Ask about this productRelated genes to: NOX1 antibody
- Gene:
- DUOX1 NIH gene
- Name:
- dual oxidase 1
- Previous symbol:
- -
- Synonyms:
- NOXEF1, THOX1, LNOX1
- Chromosome:
- 15q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-30
- Date modifiied:
- 2016-01-15
- Gene:
- NOX1 NIH gene
- Name:
- NADPH oxidase 1
- Previous symbol:
- -
- Synonyms:
- NOH1, NOH-1, MOX1, GP91-2
- Chromosome:
- Xq22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-24
- Date modifiied:
- 2016-10-05
Related products to: NOX1 antibody
Related articles to: NOX1 antibody
- Osteoporosis, the most prevalent skeletal disorder, is primarily driven by aberrantly increased osteoclast formation and/or activity. Targeting hyperactive osteoclasts remains the cornerstone of current therapeutic strategies. Crebanine (Cre), a natural isoquinoline-derived alkaloid with diverse pharmacological activities, has not yet been explored for osteoporosis treatment. This study aimed to evaluate the therapeutic potential of Cre against ovariectomy (OVX)-induced osteoporosis and elucidate its underlying mechanisms. Cre dose-dependently inhibited osteoclast differentiation, actin ring formation, and bone resorption by downregulating nuclear factor of activated T cells 1 (NFATc1) and key osteoclast-related genes. Simultaneously, Cre enhanced osteoblast differentiation and mineralization, upregulated osteoblast marker genes, and restored hydrogen peroxide-impaired alkaline phosphatase (ALP) activity impaired by hydrogen peroxide, indicating dual regulation of bone remodeling. Mechanistically, Cre activated sirtuin 1 (Sirt1), promoting p65 deacetylation, inactivated IκB kinase (IKK), and stabilized IκBα, thus inhibiting nuclear factor-kappaB (NF-κB) signaling. Additionally, Cre reduced reactive oxygen species (ROS) by upregulating antioxidant enzymes (heme oxygenase-1 (HO-1), catalase) and suppressing nicotinamide adenine dinucleotide (NAD) phosphate (NADPH) oxidases (NOX1/4). Furthermore, Cre specifically bound to the predicted site of receptor activator of NF-κB (RANK), blocking RANK ligand (RANKL)-RANK interaction and disrupting downstream protein kinase B (Akt) and mitogen-activated protein kinase (MAPK) signaling pathways. In the OVX mouse model, Cre significantly attenuated bone loss and osteoclastogenesis. Crucially, Cre showed no toxicity in liver or kidney function tests. Collectively, these findings demonstrate that Cre exerts dual therapeutic effects, inhibiting osteoclastogenesis via Sirt1-mediated NF-κB/ROS suppression and promoting osteoblast activity, providing a promising therapeutic strategy for osteoporosis. - Source: PubMed
Publication date: 2025/07/31
Zhang HaojieZhao XuanWang ZhengMiao JiansenHu XinliCui PengJin ChenZhao XibinLiang HaiboYe HantaoXu YiningChen XiaolongWang WeiLu Shibao - The retinal pigment epithelium (RPE) performs key roles in preserving retinal integrity and must continuously manage oxidative stress (OS). We previously demonstrated that the canonical phospholipase D isoforms, PLD1 and PLD2, mediate the RPE inflammatory response triggered by inflammatory injury. This study explores the mechanisms of modulation of OS mediated by PLD inhibition in RPE cells exposed to high glucose (HG) levels. ARPE-19, D407 and the novel human RPE cell line ABC were cultured under HG (33 mM) or normal glucose (NG, 5.5 mM) conditions. To inhibit PLD1, PLD2, and NADPH oxidase (NOX), VU0359595 (PLD1i), VU0285655-1 (PLD2i), and diphenyleneiodonium chloride (DPI) were used, respectively. HG exposure significantly increased reactive oxygen species (ROS) levels and reduced mitochondrial membrane potential (MMP) in ARPE-19 and D407 cells. These effects were prevented by PLD1i and PLD2i in an Nrf-2 and cyclooxygenase-2 -independent manner. In ARPE-19 cells, DPI prevented OS induced by HG as well as the stress triggered by the combination of phosphatidic acid + diacylglycerol, bioactive lipids generated through the PLD pathway-. Similarly, HG elevated ROS levels in ABC cells, and this increase was prevented by PLD1i and DPI. RNAseq analysis showed differential expression of NOX family members (NOX1,2 and 4 and DUOX1 and 2) in ARPE-19 and ABC cells. Our results demonstrate that PLDs inhibition prevent HG-induced OS in RPE cells, possibly by reducing NOX activity. The PLD pathway constitutes a novel pharmacological target to simultaneously mitigate OS and the inflammatory response, two hallmarks of retinal degenerative diseases. - Source: PubMed
Publication date: 2026/01/28
