Only in Titles

Search results for: G Protein Coupled Receptor GPR92 GPR93, Human

paperclip

#21094899   // To Up

The emerging role of promiscuous 7TM receptors as chemosensors for food intake.

In recent years, several highly promiscuous seven transmembrane (7TM) receptors have been cloned and characterized of which many are activated broadly by amino acids, proteolytic degradation products, carbohydrates, or free fatty acids (FFAs) and are expressed in taste tissue, the gastrointestinal (GI) tract, endocrine glands, adipose tissue, and/or kidney. This has led to the hypothesis that these receptors may act as sensors of food intake modulating, for example, release of incretin hormones from the gut, insulin/glucagon from the pancreas, and leptin from adipose tissue. In the present review, we describe the molecular mechanisms of nutrient-sensing of the calcium-sensing receptor (CaR), the G protein-coupled receptor family C, group 6, subtype A (GPRC6A), and the taste1 receptor T1R1/T1R3-sensing L-α-amino acids; the carbohydrate-sensing T1R2/T1R3 receptor; the proteolytic degradation product sensor GPR93 (also termed GPR92); and the FFA sensing receptors FFA1, FFA2, FFA3, GPR84, and GPR120. Due to their omnipresent nature, the natural ligands have had limited usability in pharmacological/physiological studies which has hampered the elucidation of the physiological function and therapeutic prospect of their receptors. However, an increasing number of subtype-selective ligands and/or receptor knockout mice are being developed which at least for some of the receptors have validated them as promising drug targets in, for example, type II diabetes.
Petrine Wellendorph, Lars Dan Johansen, Hans Bräuner-Osborne

2558 related Products with: The emerging role of promiscuous 7TM receptors as chemosensors for food intake.

100 tests100 assays1,000 tests96 Tests50 assays96 wells100Tests100100 assays100 assays

Related Pathways

paperclip

#19524700   2009/06/12 To Up

Non-Edg family lysophosphatidic acid (LPA) receptors.

Lysophosphatidic acid (LPA; 1- or 2-acyl-sn-glycero-3-phosphate) is a bioactive phospholipid with mitogenic and/or morphological effects on many cell types. In addition, LPA has been reported to play important roles in various biological processes. It was originally thought that the cellular effects of LPA are mediated by three subtypes of G-protein-coupled receptors: LPA(1)/Edg2, LPA(2)/Edg4, and LPA(3)/Edg7. They share 50-57% amino acid identities and, together with five sphingosine-1-phosphate receptors (S1P(1)/Edg1, S1P(2)/Edg5, S1P(3)/Edg3, S1P(4)/Edg6, and S1P(5)/Edg8), comprise the endothelial cell differentiation gene (Edg) family. However, even after finding of the Edg family LPA receptors, the existence of an additional LPA receptor(s) has been implied by several reports. In 2003, we identified p2y9/GPR23 as a fourth LPA receptor, LPA(4), which is structurally distant from the Edg family LPA receptors. LPA(4)/p2y9/GPR23 has stimulated identification of two additional LPA receptors, LPA(5)/GPR92/GPR93 and LPA(6)/p2y5. These findings made us aware of the existence of a novel "non-Edg" LPA receptor family. This review article focuses on the identification, properties and possible functions of the non-Edg family LPA receptors: LPA(4)/p2y9/GPR23, LPA(5)/GPR92/GPR93 and LPA(6)/p2y5.
Satoshi Ishii, Kyoko Noguchi, Keisuke Yanagida

1865 related Products with: Non-Edg family lysophosphatidic acid (LPA) receptors.

50 5 mg100ug Lyophilized 1 G 1 G 25 G 5 G 5 G 5 G 6 ml Ready-to-use 0,5 ML10 mg

Related Pathways

paperclip

#19487246   2009/06/01 To Up

Molecular pharmacology of promiscuous seven transmembrane receptors sensing organic nutrients.

A number of highly promiscuous seven transmembrane (7TM) receptors have been cloned and characterized within the last few years. It is noteworthy that many of these receptors are activated broadly by amino acids, proteolytic degradation products, carbohydrates, or free fatty acids and are expressed in taste tissue, the gastrointestinal tract, endocrine glands, adipose tissue, and/or kidney. These receptors thus hold the potential to act as sensors of food intake, regulating, for example, release of incretin hormones from the gut, insulin/glucagon from the pancreas, and leptin from adipose tissue. The promiscuous tendency in ligand recognition of these receptors is in contrast to the typical specific interaction with one physiological agonist seen for most receptors, which challenges the classic "lock-and-key" concept. We here review the molecular mechanisms of nutrient sensing of the calcium-sensing receptor, the G protein-coupled receptor family C, group 6, subtype A (GPRC6A), and the taste1 receptor T1R1/T1R3, which are sensing L-alpha-amino acids, the carbohydrate-sensing T1R2/T1R3 receptor, the proteolytic degradation product sensor GPR93 (also termed GPR92), and the free fatty acid (FFA) sensing receptors FFA1, FFA2, FFA3, GPR84, and GPR120. The involvement of the individual receptors in sensing of food intake has been validated to different degrees because of limited availability of specific pharmacological tools and/or receptor knockout mice. However, as a group, the receptors represent potential drug targets, to treat, for example, type II diabetes by mimicking food intake by potent agonists or positive allosteric modulators. The ligand-receptor interactions of the promiscuous receptors of organic nutrients thus remain an interesting subject of emerging functional importance.
Petrine Wellendorph, Lars Dan Johansen, Hans Bräuner-Osborne

2820 related Products with: Molecular pharmacology of promiscuous seven transmembrane receptors sensing organic nutrients.

6 ml Ready-to-use 500g 2 ml Ready-to-use 5 G 100ul50 2 Pieces/Box 2 ml Ready-to-use 2x5L 100ul50 ug 100 UG

Related Pathways