anti-G Protein-Coupled Receptor 132 (GPR132) Antibodies

Human G Protein-Coupled Receptor 132 (GPR132) interaction partners

1. G protein-coupled receptor 132 (Gpr132) functions as a key macrophage sensor of the rising lactate in the acidic tumor milieu to mediate the reciprocal interaction between cancer cells and macrophages during breast cancer metastasis. Lactate activates macrophage Gpr132 to promote the alternatively activated macrophage (M2)-like phenotype, which, in turn, facilitates cancer cell adhesion, migration, and invasion.

2. High GPR132 expression is associated with acute lymphoblastic leukemia.

3. coexpression of OGR1- and G2A-enhanced proton sensitivity and proton-induced calcium signals. This alteration is attributed to oligomerization of OGR1 and G2A. The oligomeric potential locates receptors at a specific site, which leads to enhanced

4. we found an additional novel G2A variant (G2A-b) that is the major transcript with functional response to ligand stimulation as well as G2A-a, and succeeded in discriminating proton-sensing and oxidized fatty acid-sensing activities of G2A.

5. G2A is a negative modifier of lymphoid leukemogenesis initiated by the BCR-ABL oncogene

6. In atherosclerotic plaques of human coronary arterial specimens, G2A is expressed by macrophages within the lipid-rich plaques, whereas no immunoreactivity of G2A is observed in fibrous plaques where macrophages do not exist.

7. G2A can activate a specific combination of G proteins, and G2A/LPC-induced apoptosis involves both G alpha(13)- and G alpha(s)-mediated pathways

8. G2A was not detected in either brain or skin vascular endothelial cell type.

9. G2A is a proton-sensing G-protein-coupled receptor antagonized by lysophosphatidylcholine

10. Activity of the human G2A receptor is less sensitive to pH fluctuations as measured by inositol phosphate and cAMP accumulation.

11. results indicate that G protein-coupled receptor G2A is a receptor for 9-hydroxyoctadecadienoic acid (9-HODE) and other oxidized free fatty acids and is activated by oxidized free fatty acids

12. G2A latent within neutrophil secretory vesicles may facilitate signaling through lysophospholipids for neutrophil activation and calcium flux.

13. 9-HODE-G2A signaling plays proinflammatory roles in skin under oxidative conditions

14. the G-protein-coupled receptor G2A, unlike its relative GPR4, is involved in the chemotaxis of monocytic cells.

Mouse (Murine) G Protein-Coupled Receptor 132 (GPR132) interaction partners

1. this study shows that G2A protects mice againstsSepsis by modulating Kupffer cell activation via cooperativity with adenosine receptor 2b

2. G2A is necessary to position macrophages in the proinflammatory microenvironment surrounding the center of inflammation. In absence of G2A the macrophages are localized in an antiinflammatory microenvironment and macrophage polarization is shifted toward M2-like macrophages.

3. GPR132 responds to a select panel of oxygenated polyunsaturated fatty acids to enhance both embryonic and adult hematopoiesis.

4. G2A overexpression reduced the infiltration of granulocytes and attenuated hyperalgesia after CFA injection. G2A knockdown increased the number of immune cells before CFA injection and prolonged the inflammatory hyperalgesia.

5. Lactate activates macrophage Gpr132 to promote the alternatively activated macrophage (M2)-like phenotype, which, in turn, facilitates cancer cell adhesion, migration, and invasion. Consequently, Gpr132 deletion reduces M2 macrophages and impedes breast cancer lung metastasis in mice.

6. The authors report that macrophage PPARgamma deletion in mice not only exacerbates mammary tumor development but also impairs the anti-tumor effects of rosiglitazone. Mechanistically, the authors identify Gpr132 as a novel direct PPARgamma target in macrophage whose expression is enhanced by PPARgamma loss but repressed by PPARgamma activation.

7. the data suggest that G2A signaling serves to dampen intestinal inflammation via the production of IFN-gamma, which, in turn, enhances monocyte maturation to a less inflammatory program and ultimately reduces eosinophil-induced injury of colonic tissues

8. Lyso-PS signaled to macrophages in a G2A-dependent manner for their enhanced production of prostaglandin E2 (PGE2) via a calcium-dependent cytosolic phospholipase A2/cyclooxygenase-mediated mechanism.

9. G2A is expressed predominantly by macrophages within atherosclerotic lesions at the aortic root of apolipoprotein E-deficient mice.

10. role of G2A in lysophosphatidylcholine-mediated T-cell migration

11. G2A signaling regulates macrophage chemotaxis to lysophosp[hatidylcholine.

12. data indicate the ability of lysophosphatidylcholine to stimulate macrophage & T-cell chemotaxis via G2A is not manifested in vivo & G2A-mediated proapoptotic rather than chemotactic action is most penetrant during atherogenesis

13. the neuritogenic effect of sPLA2 is mediated by generation of LPC and subsequent activation of G2A

14. Examination of lipoprotein profiles revealed elevated levels of circulating high-density lipoprotein (HDL) cholesterol in G2A-/- LDLR-/- mice compared with their G2A+/+ LDLR-/- counterparts after extended periods of diet intervention.

15. Endothelial G2A expression may aid in prevention of vascular inflammation and atherosclerosis.

16. The G2A receptor is important for hepatobiliary bile salt, cholesterol, and phospholipid homeostasis and for the pathogenesis of cholesterol gallstone formation.

17. NADPH oxidase-dependent generation of lysophosphatidylserine enhances clearance of activated and dying neutrophils via G2A.

18. In the absence of G2A, increased macrophage activation and decreased apoptosis is associated with accumulation of macrophages in the aorta and increased atherosclerosis

19. study of the G2A-mediated effects in the pathophysiology of T cell-mediated autoimmune disease; it was concluded that the proposed anti-proliferative and chemotactic functions of G2A are not manifested in vivo

20. ApoE-dependent modulation of HDL and atherosclerosis by G2A in LDL receptor-deficient mice independent of bone marrow-derived cells.