scholarly journals The neuropeptide head activator is a high-affinity ligand for the orphan G-protein-coupled receptor GPR37

2006 ◽  
Vol 119 (3) ◽  
pp. 542-549 ◽  
Author(s):  
M. Rezgaoui
Keyword(s):  
G Protein ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Affinity Ligand ◽  
Head Activator ◽  
G Protein Coupled ◽  
High Affinity Ligand

Molecular basis of G protein-coupled receptor high affinity for gastrin-releasing peptide (GRP)

2003 ◽  
Vol 124 (4) ◽  
pp. A469
Author(s):  
Tomoo Nakagawa ◽  
Jose A. Tapia ◽  
Kenji Tokita ◽  
Samuel Mantey ◽  
Michael Schumann ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptor ◽  
Gastrin Releasing Peptide ◽  
High Affinity ◽  
G Protein Coupled

scholarly journals The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

2011 ◽  
Vol 108 (6) ◽  
pp. 2534-2539 ◽  
Author(s):  
M. F. Bolliger ◽  
D. C. Martinelli ◽  
T. C. Sudhof
Keyword(s):  
Cell Adhesion ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
G Protein Coupled

A high-affinity peptide substrate for G protein-coupled receptor kinase 2 (GRK2)

Amino Acids ◽  
2019 ◽  
Vol 51 (6) ◽  
pp. 973-976
Author(s):  
Daisuke Asai ◽  
Masaharu Murata ◽  
Riki Toita ◽  
Takahito Kawano ◽  
Hideki Nakashima ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
Peptide Substrate ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Affinity Peptide ◽  
G Protein Coupled

scholarly journals Urotensin-II peptidomimetic incorporating a non-reducible 1,5-triazole disulfide bond reveals a pseudo-irreversible covalent binding mechanism to the urotensin G-protein coupled receptor

2017 ◽  
Vol 15 (21) ◽  
pp. 4704-4710 ◽  
Author(s):  
Salvatore Pacifico ◽  
Aidan Kerckhoffs ◽  
Andrew J. Fallow ◽  
Rachel E. Foreman ◽  
Remo Guerrini ◽  
...  
Keyword(s):  
G Protein ◽  
Disulfide Bond ◽  
Covalent Binding ◽  
Urotensin Ii ◽  
Binding Mechanism ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
G Protein Coupled ◽  
Insight Into

New high affinity peptidomimetic ligands have been developed that provided new insight into the mechanism of binding of U-II peptide with the urotensin-II receptor.

Sphingosine-1-phosphate is a ligand for the G protein-coupled receptor EDG-6

Blood ◽  
2000 ◽  
Vol 95 (8) ◽  
pp. 2624-2629 ◽  
Author(s):  
James R. Van Brocklyn ◽  
Markus H. Gräler ◽  
Günter Bernhardt ◽  
John P. Hobson ◽  
Martin Lipp ◽  
...  
Keyword(s):  
G Protein ◽  
Hek293 Cells ◽  
Hematopoietic Tissue ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Extracellular Signal ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor ◽  
High Concentrations ◽  
G Protein Coupled

Abstract EDG-6 is a recently cloned member of the endothelial differentiation gene (EDG) G protein-coupled receptor family that is expressed in lymphoid and hematopoietic tissue and in the lung. Homology of EDG-6 to the known sphingosine-1-phosphate (SPP) receptors EDG-1, EDG-3, and EDG-5 and lysophosphatidic acid (LPA) receptors EDG-2 and EDG-4 suggested that its ligand may be a lysophospholipid or lysosphingolipid. We examined the binding of [32P]SPP to HEK293 cells, transiently transfected with cDNA encoding EDG-6. Binding of [32P]SPP was saturable, demonstrating high affinity (KD = 63 nmol/L). Binding was also specific for SPP, as only unlabeled SPP and sphinganine-1-phosphate, which lacks the trans double bond at the 4 position, potently displaced radiolabeled SPP. LPA did not compete for binding of SPP at any concentration tested, whereas sphingosylphosphorylcholine competed for binding to EDG-6, but only at very high concentrations. In addition, SPP activated extracellular signal-regulated kinase (Erk) in EDG-6 transfected cells in a pertussis toxin-sensitive manner. These results indicate that EDG-6 is a high affinity receptor for SPP, which couples to a Gi/o protein, resulting in the activation of growth-related signaling pathways.

scholarly journals Role of the G-Protein-Coupled Receptor GPR12 as High-Affinity Receptor for Sphingosylphosphorylcholine and Its Expression and Function in Brain Development

2003 ◽  
Vol 23 (3) ◽  
pp. 907-914 ◽  
Author(s):  
Atanas Ignatov ◽  
Julia Lintzel ◽  
Irm Hermans-Borgmeyer ◽  
Hans-Jürgen Kreienkamp ◽  
Patrick Joost ◽  
...  
Keyword(s):  
Brain Development ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
And Function ◽  
G Protein Coupled

scholarly journals Characterization of a novel G-protein coupled receptor from the parasitic nematode H. contortus with high affinity for serotonin

2004 ◽  
Vol 86 (1) ◽  
pp. 255-266 ◽  
Author(s):  
Martin W. Smith ◽  
Tracy L. Borts ◽  
Renee Emkey ◽  
Carolyn A. Cook ◽  
Christina J. Wiggins ◽  
...  
Keyword(s):  
G Protein ◽  
Parasitic Nematode ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
G Protein Coupled

Sphingosine-1-phosphate is a ligand for the G protein-coupled receptor EDG-6

Blood ◽  
2000 ◽  
Vol 95 (8) ◽  
pp. 2624-2629
Author(s):  
James R. Van Brocklyn ◽  
Markus H. Gräler ◽  
Günter Bernhardt ◽  
John P. Hobson ◽  
Martin Lipp ◽  
...  
Keyword(s):  
G Protein ◽  
Hek293 Cells ◽  
Hematopoietic Tissue ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Extracellular Signal ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor ◽  
High Concentrations ◽  
G Protein Coupled

EDG-6 is a recently cloned member of the endothelial differentiation gene (EDG) G protein-coupled receptor family that is expressed in lymphoid and hematopoietic tissue and in the lung. Homology of EDG-6 to the known sphingosine-1-phosphate (SPP) receptors EDG-1, EDG-3, and EDG-5 and lysophosphatidic acid (LPA) receptors EDG-2 and EDG-4 suggested that its ligand may be a lysophospholipid or lysosphingolipid. We examined the binding of [32P]SPP to HEK293 cells, transiently transfected with cDNA encoding EDG-6. Binding of [32P]SPP was saturable, demonstrating high affinity (KD = 63 nmol/L). Binding was also specific for SPP, as only unlabeled SPP and sphinganine-1-phosphate, which lacks the trans double bond at the 4 position, potently displaced radiolabeled SPP. LPA did not compete for binding of SPP at any concentration tested, whereas sphingosylphosphorylcholine competed for binding to EDG-6, but only at very high concentrations. In addition, SPP activated extracellular signal-regulated kinase (Erk) in EDG-6 transfected cells in a pertussis toxin-sensitive manner. These results indicate that EDG-6 is a high affinity receptor for SPP, which couples to a Gi/o protein, resulting in the activation of growth-related signaling pathways.

Sign in / Sign up

Export Citation Format

Share Document