Molecular Signaling Through G-Protein-Coupled Receptors and the Control of Intracellular Calcium in Myometrium

2005 ◽  
Vol 12 (7) ◽  
pp. 479-487 ◽  
Author(s):  
Barbara M. Sanborn ◽  
Chun-Ying Ku ◽  
Sergiy Shlykov ◽  
Lidiya Babich
Keyword(s):  
Intracellular Calcium ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Molecular Signaling ◽  
G Protein Coupled

scholarly journals Identification of a Novel Family of Targets of PYK2 Related to Drosophila Retinal Degeneration B (rdgB) Protein

1999 ◽  
Vol 19 (3) ◽  
pp. 2278-2288 ◽  
Author(s):  
Sima Lev ◽  
John Hernandez ◽  
Ricardo Martinez ◽  
Alon Chen ◽  
Greg Plowman ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Retinal Degeneration ◽  
G Protein ◽  
Binding Proteins ◽  
G Protein Coupled Receptors ◽  
Sequence Motif ◽  
Phosphoinositide Metabolism ◽  
Amino Terminal ◽  
Terminal Domain ◽  
G Protein Coupled

ABSTRACT The protein tyrosine kinase PYK2 has been implicated in signaling pathways activated by G-protein-coupled receptors, intracellular calcium, and stress signals. Here we describe the molecular cloning and characterization of a novel family of PYK2-binding proteins designated Nirs (PYK2 N-terminal domain-interacting receptors). The three Nir proteins (Nir1, Nir2, and Nir3) bind to the amino-terminal domain of PYK2 via a conserved sequence motif located in the carboxy terminus. The primary structures of Nirs reveal six putative transmembrane domains, a region homologous to phosphatidylinositol (PI) transfer protein, and an acidic domain. The Nir proteins are the human homologues of the Drosophila retinal degeneration B protein (rdgB), a protein implicated in the visual transduction pathway in flies. We demonstrate that Nirs are calcium-binding proteins that exhibit PI transfer activity in vivo. Activation of PYK2 by agents that elevate intracellular calcium or by phorbol ester induce tyrosine phosphorylation of Nirs. Moreover, PYK2 and Nirs exhibit similar expression patterns in several regions of the brain and retina. In addition, PYK2-Nir complexes are detected in lysates prepared from cultured cells or from brain tissues. Finally, the Nir1-encoding gene is located at human chromosome 17p13.1, in proximity to a locus responsible for several human retinal diseases. We propose that the Nir and rdgB proteins represent a new family of evolutionarily conserved PYK2-binding proteins that play a role in the control of calcium and phosphoinositide metabolism downstream of G-protein-coupled receptors.

scholarly journals Lysophosphatidylcholine Containing Anisic Acid Is Able to Stimulate Insulin Secretion Targeting G Protein Coupled Receptors

Nutrients ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 1173 ◽  
Author(s):  
Anna Drzazga ◽  
Marta Okulus ◽  
Magdalena Rychlicka ◽  
Łukasz Biegała ◽  
Anna Gliszczyńska ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Insulin Secretion ◽  
Intracellular Calcium ◽  
G Protein ◽  
Phenolic Acids ◽  
G Protein Coupled Receptors ◽  
Calcium Flux ◽  
Pancreatic Cell ◽  
Anisic Acid ◽  
G Protein Coupled

Diabetes mellitus is a worldwide health problem with high rates of mortality and morbidity. Management of diabetes mellitus by dietary components is achievable especially at the initial stage of the disease. Several studies confirmed the antidiabetic activities of simple phenolic acids and lysophosphatidylcholine (LPC). The main goal of this study was to identify new potential insulin secretion modulators obtained by combining the structures of two natural compounds, namely O-methyl derivatives of phenolic acids and phospholipids. LPC and phosphatidylcholine bearing methoxylated aromatic carboxylic acids were tested as potential agents able to improve glucose-stimulated insulin secretion (GSIS) and intracellular calcium mobilization in MIN6 β pancreatic cell line. Our results show that LPC with covalently bonded molecule of p-anisic acid at the sn-1 position was able to induce GSIS and intracellular calcium flux. Notably, 1-anisoyl-2-hydroxy-sn-glycero-3-phosphocholine did not affect the viability of MIN6 cells, suggesting its potential safe use. Furthermore, we have shown that three G protein coupled receptors, namely GPR40, GPR55, and GPR119, are targeted by this LPC derivative.

Functional Screening of G Protein–Coupled Receptors by Measuring Intracellular Calcium with a Fluorescence Microplate Reader

2002 ◽  
Vol 7 (3) ◽  
pp. 233-246 ◽  
Author(s):  
Matthias U. Kassack ◽  
Barbara Höfgen ◽  
Jochen Lehmann ◽  
Niels Eckstein ◽  
J. Mark Quillan ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Functional Screening ◽  
Microplate Reader ◽  
G Protein Coupled

scholarly journals Evidence of G-Protein-Coupled Receptors (GPCR) in the Parasitic Protozoa Plasmodium falciparum—Sensing the Host Environment and Coupling within Its Molecular Signaling Toolkit

2021 ◽  
Vol 22 (22) ◽  
pp. 12381
Author(s):  
Pedro H. S. Pereira ◽  
Celia R. S. Garcia
Keyword(s):  
Plasmodium Falciparum ◽  
G Protein ◽  
Biological Response ◽  
Protozoan Parasite ◽  
G Protein Coupled Receptors ◽  
Complex Life Cycle ◽  
Molecular Signaling ◽  
Parasite Plasmodium Falciparum ◽  
And Function ◽  
G Protein Coupled

Throughout evolution, the need for single-celled organisms to associate and form a single cluster of cells has had several evolutionary advantages. In complex, multicellular organisms, each tissue or organ has a specialty and function that make life together possible, and the organism as a whole needs to act in balance and adapt to changes in the environment. Sensory organs are essential for connecting external stimuli into a biological response, through the senses: sight, smell, taste, hearing, and touch. The G-protein-coupled receptors (GPCRs) are responsible for many of these senses and therefore play a key role in the perception of the cells’ external environment, enabling interaction and coordinated development between each cell of a multicellular organism. The malaria-causing protozoan parasite, Plasmodium falciparum, has a complex life cycle that is extremely dependent on a finely regulated cellular signaling machinery. In this review, we summarize strong evidence and the main candidates of GPCRs in protozoan parasites. Interestingly, one of these GPCRs is a sensor for K+ shift in Plasmodium falciparum, PfSR25. Studying this family of proteins in P. falciparum could have a significant impact, both on understanding the history of the evolution of GPCRs and on finding new targets for antimalarials.

scholarly journals Integrated On-chip Photodetection of Intracellular Calcium in Response to the Activation of G-protein Coupled Receptors

2012 ◽  
Vol 47 ◽  
pp. 993-996
Author(s):  
S.A.M. Martins ◽  
G. Moulas ◽  
J.R.C. Trabuco ◽  
G.A. Monteiro ◽  
V. Chu ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
On Chip ◽  
G Protein Coupled
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