GPR39 antibody
- Known as:
- GPR39 (anti-)
- Catalog number:
- orb101834
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- GPR39 antibody
Related genes to: GPR39 antibody
- 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 antibody
Related articles to: GPR39 antibody
- Acute kidney injury (AKI) is a life-threatening event prevalent in hospitalized patients but also not rare among endurance sports athletes. Hypoxia, oxidative stress, and sterile inflammation are the key pathophysiological factors driving kidney damage in AKI. Zinc is an essential trace element required for the intact function of approximately 3000 proteins (~10% of the human proteome), including over 300 enzymes for which zinc serves as a cofactor. Cell biological tasks of zinc signaling include adaptive responses to hypoxia and oxidative stress, as well as anti-inflammatory effects. The underlying molecular pathways involve modulation of hypoxia-inducible factor signaling, suppression of reactive oxygen species (ROS) generation, and inhibition of the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the latter being the major pro-inflammatory transcription factor. As a catalytic cofactor for the "classical" histone deacetylases, zinc is essential for epigenetic control of gene expression, thereby exerting further adaptive effects. Apart from the intracellular zinc signaling, extracellular zinc elicits cytoprotective and anti-inflammatory effects via the G Protein-Coupled Receptor 39 (GPR39). GPR39 activation by zinc binding may exert antioxidant and anti-inflammatory effects mediated by the zinc-finger protein A20 (TNFAIP3) and NF-κB suppression, followed by reduced production of pro-inflammatory cytokines such as tumor necrosis factor (TNF), interleukin-1β (IL-1β), and IL-6. At the same time, GPR39 signaling may stimulates the release of the anti-inflammatory cytokine IL-10, thus shifting the kidney tissue towards an anti-inflammatory milieu, promoting renal recovery. The present review focuses on the role of zinc in AKI to identify potential therapeutic strategies targeting zinc signaling for renoprotection and biomarker-based risk stratification. - Source: PubMed
Publication date: 2026/06/01
Lebedeva SvetlanaBravyy YanBeknazarova AnnaSmolyarchuk Elena AMutig Kerim - In this review, we, on behalf of the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology, describe criteria for assessing the evidence for pairing receptors with endogenous/physiological ligands for formal receptor deorphanization. This process is illustrated through consideration of the class A G protein-coupled receptors (GPCRs) not yet formally paired with an endogenous/physiological ligand by the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology. Of the 67 orphan class A GPCRs considered, 25 class A GPCRs have no identified endogenous agonists, although 5 (GPR21, GPR27, GPR52, GPR85, and GPR88) have synthetic ligands that have the potential to be used as tools for uncovering physiological roles and further pharmacological properties of these receptors. Surprisingly, 6 orphan GPCRs (GPR135, GPR152, GPR153, MRGPRF, MRGPRG, and MRGPRX3) have no clear pharmacology or phenotype reported following genetic disruption. Thirty-two orphan GPCRs have been paired with at least 1 endogenous agonist (mainly lipids and their derivatives, peptides, and other metabolites), but further characterization is required from the scientific community to validate these results. We identify 10 orphan class A GPCRs for which there are plausible grounds for considering deorphanization: GPR4 (protons), GPR15 (GPR15L), GPR31 (12S-hydroxyeicosatetraenoic acid), GPR39 (zinc divalent ions, Zn), GPR65 (protons), GPR68 (protons), GPR132 (9-hydroxyoctadecadienoic acid), GPR183 (7α,25-dihydroxycholesterol), MRGPRD (β-alanine), and MRGPRX1 (bovine adrenal medulla peptide 8-22). The issue of nomenclature for these 10 GPCRs will be considered by further subcommittees of the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology. We hope this review will prompt further investigations into these members of the currently most widely clinically exploited protein superfamily. SIGNIFICANCE STATEMENT: The use of systematic, rational nomenclature for drug targets provides a framework to ensure consistent identification and rapid recognition. Given that G protein-coupled receptors have fundamental physiological roles and are widespread targets of drugs in current clinical use, we hope the target summary and deorphanization criteria provided here will prompt renewed efforts to investigate these orphan receptors as regulators of physiology and as opportunities for future therapeutic exploitation. - Source: PubMed
