Introduction of CHRNE
CHRNE, also known as acetylcholine receptor subunit epsilon (ACHRE), is one of the subunits of the acetylcholine receptor (AChR) and is encoded by the CHRNE gene in humans. The mammalian ChR is a pentameric transmembrane ion channel composed of 2α, 1β, 1δ and 1ε or 1γ subunit. Upon innervation, fetal form of AChR containing the γ subunit is replaced by adult form containing ε subunit. The muscle-type AChRs are located at the endplate of neuromuscular junctions (NMJ) where they mediate neuromuscular transmission, whereas the neuronal-type receptors are found throughout the peripheral and central nervous system. Neuronal-type subunits are expressed in multiple tissues, including vertebrate adult skeletal muscle, digestive system, lungs, keratinocytes, endothelial cells, and lymphocytes, while the muscle-type 1 receptor subunit is expressed in chick ciliary ganglia.
|Basic Information of CHRNE|
|Protein Name||Acetylcholine receptor subunit epsilon|
|Organism||Homo sapiens (Human)|
Function of CHRNE Membrane Protein
Replacement of the γ subunit in the embryonic AChR by ε subunit in the adult form is essential for maintenance of functional neuromuscular synapses in adult muscles, and leads to a greater channel conductance to Na+, K+ and Ca2+ than in fetal receptors. The expression of γ and ε subunits of the AChR from mammalian skeletal muscle is regulated independently during myogenic differentiation and innervation. Furthermore, the AChR ε subunit is expressed in thymocytes and thus may promote the production of AChR-reactive T cells in the early stages of maturation. The mutations in AChR ε subunit may lead to myasthenia gravis syndrome in individuals with the appropriate immunogenetic background. Mice lacking the ε-subunit die in early stages of life due to the lack of endplate AChR, suggesting ε subunit is essential for maintaining NMJ function.
Fig.1 Structure and subunit composition of adult AChR in muscle cells. (Hoffmann, 2006)
Application of CHRNE Membrane Protein Literature
This article suggests that for the first time, muscle synaptic function can be ascribed to a receptor isoform that is composed of only three different subunits and the unique functional features offered by the α(2)βδ(2) receptor likely play a central role in mediating the persistent contractions characteristic to this muscle type.
This article suggests that AChRs formed in combination with a Torpedo gamma subunit have a significantly lower conductance than those containing a mouse epsilon subunit.
This article reveals that the interaction between the HLA class II allele and the AChR subunit may have a profound effect on the clinical course of myasthenia gravis.
This article shows that extracellular domain (ECD) of the human AChR subunit (α, β, γ, δ, and ε) expressed in yeast produces a strong antigenic response in Lewis rats, and the pathogenicity is significantly different.
CHRNE Preparation Option
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