Echevarría María STenconi Paula EBermúdez VicenteCalandria Jorgelina MBazan Nicolas GMateos Melina V - 6-Cyanodopamine (6-CYD) is a novel endogenous catecholamine that is released from rat isolated vas deferens epithelium and regulates smooth muscle contractility. Here it was investigated whether 6-CYD is released from human epididymal vas deferens (HEVD) and its interaction with the classical catecholamines dopamine, noradrenaline, and adrenaline. Basal release of 6-CYD was quantified by liquid chromatography coupled to tandem mass spectrometry in the absence and presence of either the voltage-gated sodium channel blocker tetrodotoxin or the dual NADPH oxidase NOX inhibitor GKT137831. Concentration-response curves to dopamine, noradrenaline, and adrenaline were performed in the presence and absence of 6-CYD. Frequency-dependent electric-field stimulation (EFS) was conducted with and without pre-incubation with 6-CYD. The basal release of 6-CYD was decreased with pre-incubation with GKT137831 and unaffected by tetrodotoxin. Although 6-CYD itself (up to 100 μM) did not induce HEVD contractions, at 10 nM it remarkably potentiated the contractions induced by dopamine, noradrenaline, and EFS. At 100 nM, 6-CYD also potentiated the adrenaline-induced HEVD contractions. The potentiation of noradrenaline-induced contractions by 6-CYD was not observed in HEVD pre-treated with tetrodotoxin (1 μM). In separate experiments, HEVD strips also released 6-nitrodopamine (6-ND) that was significantly reduced by GKT137831 (1 μM). Co-incubation (30 min) with 6-CYD (100 pM) and 6-ND (100 pM) caused a significant leftward shift in the concentration-response curve to noradrenaline. The results indicate that epithelium 6-CYD is an endogenous mediator of HEVD contractility. Whether NADPH oxidases are involved in 6-CYD biosynthesis remains to be further investigated. - Source: PubMed
Publication date: 2025/11/04
Britto-Júnior JoséLuvizotto RodrigoJabbour SamiLima Antonio TiagoMiller Alex HenriqueMoraes Maria Elisabete APeterson Larryn WAntunes EdsonFregonesi AdrianoDe Nucci Gilberto - Functional neutrophil diversity is recognized as a driver of development, progression and resolution of disease. Recruited neutrophils are imprinted by biochemical, biophysical and mechanical stimuli of the encountered microenvironment, altering their genetic and phenotypic program. The functional implications of this reprogramming are of critical importance for devising strategies to modify neutrophil behavior. Oxidant production affects neutrophil responses, shapes the microenvironment and often determines disease outcome in inflammation, infection and cancer. Here we report neutrophil diversification at mucosal barriers in inflammatory and infectious disease, culminating in tissue and stimulus-dependent de novo expression of the NADPH oxidases NOX1, DUOX2, and DUOX1 in recruited neutrophils. In contrast to proinflammatory DUOX2, myeloid NOX1 ameliorated colonic inflammation, yet epithelial NOX1 increased neutrophil recruitment from the onset, with a similar response observed in pulmonary S. aureus infection. In contrast, neutrophil DUOX expression did not alter S. aureus disease progression but extended host survival in influenza A virus infection. Thus, at gut and lung barriers an expansion of neutrophil oxidases occurs that highlights proinflammatory and antimicrobial DUOX2 activity, while NOX1 function seems intricate with multiple inputs. Evaluation of these de novo expressed oxidases in other neutrophil-driven diseases will further uncover their contribution to host protection and pathogenesis. - Source: PubMed
Publication date: 2025/10/09
Singh Ashish KO'Mara MauriceDrieu La Rochelle JulieTherry NoemieD'Alessio AuroraBaugh JohnBarre Ramya SMatsumoto MisakiNogales AitorMartínez-Sobrido LuisKnaus Ulla G - Reactive oxygen species (ROS) are short-lived and act in a site-specific manner, underscoring the importance of identifying the subcellular localization of their sources. ROS-generating NADPH oxidases (NOX) regulate pancreatic beta cell (dys)function. However, their subcellular localization and cytokine-mediated regulation in these cells remain largely unknown. We characterized the expression, subcellular localization and time-dependent cytokine-induced regulation of NOX isoforms in beta cells. - Source: PubMed
Publication date: 2025/10/06
de Almeida Davidson CorreaVilas-Boas Eloisa AparecidaCoelho Ferreira Paulo HenriqueFerreira Sandra MaraCarpinelli Angelo RafaelOrtis Fernanda