Publication date: 2026/05/08
Alexander Stephen P HBennett Kirstie ABrown Andrew JGlass MichelleGloriam David EHanson JulienInsel Paul AKelly EamonnLangmead Christopher JMartemyanov Kirill ANeubig Rick ROffermanns StefanRosenkilde Mette MSchulte GunnarSmith Nicola JWu HuixianFaccenda ElenaHarding Simon DDavenport Anthony P - Heat stress (HS) is a major environmental challenge in modern poultry production, where high metabolic heat output and intensive genetic selection increase vulnerability to thermal load. Beyond impairing thermoregulation and feed intake, HS disrupts intestinal barrier integrity, induces oxidative stress and inflammation, and promotes systemic metabolic dysregulation. The gastrointestinal tract has therefore emerged as a central target and amplifier of HS-induced pathology, highlighting the importance of gut-focused nutritional interventions. Zinc (Zn), an essential trace element with broad catalytic and regulatory functions, has gained attention as a key modulator of intestinal and systemic resilience under HS conditions. Accumulating evidence indicates that Zn not only supports antioxidant defenses and immune regulation but also preserves epithelial architecture by stabilizing tight junctions (TJ), modulating heat shock responses, suppressing inflammatory signaling, and promoting epithelial renewal. At the molecular level, Zn acts as a signaling ion through activation of the Zn-sensing receptor, G protein-coupled receptor 39 (GPR39) and downstream phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT)/mammalian target of rapamycin (mTOR) and mitogen-activated protein kinase (MAPK) pathways, thereby facilitating epithelial repair and barrier restoration. Recent avian intestinal organoid studies provide direct mechanistic evidence that organic and moderately chelated Zn sources, such as Zn proteinate, more effectively alleviate HS-induced epithelial injury than inorganic forms. Complementary in vivo data further demonstrate HS-induced redistribution of Zn via coordinated regulation of Zn transporters and metallothionein, linking local intestinal protection with systemic Zn homeostasis. In conclusion, current evidence positions Zn as a central nutritional regulator of HS resilience and supports the development of precision Zn supplementation strategies for sustainable poultry production under increasing thermal stress. - Source: PubMed
Publication date: 2026/05/25
Erek GozdeArapbai Uulu NursultanSahin Kazim - Spinal glycinergic disinhibition represents an important contributor to mechanical pain hypersensitivity. However, the molecular mechanisms through which peripheral inflammation induces glycinergic disinhibition remain incompletely understood. Here we show that the protein tyrosine phosphatase-1B (PTP1B) is present at inhibitory synapses of spinal somatostatin-positive (SOM) interneurons, a key subpopulation of mechanosensory neurons that conveys nociceptive information. PTP1B directly binds to and dephosphorylates the glycine receptor α1 subunit (GlyR α1). Peripheral inflammation-induced hyperexpression of PTP1B competitively interrupts the interaction of GlyR α1 with GPR39, leading to glycinergic disinhibition, enhanced excitatory output of SOM interneurons, and behavioral hypersensitivity. Pharmacological activation of GPR39, however, could disrupt the PTP1B-GlyR α1 interaction and resume GPR39 binding, resulting in reinstated glycinergic inhibition. Our findings uncover the important role of PTP1B in glycinergic disinhibition following peripheral inflammation and suggest a mechanistic model for dynamic regulation of glycinergic transmission by alternative interactions of GlyR α1 with PTP1B and GPR39. - Source: PubMed
Publication date: 2026/05/20
Bai Hu-HuBai XueLiu Xiao-XueGao Yu-BoLi JuanYang XuDang Jia-NingWang YingZhang Yu-XuanZhang Zhi-YangZhang QiLiu Yan-NiLiu Jiang-PingSuo Zhan-Wei - - Source: PubMed
Publication date: 2026/04/29
Huang YanyunZi ZhentaoXia ChenliangRao Yi