Human Polyclonal VASP Ab
- Known as:
- Human Polyclonal VASP Antibody
- Catalog number:
- a0166
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- ABclonal
- Gene target:
- Human Polyclonal VASP
Related genes to: Human Polyclonal VASP Ab
- Gene:
- VASP NIH gene
- Name:
- vasodilator stimulated phosphoprotein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 1996-06-07
- Date modifiied:
- 2017-06-13
Related products to: Human Polyclonal VASP Ab
Related articles to: Human Polyclonal VASP Ab
- Hemin, which gets released during erythrocyte lysis, induces concentration-dependent platelet activation, aggregation, and thrombus formation as well as plasma membrane destruction and cytoskeleton reorganization. Classical platelet antagonists do not inhibit the plasma membrane destruction induced by high concentrations of hemin. Both cyclic guanosine monophosphate (cGMP) and adenosine 3':5' -cyclic monophosphate (cAMP) are key endogenous inhibitors of platelet activation. Thus, we investigated whether they inhibit hemin-induced plasma membrane destruction, both individually and in combination. In addition to standard platelet assays, we performed cGMP and cAMP ELISAs, immunoblot analysis of vasodilator-stimulated phosphoprotein (VASP) and immunofluorescence staining. We found that pharmacological modulation of these pathways via NO donors (DEA/NO), soluble guanylyl cyclase (sGC) stimulators (riociguat) or IP receptor agonists (PGE), and phosphodiesterase (PDE) inhibitors (PDE-5 inhibitor: sildenafil, PDE-3 inhibitor: ibudilast), phosphorylate the downstream vasodilator-stimulated phosphoprotein (VASP) and inhibit hemin-induced platelet activation and degranulation. In particular, synergistically modulation of cGMP and cAMP and the resulted phosphorylation of VASP at Ser239 and Ser157 significantly attenuates platelet aggregation and plasma membrane destruction induced by high concentrations of hemin. Further, the riociguat NO-induced cGMP synthesis was significantly reduced in the presence of hemin. In comparison, the PGE-induced cAMP synthesis was enhanced in the presence of hemin. In conclusion, high concentrations of hemin change the cGMP and cAMP synthesis induced by their associated stimulators, while promoting plasma membrane destruction, which can be significantly inhibited by the simultaneous administration of riociguat DEA/NO and PGE. - Source: PubMed
Publication date: 2026/07/23
Laspa ZoiRohlfing Anne-KatrinFischer MelinaKollotzek FerdinandCastor TatsianaBorst OliverSowa Pamela WeronikaSigle ManuelHarm TobiasGawaz Meinrad Paul - Antiplatelet drugs are a pillar in the treatment strategy to prevent ischemic events in cardiovascular patients. However, the action of existing therapies is nonuniform, and the causative mechanism for this variability remains poorly understood. The differences between the microRNA profiles of individuals have been suggested to impact platelet reactivity and treatment outcomes. microRNA-150 (miR-150) has been previously associated, in several clinical reports, with platelet function variability and cardiovascular events. Therefore, we initiated our analysis by examining the mechanistic role of miR‑150 in platelet function. We employed transgenic zebrafish larvae designed to specifically increase miR‑150 expression in thrombocytes. Laser-induced caudal vein injury in these animals resulted in a smaller thrombus and decreased thrombocyte accumulation. RNA sequencing of miR-150-overexpressing thrombocytes identified a downregulated transcript encoding microtubule associated serine/threonine kinase-like (mastl), a key regulator of P2Y12 receptor downstream signaling. Overnight treatment of the transgenic fish with clopidogrel, a P2Y12 inhibitor, showed decreased thrombus formation in the control, but not in miR-150-overexpressing animals. This phenotype was reversed by overexpressing mastl. Next, we utilized a VASP phosphorylation assay to show that MASTL deficiency partially protects human platelets from P2Y12 inhibition. Finally, using miRNA:mRNA interaction predictors and experimental assays, we identified MASTL-targeting miRNAs in humans - miR-17-‑5p and miR-106a-5p - which were significantly upregulated in a population of clopidogrel-resistant patients. Our studies therefore support a model in which miR-150 in zebrafish, and miR-17‑5p or miR-106a-5p in humans, modulates MASTL expression, which in turn alters VASP phosphorylation and platelet sensitivity to P2Y12 inhibition. - Source: PubMed
Publication date: 2026/07/20
