ADA17_HUMAN TACE ELISA tesk kit
- Known as:
- ADA17_HUMAN TACE Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen16978
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- ADA17_HUMAN TACE ELISA tesk kit
Related genes to: ADA17_HUMAN TACE ELISA tesk 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
Related products to: ADA17_HUMAN TACE ELISA tesk kit
Related articles to: ADA17_HUMAN TACE ELISA tesk kit
- A healthy cardiovascular system requires a healthy endothelium. The endothelium is a central regulator of hemostasis, vascular permeability, inflammation, blood pressure, and, perhaps most fundamentally, blood flow. It is therefore of no surprise that endothelial dysfunction underlies many of the vascular complications that occur in metabolic disease (e.g. peripheral artery disease, vascular retinopathy, and coronary artery disease). Endothelial function is often assessed using flow mediated dilation (FMD), and in their recent study, Power and colleagues provide novel insight into the mechanisms by which FMD is impaired in type 2 diabetes (T2D). In T2D, loss of FMD is driven, in part, by the shedding of the glycocalyx (). This hair-like structure on the surface of the endothelium maintains an erythrocyte-free zone, preserves redox homeostasis, mitigates inflammation, and senses shear stress. The glycocalyx is a complex matrix made up of proteoglycans, glycoproteins, glycolipids, and glycosaminoglycans, and each of these components plays an essential role in its functions. Power and colleagues found patients with T2D had impaired FMD and elevated plasma hyaluronan, suggesting glycocalyx shedding. Hyaluronan is a glycosaminoglycan in the glycocalyx that works in concert with CD44 to propagate flow-induced signaling. Notably, they found endothelial CD44 expression was decreased in the db/db model of T2D. Using isolated mouse mesenteric arteries, they demonstrated cleavage of hyaluronan with hyaluronidase or blocking the binding site of hyaluronan on CD44 blunted FMD. Similarly, knockdown of CD44 in cultured endothelial cells blunted shear stress induced increases in intracellular calcium and endothelial nitric oxide synthase. Together these data demonstrate the importance of hyaluronan-CD44 signaling for endothelial mechanotransduction. Building on their previous work which reported upregulation of a disintegrin and metalloprotease 17 (ADAM17) in arteries from patients with T2D, they found elevated plasma ADAM17 activity in their patient population and increased endothelial ADAM17 expression in db/db mice. They therefore investigated whether cleavage of CD44 by ADAM17 contributes to impaired FMD in T2D. They found both activation and overexpression of ADAM17 blunted the response to shear stress in cultured endothelial cells. Furthermore, ADAM17 overexpression cleaved CD44 as demonstrated by reduced cell-surface CD44 and increased CD44 in the supernatant. Similar results were achieved when endothelial cells were treated with recombinant ADAM17, and recombinant ADAM17 was sufficient to impair CD44-hyaluronan binding . Perhaps most importantly, recombinant ADAM17 was sufficient to blunt FMD in isolated mouse mesenteric arteries. Altogether these data suggest ADAM17 upregulation contributes to the endothelial dysfunction observed in patients with T2D. These studies build on previous work implicating ADAM17 as a driver of endothelial dysfunction in metabolic disease and provide a novel mechanism by which ADAM17 impairs endothelial-dependent vasodilation. Previous work has demonstrated ADAM17 cleaves glypican-1, a proteoglycan component of the glycocalyx, thereby blunting FMD, and ADAM17 cleaves the insulin receptor, blunting insulin-dependent vasodilation. Still questions remain regarding how ADAM17 activity impacts other functions of the glycocalyx and how other flow-sensing mechanisms such as piezo channels may compensate in these conditions. The use of endothelial-specific ADAM17 knockout mice offers an exciting avenue to pursue these questions . Altogether, ADAM17 may be a promising target to preserve or restore the endothelial glycocalyx and endothelial function in T2D. Vascular dysfunction gives rise to major T2D comorbidities such as nephropathy, neuropathy, and cardiovascular disease. Continued efforts to investigate the mechanisms that drive endothelial dysfunction may offer new therapeutic targets to treat or prevent these comorbidities, thereby decreasing mortality and improving quality of life for patients with T2D. - Source: PubMed
Publication date: 2026/06/05
Dunaway Luke S - Iron homeostasis is a tightly regulated mechanism, wherein the uptake, transport, storage and export of iron are stringently controlled. Dysregulation and excessive iron uptake lead to iron-dependent programmed cell death called ferroptosis, a promising future cancer therapy target. Cellular iron uptake is limited by the surface presence of membrane-bound transferrin receptor 1 (TfR1). Soluble TfR1 is used as a major clinical marker to differentiate anemia types. Here we identify iRhoms, the regulatory interactors of the surface protease ADAM17, as substrate platforms. They bind TfR1 and facilitate ADAM17-mediated proteolytic TfR1 release (TfR1 shedding). Thereby, the iRhom-ADAM17 complex regulates TfR1 surface levels. Notably, TfR1 preferentially binds to pro-inflammatory iRhom2 over iRhom1, with the cytosolic N terminus of iRhom serving as a critical binding determinant. By CRISPR-Cas9-based knockout and pharmacological inhibition in vitro, in human primary endothelial cells as well as in ex vivo human lung slices, we also demonstrate that TfR1 is a shared substrate of ADAM10 and ADAM17. Functionally, we found that ADAM17-dependent TfR1 shedding reduces excessive iron uptake. By live cell imaging, we identified TfR1 shedding as a protective mechanism against ferroptosis. Moreover, reduced TfR1 shedding correlaśtes with elevated serum iron levels in ADAM17-hypomorphic mice, highlighting its systemic relevance for patho(physiological) iron homeostasis. iRhom-ADAM17 complex and ADAM10-shed TfR1. Cellular iron uptake is facilitated by TfR1. TfR1 interacts with the substrate platform iRhom, which is a regulator of the protease ADAM17. The iRhom-ADAM17 complex and ADAM10 cleave TfR1, thereby releasing soluble TfR1. By this, iron overloaded is prevented. Therefore, ectodomain shedding of TfR1 is a protective mechanism to hinder ferroptosis. - Source: PubMed
