• nAChRα1β1δε/γ

    Inhibition of the transient currents by the nAChR specific antagonist BTX measured on a SURFE²R-ONE.

    Schulz P. et al., 2009

AChRα1β1δε/γ | Muscle-type nicotinic acetylcholine receptor

Family:
Acetylcholine Receptors

Subgroups:
The family has been devided into nicotinic acetylcholine receptors (ionotropic channels) and muscarinic acetylcholine receptors (metabotropic G-protein coupled receptors). Both subgroups are sensitive to acetylcholine.

Topology:
Nicotinic acetylcholine receptors: As typical cys-loop receptors, acetylcholine receptor subunits contain four transmembrane spanning domains TM1-TM4. Five subunits form a pore, homomeric and heteromeric combinations are possible.17 vertebrate subunits have been identified: α genes: CHRNA1 - CHRNA10; β genes: CHRNB1 . CHRNB4, as well as CHRND (delta), CHRNE (epsilon), CHRNG (gamma)
Muscarinic acetylcholine receptors: 5 receptors have been described (M1 - M5), encoded by the 5 genes CHRM1 - CHRM5. These proteins contain seven transmembrane regions and do not form homo or heteromers. 

AChRα1β1δε/γ: Background Information


Overview:

The muscle-type nicotinic receptor is a multi-pass membrane protein complex and neurotransmitter-gated ion-channel, consisting of the subunit combination (α1)2β1δε (adult receptor) or (α1)2β1δγ (fetal receptor). It is located in the neuromuscular junction, where activation yields EPSP, mainly by increased Na+ and K+ conductance.


Data Sheet:

Gene:
CHRNA1, CHRNB1, CHRND, CHRNE or CHRNG

Human Protein:
UniProt P02708 (CHRNA1), P11230 (CHRNB1), Q07001 (CHRND), Q04844 (CHRNE), P07510 (CHRNG)

Tissue:
Isoform 1 of the alpha subunit CHRNA1 is only expressed in skeletal muscle. Isoform 2 is constitutively expressed in skeletal muscle, brain, heart, kidney, liver, lung and thymus

Function/ Application:
Signal transduction at the neuromuscular junction for skeletal muscle contraction

Pathology:
The alpha subunit CHRNA1 is the main focus for antibody binding in Myasthenia Gravis, Myasthenic Syndrome Congenital, 1B, Fast-Channel and Myasthenic Syndrome, Congenital, 1A, Slow-Channel

Interaction:
Alpha-conotoxin ImII, is clustered at the neuromuscular junction via the extracellular matrix protein agrin

Modulator:
Acetylcholine, carbachol, suxamethonium, α-Bungarotoxin, α-Conotoxin, Hexamethonium, Pancuronium, Tubocurarine

Assays:
SSM-based technology (SURFE²R)

Reviews and Links

Testimonials

Dr. Thomas Seeger & Karin V. Niessen - Statement about the SURFE²R Technology

Icon N1   “The SURFE²R makes extremely challenging electrophysiological targets accessible to robust routine analyses. For example, we have developed an assay for investigating nicotinic acetylcholine receptor ion channels, using membranes from the Pacific electric ray, Torpedo California. In this way, we overcome many of the well-known difficulties associated with this ion channel, which allows us to efficiently obtain information regarding compound pharmacology. Obtained pharmacology values match those of patch clamp recordings exceptionally well. We find that the SURFE²R is an excellent platform for characterization of electrogenic processes in isolated membranes.”

Karin V. Niessen, Dr. Thomas Seeger
Bundeswehr Institute of Pharmacology and Toxicology, Munich, Germany

Publications

2018 - In vitro pharmacological characterization of the bispyridinium non-oxime compound MB327 and its 2- and 3-regioisomers

Icon 96SE  SURFE²R 96SE publication in Toxicology Letters (2018)

Authors: 
Niessen K.V., Seeger T. Rappenglück S., Wein T., Höfner G., Wanner K.T., Thiermanna H., Worek F.

2016 - Functional analysis of Torpedo californica nicotinic acetylcholine receptors in multiple activation states by SSM-based electrophysiology

Icon 96SE   SURFE²R N96 (predecessor model of SURFE²R 96SE) publication in Toxicological Letters (2016)

Authors: 
Niessen K.V., Muschik S., Langguth F., Rappenglück S., Seeger T., Thiermann H., Worek F.

2009 - Measuring Ion Channels on Solid Supported Membranes

Icon N1   SURFE²R ONE (a predecessor model of SURFE²R N1) publication in Biophysical Journal (2009)

Authors:
Schulz P., Dueck B., Mourot A., Hatahet L., Fendler K.

 

 

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