epithelial Sodium Channel (ENaC) by Bile Acids Involves the Degenerin Site.
2016,
Pubmed
Ilyaskin,
The degenerin region of the human bile acid-sensitive ion channel (BASIC) is involved in channel inhibition by calcium and activation by bile acids.
2018,
Pubmed
Jasti,
Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH.
2007,
Pubmed
Kellenberger,
International Union of Basic and Clinical Pharmacology. XCI. structure, function, and pharmacology of acid-sensing ion channels and the epithelial Na+ channel.
2015,
Pubmed
Kellenberger,
Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure.
2002,
Pubmed
Lefèvre,
Pharmacological and electrophysiological characterization of the human bile acid-sensitive ion channel (hBASIC).
2014,
Pubmed
Lingueglia,
Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel.
1995,
Pubmed
Sakai,
Cloning and functional expression of a novel degenerin-like Na+ channel gene in mammals.
1999,
Pubmed
Sakakura,
Simultaneous determination of bile acids in rat bile and serum by high-performance liquid chromatography.
1993,
Pubmed
Schaefer,
Molecular cloning, functional expression and chromosomal localization of an amiloride-sensitive Na(+) channel from human small intestine.
2000,
Pubmed
Schmidt,
The bile acid-sensitive ion channel (BASIC) is activated by alterations of its membrane environment.
2014,
Pubmed
Schmidt,
A Cytosolic Amphiphilic α-Helix Controls the Activity of the Bile Acid-sensitive Ion Channel (BASIC).
2016,
Pubmed
Schmidt,
Diminazene Is a Slow Pore Blocker of Acid-Sensing Ion Channel 1a (ASIC1a).
2017,
Pubmed
Setchell,
Bile acid concentrations in human and rat liver tissue and in hepatocyte nuclei.
1997,
Pubmed
Wemmie,
Acid-sensing ion channels in pain and disease.
2013,
Pubmed
Wiemuth,
A single amino acid tunes Ca2+ inhibition of brain liver intestine Na+ channel (BLINaC).
2010,
Pubmed
Wiemuth,
The bile acid-sensitive ion channel (BASIC), the ignored cousin of ASICs and ENaC.
2014,
Pubmed
Wiemuth,
Strong activation of bile acid-sensitive ion channel (BASIC) by ursodeoxycholic acid.
2013,
Pubmed
Wiemuth,
The pharmacological profile of brain liver intestine Na+ channel: inhibition by diarylamidines and activation by fenamates.
2011,
Pubmed
Wiemuth,
BASIC--a bile acid-sensitive ion channel highly expressed in bile ducts.
2012,
Pubmed
Yoder,
Gating mechanisms of acid-sensing ion channels.
2018,
Pubmed