GPR39
- Known as:
- GPR39
- Catalog number:
- Y213650
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- GPR39
Related genes to: GPR39
- Gene:
- GPR39 NIH gene
- Name:
- G protein-coupled receptor 39
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2016-10-05
Related products to: GPR39
Related articles to: GPR39
- GPCRs serve to coordinate renal collecting duct function, orchestrating fine-tuned regulation of water, electrolyte, and acid-base homeostasis. Classical GPCRs such as the vasopressin V2 receptor (V2R) have well-established roles: the V2R serves to regulate water reabsorption, and V2R dysregulation can underly diabetes insipidus. However, transcriptomic and phosphoproteomic advances have revealed a diverse repertoire of understudied GPCRs expressed in the collecting duct whose physiological roles remain largely undefined. Here, we review emerging insights into three such receptors-GPR39, ADGRF5, and ADGRG3-highlighting their distinct contributions to collecting duct function. We also discuss atypical GPCR-related signaling, including PKD1 and MAGED2, which expand the conceptual framework of GPCR biology in renal function. Collectively, these findings illustrate that GPCRs play diverse and underappreciated roles in collecting duct physiology and pathophysiology, and that continued mechanistic studies may uncover new therapeutic opportunities for kidney disease. - Source: PubMed
Publication date: 2026/04/17
Kui Mackenzie KZhang Jessica JPluznick Jennifer L - Coronary autoregulation is the ability of the normal heart to maintain constant coronary blood flow (CBF) over a wide range of coronary driving pressures (CDP). Despite being vital for survival, the mechanism of coronary autoregulation is unknown. We hypothesized that GPR39, present in vascular smooth muscle cells, together with its endogenous agonist 15-hydroxyeicosatetraenoic acid (15-HETE) orchestrate coronary autoregulation. - Source: PubMed
Publication date: 2026/03/23
Le D ElizabethKajimoto MasakiZhao YanMethner CarmenCao ZhipingCianciulli AgostinoSemeraro TeresaLaura Trist Iuni MargaretFranchi JessicaMarcheselli ChiaraParazzoli AlbertoMicheli FabrizioKaul Sanjiv - GPR39 is a zinc-sensing G protein-coupled receptor with critical roles in neurophysiological and metabolic processes across brain, pancreas, gut, liver, and fat tissues. Activated by extracellular zinc ions, GPR39 is involved in neurodegenerative diseases including altered levels in Alzheimer's disease (AD). Quantifying GPR39 levels could significantly advance understanding of its role in various metabolic and disease processes, enabling drug development and treatment monitoring. Our study reports the synthesis, radiolabeling, and comprehensive preclinical evaluation of the first radiotracer for GPR39 imaging: [C]TMN-OMe. The radiotracer demonstrated high radiochemical purity, molar activity, and stability in human serum. microPET/CT imaging, biodistribution, and autoradiography analyses confirmed selective binding to GPR39, with significantly reduced brain uptake in GPR39 knockout and AD mice, and in blockade conditions. Collectively, these findings support using [C]TMN-OMe to quantify GPR39 levels and define GPR39-based imaging as a novel platform to study mechanistic changes in neurological disorders. - Source: PubMed
Publication date: 2026/03/18
Bhoopal BhuvanachandraGollapelli Krishna KumarDamuka NareshKrizan IvanMiller MackFitzgerald Ryan WAmesar NishkaMumbaraddi DundappaZhu DongqinCervera-Juanes RitaJadiya PoojaWhitlow Christopher TSolingapuram Sai Kiran K - - Source: PubMed
Publication date: 2026/03/05
Santos-Zas IciaGurriaran-Rodriguez UxiaCid-Diaz TaniaLeal-Lopez SaulCasanueva Felipe FPazos-Randulfe YolandaCamiña Jesus P - Bile acids (BAs), long known for roles in food emulsion, also function as biological signals. By measuring intracellular calcium, we have recently discovered that GPR39, a G protein-coupled receptor, is a receptor for 3-O-sulfated BAs including lithocholic acid 3-sulfate (LCAS), taurolithocholic acid 3-sulfate (TLCAS) and glycolithocholic acid 3-sulfate (GLCAS) in cultured cells and in pancreatic acinar cells. We have now used multiple assays from electrophysiologic recording in Xenopus oocytes, Ca imaging, NanoBiT, ONE-GO, and TANGO to validate GPR39 activation by BAs. Among 30 BAs, only sulfated forms (LCAS, TLCAS and GLCAS) evoked GPR39 activation, activating 9 distinct Gα protein subtypes across the Gα, Gα, and Gα subfamilies. LCAS induced phosphorylation of ERK1/2 in the pancreas and the liver, which was markedly attenuated in Gpr39 knockout mice. Mutagenesis analysis identified the key residues essential for GPR39 signaling. Our results have revealed new signaling molecules downstream of GPR39 activation. - Source: PubMed
Publication date: 2026/02/04
Huang YanyunZi ZhentaoXia ChenliangRao Yi