ADAM17 ELISA kit
- Known as:
- ADAM17 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ADAM17-Hu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- ADAM17 ELISA kit
Related genes to: ADAM17 ELISA kit
- Gene:
- ADAM17 NIH gene
- Name:
- ADAM metallopeptidase domain 17
- Previous symbol:
- TACE
- Synonyms:
- cSVP, CD156B
- Chromosome:
- 2p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-10
- Date modifiied:
- 2019-04-23
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- ADAM17, a transmembrane protease, catalyzes the release of soluble proinflammatory TNF-α, and its inhibition emerges as an attractive therapeutic strategy for treating TNF-α-driven chronic inflammatory diseases. Current small molecule ADAM17 inhibitors exhibit hepatotoxicity and limited efficacy, precluding FDA approval. Therefore, there is a strong demand for novel ADAM17 inhibitor drugs to block soluble TNF-α production in inflammatory diseases. Here, we hypothesized that fexofenadine, an oral H1 receptor antagonist and FDA-approved as an antihistamine, additionally binds and inhibits the catalytic activity of human ADAM17 through its geometric and electronic complementarity with ADAM17 active site determinants, thereby blocking soluble TNF-α release. We show that the unique architecture of human ADAM17's large L-shaped hydrophobic cavity consisting S1'/S3' subsites, shaped by ALA439 and LEU348, possesses optimal subsite complementarity to fexofenadine. The binding of fexofenadine to ADAM17 is driven by the orientation of its piperidine and diphenylmethanol groups within the S3' subsite by its conformationally adaptable hydroxybutyl inter-linker that traverses the polar tunnel between S1' and S3' pockets, and its carboxylate that bidentately chelates the histidine-triad-coordinated catalytic Zn in ADAM17 active site. Further, fexofenadine, at therapeutic antihistamine dose, inhibits ADAM17 catalytic activity and consequently suppresses TNF-α production in inflammatory-activated human monocytic cells. ADAM17 inhibition by fexofenadine reduces soluble TNF-α-driven endothelial barrier dysfunction comparably to the FDA-approved TNF-α-neutralizing biologic etanercept. These results identify fexofenadine as a novel ADAM17 inhibitor, suggesting its repurposing potential for TNF-driven chronic inflammatory diseases and inhibition of ADAM17-catalyzed release of TNF-α as a novel mechanism for fexofenadine's anti-inflammatory effects. - Source: PubMed
Publication date: 2026/05/10
Puthiyottil ShahidJose DeepthiKuriakose NishamolSkaria Tom - Severe cases of COVID-19 can result in acute respiratory distress syndrome, extensive lung damage, and long-term structural changes, particularly extracellular matrix (ECM) remodeling. ECM remodeling is characterized by excessive collagen deposition and imbalanced activity of enzymes, such as matrix metalloproteinases. Although immune and inflammatory pathways in patients with COVID-19 are well understood, the epigenetic and post-transcriptional regulation is not well understood. In this exploratory study, we examined DNA methylation and miRNA-mediated regulation in lung tissues from fatal cases of COVID-19. - Source: PubMed
Publication date: 2026/05/07
Cardoso Gabriela Casanida Cunha Regiane StafimMiniskiskosky GuilhermeMachado-Souza Cleberde Noronha Luciade Paula Caroline Busatta VazTuon Felipe Franciscode Souza Ramos Cavalieri Edneia Amancio - ADAM17, the major sheddase in mammalian cells, releases membrane-tethered EGFR ligands and inflammatory cytokines, and is a central regulator of cell signalling. The rhomboid pseudoproteases, iRhom1 and iRhom2, function as essential cofactors of ADAM17, controlling its maturation and activation. In contrast to the well-characterized iRhom2, the mechanism and regulation of its ubiquitously expressed paralog iRhom1 remain undefined. Here, we present a 2.5 angstrom cryo-EM structure of the full-length human iRhom1/ADAM17 complex, revealing a previously unrecognized sterol-binding pocket located between TMD2 and TMD5. Structure-guided mutagenesis and pharmacological perturbation of sterol binding demonstrate that sterol binding is required to stabilize the iRhom1/ADAM17 complex and sustain its shedding activity. Strikingly, this regulation is paralog-specific: iRhom2 precludes sterol binding and instead stabilizes ADAM17 through direct intramolecular interactions. Furthermore, two human iRhom1 variants associated with cardiac disease localize adjacent to the sterol-binding pocket and disrupt ADAM17 maturation and activity. Together, these findings uncover mechanistic divergence between iRhom paralogs and establish a sterol-binding pocket in iRhom1 as a critical determinant of ADAM17 stability, revealing a potential avenue for paralog-selective therapeutic targeting. - Source: PubMed
Publication date: 2026/05/01
Lu FangfangZhao HongtuDai YaxinLee Chia-HsuehFreeman Matthew - Angiotensin-converting enzyme 2 (ACE2) is a key regulator of the renin-angiotensin-aldosterone system (RAAS). It also acts as a receptor for SARS-CoV-2 and stabilises the B0AT1 amino acid transporter at the cell surface. Therefore, surface expression of ACE2 is crucial for these physiological processes. ACE2 is released as a soluble, catalytically active form, partly through ectodomain shedding. This process mainly involves the sheddases ADAM10 and ADAM17, but the exact regulatory mechanisms remain unclear. We assessed 11 naturally occurring single-point mutations in the ACE2 stalk region. Most variants showed significantly reduced release compared to wild-type (WT) ACE2; however, the single point mutations P734L and G726R significantly increased their release. ACE2_P734L also exhibits higher surface expression, directly increasing the surface levels of B0AT1. Despite B0AT1 and ACE2 forming a tight tetrameric complex, this did not affect ACE2 shedding. This suggests that complex formation does not restrict sheddase access. Overall, these data identify the ACE2 stalk region as a major determinant of shedding efficiency. Naturally occurring variants in this region can substantially affect the release of soluble ACE2, potentially contributing to interindividual differences that are relevant for pathophysiological processes. - Source: PubMed
Publication date: 2026/04/29
Wiersch FlorianLux ChristineVanderliek-Kox JuliaSchun KatharinaLudwig AndreasDüsterhöft Stefan - The persistence of latent HIV-1 reservoirs remains the primary barrier to a cure. Shock and kill strategies aim to reactivate these reservoirs and eliminate them via effector cells, such as Natural Killer (NK) cells. However, chronic infection leaves NK cells exhausted. In this study, we investigated the interplay between cytokine-mediated NK cell activation and antibody-dependent cellular cytotoxicity (ADCC) across diverse HIV-1 subtypes. We demonstrated that while cytokine stimulation enhanced natural cytotoxicity, it simultaneously induces shedding of the Fc receptor CD16 via the metalloproteinase enzyme ADAM17. However, restoring CD16 expression through ADAM17 inhibition (TAPI-1) did not improve ADCC, suggesting that CD16 surface levels in NK cells is not the only limiting factor. On the other hand, Fc-engineered broadly neutralizing antibodies (bNAbs) with increased CD16 affinity, in particular LPLIL and GASDALIE, significantly enhance ADCC across the six different HIV-1 subtypes, regardless of NK cells activation, CD16 downregulation or limited surface Envelope expression in CD4T cells. These findings suggest that enhancing receptor affinity of bNAbs can bypass viral immune evasion and NK cell exhaustion, supporting their potential incorporation into HIV cure strategies. - Source: PubMed
Publication date: 2026/04/29
Melo ClaudiaMurphy TeresaHolmberg Carissa SKelly MaeganMcMahon Elyse KLochner Jonathan SLynch Rebecca MBosque Alberto