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  • SyncroPatch 384

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  • SyncroPatch 384

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Reproducible activation and pharmacology of α1β1γδ nAChR on the SyncroPatch 384

icon sp96   SyncroPatch 384 application note:   logo pdf   (3.4 MB)
Cells were kindly provided by CLS


Nicotinic Acetylcholine Receptors (nAChR) are acetyl¬choline- (ACh) and nicotine-gated cation permeable ion channels, which mediate fast synaptic transmission at central synapses and neuromuscular junctions. Neuromuscular nAChR form heteromeric proteins com¬posed of four subunits: α, β, γ (or ε) and δ. Depending on the developmental stage, the AChR subunit stoichiome¬try changes from α1β1γδ (embryonic) to α1β1εδ (adult). Several inherited and acquired diseases are associated with nAChR dysfunction, most of which lead to impaired neuromuscular transmission and muscle weakness. The acquired autoimmune disease myasthenia gravis (MG) is caused by autoantibodies targeting muscle nAChRs that disrupts nerve-muscle communication resulting in muscle weakness and fatigue. Inherited diseases called congenital myasthenic syndromes (CMS) are associated with several abnormalities affecting ACh-release, ace¬tylcholinesterase activity, nAChR function and⁄or nAChR number. Treatment has been limited to nonselective, chronic immunosuppressive therapies which have long-term toxicities. More selective and targeted therapies are now under development.

Here we present data collected on the SyncroPatch 384 showing activation and block of nAChRα1β1γδ expressed in human TE671 cells with rapid application of ligand or ligand plus blockers. ACh activates nAChRα1β1γδ re¬ceptors with an EC50 value similar to those reported in literature8. We recorded highly reproducible currents in response to ACh (Fig. 2) and obtained IC50 values for mecamylamine (Fig. 3) and α-conotoxin GI (Fig. 4) that were in good agreement with the literature.

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