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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

G protein-coupled receptor 116

GPR116, Ig-Hepta
a G protein-coupled receptor; may have a role in the regulation of acid-base balance [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: GPCR, GPR110, GPR115, EMR2, EMR3
Papers on GPR116
Targeted Disruption of Ig-Hepta/Gpr116 Causes Emphysema-like Symptoms That Are Associated with Alveolar Macrophage Activation.
Nakamura et al., Yokohama, Japan. In J Biol Chem, May 2015
Ig-Hepta/GPR116 is a member of the G protein-coupled receptor family predominantly expressed in the alveolar type II epithelial cells of the lung.
Gpr116 Receptor Regulates Distinctive Functions in Pneumocytes and Vascular Endothelium.
Betsholtz et al., Uppsala, Sweden. In Plos One, 2014
Despite its known expression in both the vascular endothelium and the lung epithelium, until recently the physiological role of the adhesion receptor Gpr116/ADGRF5 has remained elusive.
Defining the gene repertoire and spatiotemporal expression profiles of adhesion G protein-coupled receptors in zebrafish.
Monk et al., In Bmc Genomics, 2014
RESULTS: Here, we report that there are at least 59 aGPCRs in zebrafish that represent homologs of 24 of the 33 aGPCRs found in humans; compared to humans, zebrafish lack clear homologs of GPR110, GPR111, GPR114, GPR115, GPR116, EMR1, EMR2, EMR3, and EMR4.
International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors.
Schiöth et al., Amsterdam, Netherlands. In Pharmacol Rev, 2014
The new names, with old and alternative names within parentheses, are: ADGRA1 (GPR123), ADGRA2 (GPR124), ADGRA3 (GPR125), ADGRB1 (BAI1), ADGRB2 (BAI2), ADGRB3 (BAI3), ADGRC1 (CELSR1), ADGRC2 (CELSR2), ADGRC3 (CELSR3), ADGRD1 (GPR133), ADGRD2 (GPR144), ADGRE1 (EMR1, F4/80), ADGRE2 (EMR2), ADGRE3 (EMR3), ADGRE4 (EMR4), ADGRE5 (CD97), ADGRF1 (GPR110), ADGRF2 (GPR111), ADGRF3 (GPR113), ADGRF4 (GPR115), ADGRF5 (GPR116, Ig-Hepta), ADGRG1 (GPR56), ADGRG2 (GPR64, HE6), ADGRG3 (GPR97), ADGRG4 (GPR112), ADGRG5 (GPR114), ADGRG6 (GPR126), ADGRG7 (GPR128), ADGRL1 (latrophilin-1, CIRL-1, CL1), ADGRL2 (latrophilin-2, CIRL-2, CL2), ADGRL3 (latrophilin-3, CIRL-3, CL3), ADGRL4 (ELTD1, ETL), and ADGRV1 (VLGR1, GPR98).
A subpopulation of circulating endothelial cells express CD109 and is enriched in the blood of cancer patients.
Bertolini et al., Milano, Italy. In Plos One, 2013
Higher levels of endothelial specific transcripts expressed in developing endothelial cells CLEC14a, TMEM204, ARHGEF15, GPR116, were observed in sorted CD109+CECs when compared to sorted CD146+CECs, suggesting that these genes can play an important role not only during embryogenesis but also in adult angiogenesis.
GPR116, an adhesion G-protein-coupled receptor, promotes breast cancer metastasis via the Gαq-p63RhoGEF-Rho GTPase pathway.
Luo et al., Shanghai, China. In Cancer Res, 2013
In this study, we identified GPR116 as a novel regulator of breast cancer metastasis through expression and functional screening of the adhesion GPCR family.
Orphan G protein-coupled receptor GPR116 regulates pulmonary surfactant pool size.
Ikegami et al., Cincinnati, United States. In Am J Respir Cell Mol Biol, 2013
In this study, we demonstrate that expression of an orphan G protein-coupled receptor, GPR116, in the murine lung is developmentally regulated, reaching maximal levels 1 day after birth, and is highly expressed on the apical surface of alveolar type I and type II epithelial cells.
Essential regulation of lung surfactant homeostasis by the orphan G protein-coupled receptor GPR116.
St Croix et al., Frederick, United States. In Cell Rep, 2013
GPR116 is an orphan seven-pass transmembrane receptor whose function has been unclear.
Exome sequencing identifies early gastric carcinoma as an early stage of advanced gastric cancer.
Kim et al., Seoul, South Korea. In Plos One, 2012
The DYRK3, GPR116, MCM10, PCDH17, PCDHB1, RDH5 and UNC5C genes are recurrently mutated in EGCs and may be involved in early carcinogenesis.
Lung surfactant levels are regulated by Ig-Hepta/GPR116 by monitoring surfactant protein D.
Hirose et al., Yokohama, Japan. In Plos One, 2012
Here we show, by an analysis of gene-targeted mice exhibiting massive accumulation of surfactant, that Ig-Hepta/GPR116, an orphan receptor, is expressed on the type II cell and sensing the amount of surfactant by monitoring one of its protein components, surfactant protein D, and its deletion results in a pulmonary alveolar proteinosis and emphysema-like pathology.
Adipose tissue deletion of Gpr116 impairs insulin sensitivity through modulation of adipose function.
Wu et al., Guangzhou, China. In Febs Lett, 2012
G protein-coupled receptor 116 (GPR116) is a novel member of the G protein-coupled receptors and its function is largely unknown.
Characterization and functional study of a cluster of four highly conserved orphan adhesion-GPCR in mouse.
Langenhan et al., Oxford, United Kingdom. In Dev Dyn, 2012
RESULTS: We have studied evolution, expression, and function of an entire receptor group containing four uncharacterized aGPCR: Gpr110, Gpr111, Gpr115, and Gpr116.
Gene expression signatures differentiate adenocarcinoma of lung and breast origin in effusions.
Wang et al., Oslo, Norway. In Hum Pathol, 2012
Genes overexpressed in lung adenocarcinoma included TITF1, SFTPG, MMP7, EVA1, GPR116, HOP, SCGB3A2, and MET.
Identification of a core set of 58 gene transcripts with broad and specific expression in the microvasculature.
Betsholtz et al., Stockholm, Sweden. In Arterioscler Thromb Vasc Biol, 2008
The endothelial cell-specific expression of a selected subset of these, Eltd1, Gpr116, Ramp2, Slc9a3r2, Slc43a3, Rasip1, and NM_023516, was confirmed by real-time quantitative polymerase chain reaction and/or immunohistochemistry. CONCLUSIONS: We have used a combination of publicly available and own microarray data to identify 58 gene transcripts with broad yet specific expression in microvascular endothelium.
SEA domain autoproteolysis accelerated by conformational strain: energetic aspects.
Härd et al., Göteborg, Sweden. In J Mol Biol, 2008
SEA domain autoproteolysis accelerated by conformational strain.
SEA domain autoproteolysis accelerated by conformational strain: mechanistic aspects.
Härd et al., Göteborg, Sweden. In J Mol Biol, 2008
SEA domain autoproteolysis accelerated by conformational strain: mechanistic aspects.
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