Publication date: 2026/06/04
Schun KatharinaRinkens CindyMehling DanielYu YanKnapp SarahPeschke CarolinSonnabend FriederikeLux ChristinePabst AlessaCharlier LauraSchumacher NeeleBabendreyer AaronLudwig AndreasDüsterhöft Stefan - Hypertensive intracerebral hemorrhage (ICH) is a devastating stroke subtype with high mortality and disability, yet reliable early risk biomarkers remain elusive. This study integrated protein microarray and transcriptomics with machine learning to identify a 4-gene panel (ADAM17, TMPRSS5, PLAU, and ADAMTS13). A LightGBM model with Nested Cross-Validation demonstrated robust discriminative power, achieving AUCs of 0.94 and 0.89 in independent validation cohorts for distinguishing ICH from hypertension and ischemic stroke, respectively. SHAP analysis identified PLAU as the most influential predictor, validated by RT-qPCR and ELISA in an independent replication cohort. Notably, prospective evaluation and animal models revealed a significant PLAU surge prior to vascular rupture. Functional inhibition of PLAU using UK122 significantly delayed ICH onset in hypertensive mice, independent of blood pressure. Furthermore, GSEA and immune infiltration analysis revealed specific enrichment of the Nod-like receptor signaling pathway and a uniquely proinflammatory microenvironment (activated dendritic cells and neutrophils) in ICH. - Source: PubMed
Publication date: 2026/05/30
Gao ZiyuLiu JingSun YingyingBai CongxiaYang HaitaoXu HaochenLi HaoSong LiSuo MiaomiaoChen Jingzhou - Autism spectrum disorder (ASD) is characterized by deficits in social communication and restricted/repetitive behaviors, yet the molecular mechanisms by which prenatal environmental insults lead to circuit dysfunction remain incompletely understood. Neuregulin 1 (NRG1)-ErbB4 signaling is a key regulator of synaptic development and excitation-inhibition (E/I) balance, but whether altered NRG1 processing contributes to ASD-related phenotypes remains unclear. Here, using a prenatal valproic acid (VPA) rat model, we examined the relationship between NRG1 processing, synaptic integrity, and behavioral outcomes. Prenatal VPA exposure reduced cleaved NRG1 protein without altering transcript levels and was accompanied by decreased expression of the NRG1 sheddases ADAM10, ADAM17, and BACE1. These alterations were accompanied by attenuated ErbB4-AKT/ERK1/2 signaling, reduced synaptic scaffolding proteins, and impaired dendritic spine maturation in the hippocampus. Behaviorally, VPA-exposed offspring exhibited abnormalities across multiple ASD-relevant domains. Recombinant NRG1β1 administration during adolescence improved repetitive behaviors in both sexes, whereas deficits and rescue effects in social and sensorimotor domains were primarily observed in males. As robust social deficits were not evident in females, subsequent molecular and synaptic analyses were conducted in male hippocampus, where NRG1 restored ErbB4 signaling, synaptic organization, and spine maturity without affecting locomotor activity. Collectively, these findings indicate that altered NRG1 processing is associated with synaptic and behavioral abnormalities in the VPA model. Enhancement of NRG1-ErbB4 signaling modulates these phenotypes, supporting a functionally relevant role of this pathway in ASD-related neurodevelopmental alterations. - Source: PubMed
Publication date: 2026/05/18
Kim Yu-JinKim Han-ByeolLim Hyo-MinChoi YooriWoo Ran-Sook - Colchicine is a microtubule-targeting anti-inflammatory agent with emerging relevance in cardiovascular disease; however, its effects on injury-induced vascular remodeling remain incompletely defined. In this study, a rat iliac artery clamp injury model was used to evaluate the effects of colchicine (0.5 mg/kg/day, oral gavage) over 28 days. Histomorphometric, histopathological, and immunohistochemical analyses were performed to assess vascular remodeling. In parallel, molecular docking and STRING/Cytoscape-based protein-protein interaction (PPI) network analyses were conducted to provide structural and systems-level context. Colchicine significantly reduced intimal thickness, the intima-to-media (I/M) ratio, luminal stenosis, adventitial thickness, and collagen deposition, while preserving the lumen area and improving the remodeling index. Medial thickness was not significantly affected. Proliferative activity showed a decreasing trend without statistical significance. Circulating inflammatory cytokines, including TNF-α and IL-1β, did not differ significantly between groups. Docking analyses suggested potential interactions with β-tubulin, ADAM17, NLRP3, IKKβ, and RELA, while network analysis identified an interaction architecture centered on NF-κB-related regulatory components and inflammasome-associated signaling pathways. Colchicine attenuates injury-induced vascular remodeling in this experimental model. These findings, together with complementary in silico analyses, suggest a multi-target, inflammation-associated framework involving NF-κB-related and inflammasome-linked pathways. The in silico analyses provide supportive mechanistic context but do not establish causal relationships. - Source: PubMed
Publication date: 2026/04/28
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