Ask about this productRelated genes to: DPP3 antibody
- Gene:
- DPP3 NIH gene
- Name:
- dipeptidyl peptidase 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-25
- Date modifiied:
- 2016-02-05
Related products to: DPP3 antibody
Related articles to: DPP3 antibody
- Norepinephrine remains first-line vasopressor therapy for septic shock despite its association at high doses with undesirable cardiovascular, kidney, and immune effects. Angiotensin-II (Ang-II) is a non-catecholamine vasopressor of the renin-angiotensin-aldosterone system (RAAS) now approved to increase blood pressure in vasodilatory shock. RAAS dysregulation is common in septic shock and may represent a treatable trait. However, few prospective investigations evaluate the effect of early Ang-II use in septic shock on dysfunctional RAAS biology, host-response, or clinical outcomes. Therefore, we designed a mechanistic clinical trial to test the hypothesis that early Ang-II therapy in septic shock normalizes systemic RAAS abnormalities and modulates innate immune responses. - Source: PubMed
Publication date: 2026/09/14
Filbin Michael RLeisman Daniel EPachano-Bravo AnaGoldberg Marcia BHibbert KathrynNelson OliviaRappaport BenjaminMahler Simon AHarris LynnetteBesong Estelle BReeves BrandonMaves Ryan CPetrilli AndrewSchaich Christopher LFiles D ClarkGibbs KevinChappell Mark CKhanna Ashish K - Venovenous extracorporeal membrane oxygenation (VV ECMO) is a life‑saving intervention commonly used for severe and refractory respiratory failure. However, patient management and outcomes in this setting remain challenging as well as difficult to predict. Inflammatory reaction, namely by assessing cytokine and chemokine blood levels, may provide prognostic information, but their role in VV ECMO has not been comprehensively characterized. - Source: PubMed
Publication date: 2026/09/17
Hagiwara JunyaLiu QianqianDellaVolpe Jeffrey DDay JonathanMichalek JoelLorusso RobertoCombes AlainSousse Linda E - Dipeptidyl peptidase 3 (DPP3) is a ubiquitously expressed zinc-exopeptidase involved in oligopeptide degradation. Beyond its catalytic role, DPP3 exhibits a moonlighting role in the Keap1-Nrf2 signalling pathway, where it promotes Nrf2-dependent gene transcription through an ETGE motif-mediated interaction with the Kelch domain of Keap1. This highlights its role in oxidative stress and cancer, as persistent pathway activation supports tumour cell survival, oxidative stress resistance, and proliferation. While DPP3's catalytic activity is not required for Keap1 binding, the effects of enzyme inactivation on this interaction, and , remain unclear. Using isothermal titration calorimetry and molecular dynamics simulations, we show that DPP3 inactivation, mutation (E451A) or inhibitor binding, enhances DPP3-Keap1 complex formation by facilitating detachment of the ETGE-loop in the closed enzyme conformation, a rate-limiting step in complex assembly. Kinetic measurements further reveal that Keap1 binding modulates DPP3 catalytic activity, increasing efficiency through disproportional reductions in both and , likely by stabilizing the closed, catalytically competent conformation of the enzyme, which favours substrate binding but hinders the turnover of reaction participants. These findings reveal a bidirectional regulatory mechanism: catalytic inhibitor binding promotes moonlighting interactions with Keap1, while Keap1 binding enhances enzymatic activity. This dual regulation provides insight into how modulation of DPP3's catalytic function could influence Keap1-Nrf2 redox signaling and suggests how cancer cells might exploit multifunctional enzymes like DPP3 to support tumour progression. This hypothesis based on biochemical and computational data remains to be validated in models. - Source: PubMed
Publication date: 2026/09/14
Matić AntoniaŠupljika FilipPetohleb LukaTomašić Paić AnaKindl Domagoj CHorvat GordanBarbarić LeaOskomić MarinaMatovina MihaelaTomić Antonija - The non-canonical inflammasome is a protein complex involved in bacterial infections, and its activation leads to excessive inflammatory responses during sepsis. The precise regulation of the non-canonical inflammasome in the body remains unclear. Here, we found that some chemicals that chelate zinc ions positively regulated the activation of the non-canonical inflammasome. These chemicals acted by inhibiting the activity of dipeptidyl peptidase 3 (DPP3). DPP3 cleaved phosphatidylethanolamine binding protein 1 (PEBP1) to generate an N-terminal fragment, which could bind to caspase-4/11 and inhibit the response intensity of the non-canonical inflammasome. PEBP1 N terminus appeared in the serum of mice and patients with sepsis. DPP3-deficient mice exhibited stronger inflammatory cytokine responses and had poor survival in the LPS-induced sepsis model. Promoting the activity of DPP3 effectively constrained the response intensity of sepsis in mice and increased their survival. Our findings provide a perspective for understanding the molecular regulatory process of the non-canonical inflammasome in sepsis. - Source: PubMed
Publication date: 2026/09/09
Li MengqianZheng JiajiaKong ChunGeng XiangyangSun XiuliShen NingWang ShuoXia Pengyan - Angiotensin-(1-7) promotes vasodilation and counteracts angiotensin II in the vasculature and kidneys, while dipeptidyl peptidase 3 (DPP3) inactivates Ang-(1-7). Although circulating DPP3 (cDPP3) has been studied in chronic heart failure (HF), data in acute HF are limited. We evaluated cDPP3 levels and their association with clinical characteristics, decongestive response, and outcomes in acute HF. - Source: PubMed
Publication date: 2026/09/04
Legtenberg StijnSantos KarineBeldhuis Iris EHartmann OliverZonneveld Lara E E Cvan der Meer PeterKrikken Jan ANieuwland Wybevan Veldhuisen Dirk JVoors Adriaan ADamman KevinTer Maaten Jozine M