GALR1 Membrane Protein Introduction

Introduction of GALR1

The human GalR1 receptor was cloned from a human Bowes melanoma cell line in 1994 and contains 349 amino acid residues whose coding gene is located on the chromosome at 18q23. This gene contains at least two introns. Exon 1 encoding from the N-terminus to the end of the fifth transmembrane segment, exon 2 encodes the third intracellular loop, and exon 3 encodes the sixth transmembrane fragment to the C-terminus. Human GalR1 receptor and human GalR2 receptor, GalR3 receptors and somatostatin share certain homology with opioid receptors. The human and rat GalR1 receptors are approximately 92% homologous. The two N-linked glycosylation sites and intracellular phosphorylation sites are consistent. There are 7 sites for the action of phosphokinase A (PKA) and phosphokinase C (PKC) in the second and third intracellular loops, but the human GalR1 receptor is on its C-terminus. There are 2 phosphorylation sites on the domain.

Function of GALR1 Membrane Protein

In the inflammatory state, the GalR1 receptor may be regulated by the transcription factor NF-κB. A cells (a cell line similar to the blue spot) all can result in up-regulation of GalR1 mRNA. Forskolin's regulation of GalR1 mRNA appears to be mediated by the binding of the cAMP response element binding factor (CREB) to the CRE site of the GalR1 receptor promoter. The GalR1 receptor is coupled to the Gi/o protein, and the function of the cells is mainly inhibited. GalR1 receptors are activated to reduce the efficiency of synaptic transmission, thereby affecting many physiological processes such as ingestion, mood, memory, pain transmission, intestinal secretion, and exercise.

Fig.1 GalR1 receptor signaling directly or indirectly involves protein kinase C (PKC).

Application of GALR1 Membrane Protein in Literature

1. Li Y., et al. Galanin Protects from Caspase-8/12-initiated Neuronal Apoptosis in the Ischemic Mouse Brain via GalR1. Aging Dis. 2017, 8(1): 85-100. PubMed ID: 28203483
   
   

   This article reports that exogenous GAL protects the brain from ischemic injury by inhibiting Capasase-8/12-induced apoptosis and may be mediated by GalR1 through the cPKCγ signaling pathway.

2. Misawa K., et al. Site-specific methylation patterns of the GAL and GALR1/2 genes in head and neck cancer: Potential utility as biomarkers for prognosis. Mol Carcinog. 2017, 56(3): 1107-1116. PubMed ID: 27685843
   
   

   This article reveals that the methylation of GAL, GALR1 or GALR2 correlated most closely with the poor survival rate of patients with HPV-negative oropharyngeal cancer. Therefore, GAL and GALR 1/2 methylation status can serve as important site-specific biomarkers for predicting clinical outcome in HNSCC patients.

3. Fang P., et al. Central injection of GALR1 agonist M617 attenuates diabetic rat skeletal muscle insulin resistance through the Akt/AS160/GLUT4 pathway. Mech Ageing Dev. 2017, 162: 122-128. PubMed ID: 27041232
   
   

   The article reveals that galanin has an anti-diabetic effect. Studies have shown that administration of galanin can relieve insulin resistance by promoting the expression and translocation of glucose transporter 4 (GLUT4) in rat skeletal muscle.

4. Misawa K., et al. Epigenetic inactivation of galanin and GALR1/2 is associated with early recurrence in head and neck cancer. Clin Exp Metastasis. 2016, 33(2): 187-95. PubMed ID: 26572146
   
   

   This article shows that GAL and its receptors play a role in HNSCC tumorigenesis. Therefore, GAL and GALR1/2 methylation status can serve as important biomarkers for clinical outcome.

5. Kottaridi C., et al. A Pyrosequencing Assay for the Quantitative Methylation Analysis of GALR1 in Endometrial Samples: Preliminary Results. Biomed Res Int. 2015. PubMed ID: 26504828
   
   

   This article evaluates that pyrosequencing methylation analysis of the GALR1 promoter can be a useful cytological marker that may help better manage women with endometrial lesions and ultimately reduce unnecessary interventions.

GALR1 Preparation Options

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Reference

1. Neil Herring, et al. (2012). The cardiac sympathetic co-transmitter galanin reduces acetylcholine release and vagal bradycardia: Implications for neural control of cardiac excitability. Journal of Molecular and Cellular Cardiology. 56(3), 667-676.

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