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The alpha-3 beta-4 nicotinic receptor, also known as the α3β4 receptor and the ganglion-type nicotinic receptor, [1] is a type of nicotinic acetylcholine receptor, consisting of α3 and β4 subunits.
Nicotinic receptor structure. Nicotinic receptors, with a molecular mass of 290 kDa, [10] are made up of five subunits, arranged symmetrically around a central pore. [3] Each subunit comprises four transmembrane domains with both the N- and C-terminus located extracellularly.
The adrenergic receptors or adrenoceptors are a class of G protein-coupled receptors that are targets of many catecholamines like norepinephrine (noradrenaline) and epinephrine (adrenaline) produced by the body, but also many medications like beta blockers, beta-2 (β 2) antagonists and alpha-2 (α 2) agonists, which are used to treat high ...
The alpha-3 beta-2 nicotinic receptor, also known as the α3β2 receptor, is a type of nicotinic acetylcholine receptor, consisting of α3 and β2 subunits. It occurs alongside the more common α3β4 nicotinic receptor in autonomic ganglia, and as an facilitatory presynaptic autoreceptor at the neuromuscular junction (NMJ). At the NMJ, it is ...
The alpha-4 beta-2 nicotinic receptor, also known as the α4β2 receptor, is a type of nicotinic acetylcholine receptor implicated in learning, [1] consisting of α4 and β2 subunits. [2] It is located in the brain, where activation yields post-and presynaptic excitation, [2] mainly by increased Na + and K + permeability.
Alpha-adrenergic agonists are a class of sympathomimetic agents that selectively stimulates alpha adrenergic receptors. The alpha-adrenergic receptor has two subclasses α 1 and α 2. Alpha 2 receptors are associated with sympatholytic properties. Alpha-adrenergic agonists have the opposite function of alpha blockers.
The protein encoded by this gene forms a homo-oligomeric channel, displays marked permeability to calcium ions and is a major component of brain nicotinic receptors that are blocked by, and highly sensitive to, alpha-bungarotoxin. Once this receptor binds acetylcholine, it undergoes an extensive change in conformation that affects all subunits ...
VLA-4's primary ligands include VCAM-1 and fibronectin. [4] One activating chemokine is SDF-1. Following SDF-1 binding, the integrin undergoes a conformational change of the alpha and beta domains that is necessary to confer high binding affinity for the endothelial adhesion molecules.