Acetylcholine Nicotinic Channel Related Drug Discovery Products

The gene encoding for the component of the muscle receptor was found and cloned thanks to the outstanding developments in molecular biology. The five genes that code for the α1, β1, γ, δ and ε subunits were cloned and their corresponding chromosomal locations were discovered shortly after. Since then, 16 different neuronal nicotinic acetylcholine receptor (nAChR) subunit-encoding genes have been found in the genomes of mammals, including humans. Additionally, a number of lines of evidence imply that the ionotropic ion channels, which have a great deal in common structurally with human nAChRs, are found in bacteria and can serve as models for understanding the nAChR's tridimensional structure.

Creative Biolabs is proud to offer acetylcholine nicotinic channel drug discovery tools with the best quality and most competitive price:

• Acetylcholine Nicotinic Channel Assays
• Ion Channel Cell Lines
• Ion Channel Membranes
• Membrane Protein Tools

Overview of Acetylcholine Nicotinic Channel

• CHRNA1, CHRNB1, CHRNG, CHRND and CHRNE

The first genes to be discovered and defined were those for the muscle nAChRs. The muscle receptor has α1, β1, γ and δ subunits in its embryonic form, but in its mature form, the γ subunit has been replaced by the ε subunit. For both development and lifelong muscle synthesis, the change in gene expression from γ subunit to ε subunit is crucial. A kind of genetically transmissible Myasthenia gravis, which affects neurotransmission at the nerve endplate, is brought on by mutations in the muscle receptor genes. Serious mutations in CHRNA1, CHRNB1, CHRND, or CHRNG are typically fatal, whereas mutations in CHRNE are not discovered until the subunit expression changes.

• CHRNA2

The frontal cortex of higher mammalian brains was shown to express CHRNA2 more than the rat brain. The observation that a point mutation in this gene was linked to a type of nocturnal epilepsy further underscored the significance of this subunit for general brain function.

• CHRNA4 and CHRNB2

The assembly of α4 and β2 subunits produces the primary core heteromeric nAChR. The synthesis of functional nAChRs with a strong affinity for nicotine was made possible by heterologous production of nAChR subunits α4 and β2.

• CHRNA6

The gene CHRNA6 codes for the α6 subunit, which is mainly expressed in the mesolimbic system and ventral tegmental region. This subunit has drawn a lot of attention due to its exceptional expression in the central nervous system, however since it is difficult to express the α6 subunit in heterologous systems, it has been questioned as to whether it might be involved in or contribute to the ligand-binding site.

• CHRNA7

When the α7 subunit was first discovered in chickens, physiologists and geneticists were very interested in it because it produces functional homomeric receptors and has special characteristics in terms of its genomic structure, localization, and function, including high calcium permeability and rapid desensitization.

• CHRNA9 and CHRNA10

ACh response in some cells in the inner ear's organ of Corti has a distinctive pharmacological profile that falls between that of nicotinic and muscarinic receptors, according to physiological studies. A different subfamily of nAChRs may exist, as suggested by the cloning and sequencing of CHRNA9, a unique gene that encodes for the α9 subunit and the discovery that this gene is selectively expressed in the outer hair cells of the inner ear. The α10 subunit is encoded for by CHRNA10, which was found in both the rat and human genomes. It was discovered that it particularly co-assembles with nAChRs α9 and α10 to form functional nAChRs.

• CHRNA3, CHRNB4 and CHRNA5

The discovery that the genes encoding the α3, β4, and α5 subunits in rodents form a cluster led to novel theories regarding the control and independent expression of these subunits. The three genes CHRNB4, CHRNA3, and CHRNA5 are near together, and while CHRNB4 and CHRNA3 have identical transcription, CHRNA5 has the reverse direction of transcription.

• CHRNA5

Although there was initially merely indirect evidence, the existence of the α5 subunit was assumed to influence the physiological and pharmacological aspects of a receptor complex.

• CHRNB3

The N-terminal domain of the subunit that CHRNB3 encodes for lacks the two adjacent cysteines, indicating that the corresponding protein must be a member of the β subunit family. CHRNB3 has several distinctive characteristics, including a small number of introns and just 6 exons.