ADAM17 ELISA kit
- Known as:
- ADAM17 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ADAM17-Ra
- 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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- Doxorubicin (Dox) is a potent first-line chemotherapeutic and widely administered against different types of cancer, but is associated with a myriad of side effects, including cancer/chemotherapy-associated thrombosis and drug-induced thrombocytopenia (DIT). Although we and others have reported Dox-induced platelet activation, the binding partner of Dox on platelets has not been previously explored. Here, we found human and mouse platelet aggregation triggered via C-Type Lectin-like Receptor-2 (CLEC-2) was obstructed by Dox, but aggregation induced by classical agonists like ADP, collagen/collagen-related peptide, or thrombin receptor-activating peptide 6 (TRAP6), was unaffected. By Isothermal Titration Calorimetry, we detected a high binding affinity between Dox and recombinant CLEC-2 at 4.2 ± 2.4 nM. Interestingly, we found significant GPIb⍺ shedding from human and mouse platelet surfaces following Dox treatment. Consistently, GPIb⍺ shedding was recapitulated following anti-CLEC-2 monoclonal antibody treatment. Using Piceatannol to selectively inhibit CLEC-2 intracellular signaling or the pan-Matrix Metalloproteinases (MMP) inhibitor GM6001 rescued GPIbα from both Dox and CLEC-2 mAb-induced shedding. Using GI254023X or GW280264X to specifically inhibit ADAM10 or ADAMs10/17, respectively, revealed inhibition of ADAM10/17, but not ADAM10 exclusively, prohibited GPIbα shedding. Collectively, this implicates the classical sheddase of GPIbα, ADAM17. Thus, we pinpointed CLEC-2 as a binding partner for Dox on platelets and a novel pathway of ADAM17-mediated GPIb⍺ shedding via CLEC-2. These data not only provide insights into a mechanism of Dox-induced platelet activation, thrombosis, and DIT, but also reveal putative precision therapeutic approaches for Dox-treated patients and nominate CLEC-2 inhibition as a means to regulate thrombotic disease and/or bleeding disorders. - Source: PubMed
Publication date: 2026/04/27
Rousseau ZackaryMa WenjingLong TianleSlavkovic SladjanaQiu XinLao XiaomeiWu Xun GraceJoshi KaishivZhu Yunqing AmeliaZhu GuenghengThu Kelsie LNi Heyu - ADAM17 (A disintegrin and metalloproteinase 17) contributes to angiotensin-converting enzyme (ACE) 2 shedding in response to angiotensin II-AT1 receptor signaling, potentially shifting the renin-angiotensin system toward its pressor arm. We investigated whether ACE inhibitor (ACEI) or AT1 receptor blocker (ARB) therapy modulates ADAM17 expression. - Source: PubMed
Publication date: 2026/04/27
Falcoff Nora LGuman Gabriela RSeguel Rolando FTabaj Gabriela CHonickman JonathanDaroca LucilaNuñez MyriamSalazar MartinParati GianfrancoGironacci Mariela M - SARS-CoV-2 infection extends beyond the respiratory tract, with the oral cavity emerging as a critical site of viral activity shaped by epithelial receptor expression, microbial interactions, and inflammatory status. Periodontal disease (PD), a chronic dysbiotic condition, may heighten susceptibility to SARS-CoV-2 through inflammation-driven upregulation of non-canonical viral entry pathways. In this study, we investigated genes in the phosphatidylserine (PS)-dependent pathway, including ADAM17, ATP11c, TIM1, TIM3, and TIM4, in gingival tissue, saliva, and oral keratinocytes to define how PD and SARS-CoV-2 coordinately modulate oral viral entry mechanisms. Prepandemic gingival biopsies revealed significant upregulation of all non-canonical receptors in inflamed tissue, indicating that PD alone establishes a permissive molecular environment for PS-mediated microbial entry. In a post-vaccination cohort, salivary expression of these receptors was markedly elevated in COVID-19-positive individuals with PD, accompanied by significantly increased salivary PS levels, suggesting synergistic effects of viral exposure and periodontal inflammation. co-infection of primary human oral keratinocytes with SARS-CoV-2 and periodontal pathogens ( , ) induced robust, synergistic activation of PS-dependent entry genes, particularly TIM family receptors. Together, these findings identify PS and its associated receptors as inflammation-responsive mediators that expand SARS-CoV-2 entry routes in the oral mucosa. This work highlights a mechanistic intersection between COVID-19 and periodontal disease, with implications for viral persistence, immune dysregulation, and long-term oral health outcomes. - Source: PubMed
Publication date: 2026/04/13
Valverde AraceliCapistrano KristelleNaqvi Raza AliElshourbagy SarahEtminan SodabehSandoval GloriaBambrilla MariaNares SalvadorShukla DeepakSchwartz JoelNaqvi Afsar - Tumour necrosis factor-α (TNF-α) is a central pro-inflammatory cytokine whose biogenesis, secretion, and signalling are tightly interconnected with cellular protein-quality control systems. Current evidence shows that TNF-α maturation, co-translational and post-modifications, ER-luminal folding and trimerisation, Golgi trafficking, and ectodomain shedding by ADAM17 are constrained by ER chaperones and ER-associated degradation (ERAD). Furthermore, TNF-α signalling reciprocally interfaces with the proteostasis network (PN) largely through inflammatory stress pathways such as NF-κB-dependent transcriptional control of chaperones, ubiquitin-proteasome components, and autophagy regulators. However, dysregulation of this bidirectional crosstalk mechanistically contributes to disease, including chronic inflammatory disorders, cancer, and degenerative diseases. In this study we provide a synthesis of the current literature on pathways related to protein homeostasis control that determines whether TNF-α exposure is adaptive or proteotoxic. We also discuss the translational implications this could have by including rational combinations of TNF-α targeted blockers with PN modulators (chemical chaperones, proteasome or autophagy modulators), which reduce the proteotoxic burden. Therefore, understanding the crosstalk between TNF-α signalling and components of the PN system promises new mechanistic insights and translational targets for TNF-α-driven diseases. - Source: PubMed
Publication date: 2026/04/25
Haidar BailasanPhilippe CélineChevet EricZahradník Jiří - LAG-3 is an inhibitory immune checkpoint implicated in T-cell dysfunction, but the significance of soluble LAG-3 (sLAG-3) in chronic hepatitis B (CHB) remains unclear. Whether checkpoint blockade can restore intrahepatic antiviral T-cell function during HBV antigen clearance also remains to be defined. - Source: PubMed
Publication date: 2026/04/22
Chen JingnaZu YingqiuJiang GeerFang ZhongYuan Zhenghong