Introduction of GALR2
The GalR2 receptor was first cloned from a rat, it contains 372 amino acid residues and its coding gene has an intron. Exon 1 encodes from the N-terminus of the receptor to the end of the third transmembrane segment, and exon 2 encodes the second intracellular loop to the C-terminus. The extracellular domain of the rat GalR2 receptor has three nitrogen-linked glycosylation sites, while the intracellular domain has a different phosphorylation site than the GalR1 receptor. The C-terminus of the human GalR2 receptor is 15 amino acid residues more than the GalR2 receptor in the rat, and its GalR1 and GalR2 receptors are only about 42% homologous, suggesting that these two receptors have different regulatory functions.
|Basic Information of GALR2|
|Protein Name||Galanin receptor type 2|
|Aliases||GAL2-R, GALNR2, GALR-2, Galanin receptor 2|
|Organism||Homo sapiens (Human)|
Function of GALR2 Membrane Protein
GalR2 receptors may be coupled to Gq/11 proteins. They activate phospholipase C and promote synaptic transmission efficiency in GalR2 receptor expressing neurons. In addition, GalR2 receptors and forskolin are activated in CHO and HEK293 cells. The cAMP is conjugated and coupled to PKC-dependent MAPK activation in CHO cells, both of which are PTX-sensitive. These characteristics are coupled with Gi-coupled adenylyl cyclase inhibition and Go-coupled MAPK activation, indicating that the GalR2 receptor is also coupled to the Gi/o protein.
Fig.1 Neurons release GAL following injury or inflammation and activate tumour-expressed GALR2. (Scanlon, 2012)
Application of GALR2 Membrane Protein in Literature
This article reports that the galanin analog NAX 810-2 has a good preclinical character as a novel and first class analgesic.
This article reveals that NAX 810-2 effectively activates GalR2 at therapeutic concentrations.
The article reveals that the mechanism for the allosteric modulation caused by PAMs is the binding of the PAM at pocket III, which is formed by galanin, ECL2, TM2, TM3, and ECL1, which results in the disruption of the Na(+)-binding site and/or the Na(+) ion pathway, leading to GALR2 agonism.
This article shows that nonbrain-penetrating galanin analog reduces pain behaviors in several models and does not produce some of the dose-limiting toxicities associated with other analgesics.
This article evaluates that GALR2 stimulates tumor angiogenesis in SCCHN via p38-mediated inhibition of TTP with resultant enhanced cytokine secretion.
GALR2 Preparation Options
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