Ciepla PaulinaFish Richard JNolli SéverineDunoyer-Geindre SylvieCharlon-Gay JuliaReny Jean-LucNeerman-Arbez MargueriteFontana Pierre - Platelets are anucleate cells that can be studied by benchtop flow cytometers and today there are several types of flow cytometric assays for platelets. Platelet structure studies in clinical flow cytometry mostly target rare congenital platelet glycoprotein deficiencies (e.g., Glanzmann-thrombasthenia, and Bernard-Soulier syndrome) that can be considered as the prototypes for platelet flow analysis, since the identification of complete or partial deficiency of these molecules provides the proper diagnosis. Another area of platelet flow cytometry is the detection of activated platelets. Mostly it means the gold standard platelet P-selectin assay or the investigation of PAC-1 binding-an assay where the activation dependent epitope of the GPIIb/IIIa receptor is investigated-but the measurement of platelet-leukocyte aggregates and microparticle analysis have gained increasing role. A unique platelet subtype is the subgroup designated as coated platelets that are formed by the simultaneous activation with collagen and thrombin. In clinical practice further functional assays are also informative tests: the monitoring of clopidogrel resistance by measuring the intracellular phosphorylated VASP and identifying heparin induced thrombocytopenia (HIT) by the use of patient plasma. The flow cytometric HIT test utilize the detection of phosphatidylserine expression on normal platelets or the formation of microparticles in the presence of the patient's plasma and therapeutic concentration of heparin, thus it seems reasonable to suggest it for the study of the functionality of the HIT antibodies. Nevertheless, there are also limitations to these assays as several of them require fresh samples, thus sample transport to specialized laboratories is not always feasible. - Source: PubMed
Publication date: 2026/07/17
Kappelmayer JánosGonda LénárdKrajcsir BálintDebreceni Ildikó Beke - Arterial thrombosis is driven by excessive platelet activation, in which the P2Y12 receptor is a key amplifier of ADP-dependent signaling and a clinically validated antiplatelet target. P2Y12-oriented computational screening may facilitate the discovery of structurally diverse compounds with antiplatelet activity and provide new starting points for antithrombotic intervention. - Source: PubMed
Publication date: 2026/07/15
Yuan HaitaoMeng PanpanZhao RuiXu ZifanWu ChenQiu YunLiu JiaqingWang LingnaZhang KaiqingWang ZhenOu YuxinLin QingZhang YiyueZhu Fangfang - Ginsenoside Rg1, a key bioactive component of Panax ginseng, is recognized for its cardiovascular protective effects, yet its role in modulating platelet activation under high shear stress remains incompletely understood. This study aimed to systematically evaluate the in vitro effects and underlying mechanisms of Rg1 on platelet aggregation under high shear stress using a microfluidic chip system. In this study, blood flow environments at venous (300 s), arterial (1500 s), and pathological arterial (5000 s) shear rates were simulated using microfluidic chips. The effects of Rg1 (0-1000 μM) on platelet aggregation and activation were assessed via fluorescence imaging, flow cytometry (measuring P-selectin and GP IIb/IIIa activation), and Western blot analysis of intracellular signaling pathways. Coagulation parameters (APTT, PT, TT) and blood compatibility were also evaluated. Our results showed that Rg1 concentration-dependently inhibited platelet aggregation across all tested shear rates, showing particularly pronounced suppression under high shear stress (5000 s). Mechanistically, Rg1 significantly reduced P-selectin expression and GP IIb/IIIa activation. Western blot analysis revealed that Rg1 exerted its antiplatelet effects primarily by suppressing the PI3K/AKT and ERK1/2 signaling pathways and enhancing VASP phosphorylation, while exhibiting limited direct inhibitory effects on the Syk/PLCγ2 pathway. Notably, Rg1 did not significantly alter standard coagulation parameters or cause hemolysis within the tested concentration range. In conclusion, ginsenoside Rg1 demonstrated potent concentration-dependent inhibition of platelet activation and aggregation under high shear stress in this in vitro study. Its mechanism involves the multi-target modulation of key intracellular signaling pathways (PI3K/AKT, ERK1/2, and PKG/VASP). Furthermore, Rg1 exhibited favorable blood compatibility without impairing coagulation function in vitro. These findings suggest that Rg1 is a promising candidate warranting further preclinical investigation for targeted intervention in arterial thrombosis, although its therapeutic efficacy and safety require validation in vivo. - Source: PubMed
Publication date: 2026/07/08
Ke Zhi-YinHuang Xiao-JingLiu Dan-NingGao Xue-MeiLiu Bei-ZhongLi Yuan