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Human VASP Primary Antibody for IHC - ABIN967238
Zhao, Jiang, Kroll, Huber: A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization. in The EMBO journal 2001
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Human Polyclonal VASP Primary Antibody for IHC - ABIN967239
Kühnel, Jarchau, Wolf, Schlichting, Walter, Wittinghofer, Strelkov: The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. in Proceedings of the National Academy of Sciences of the United States of America 2004
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Human Polyclonal VASP Primary Antibody for IHC - ABIN967240
Wang, Lu, Jin, Udo, Kandel, de Vente, Walter, Lohmann, Hawkins, Antonova: Presynaptic and postsynaptic roles of NO, cGK, and RhoA in long-lasting potentiation and aggregation of synaptic proteins. in Neuron 2005
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Human VASP Primary Antibody for IHC - ABIN967237
Millard, Bompard, Heung, Dafforn, Scott, Machesky, Fütterer: Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. in The EMBO journal 2005
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Human Polyclonal VASP Primary Antibody for WB - ABIN546517
Zhuang, Nguyen, Chen, Gudi, Eigenthaler, Jarchau, Walter, Boss, Pilz: Vasodilator-stimulated phosphoprotein activation of serum-response element-dependent transcription occurs downstream of RhoA and is inhibited by cGMP-dependent protein kinase phosphorylation. in The Journal of biological chemistry 2004
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Human Polyclonal VASP Primary Antibody for IF, IHC - ABIN5663597
Zheng, Xiong, Wu, Chen, Chen, Fleming, Gao, Bi, Ge: Quantitative Proteomics Analysis Reveals Novel Insights into Mechanisms of Action of Long Noncoding RNA Hox Transcript Antisense Intergenic RNA (HOTAIR) in HeLa Cells. in Molecular & cellular proteomics : MCP 2015
Human Polyclonal VASP Primary Antibody for IHC, WB - ABIN6714285
Jung, Lee, Hwang, Lee, Seol, Kim, Lee, Kim, Kim, Park: Vaspin increases nitric oxide bioavailability through the reduction of asymmetric dimethylarginine in vascular endothelial cells. in PLoS ONE 2013
Human Monoclonal VASP Primary Antibody for FACS, IF - ABIN126907
Iyú, Glenn, White, Fox, Heptinstall: Adenosine derived from ADP can contribute to inhibition of platelet aggregation in the presence of a P2Y12 antagonist. in Arteriosclerosis, thrombosis, and vascular biology 2011
Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation.
Our results demonstrate a novel requirement for VASP and actin polymerization in maintaining lytic granule convergence during NK cell-mediated killing.
Study results demonstrated that TNFalpha decreased VASP expression by upregulating the expression of HIF1alpha to inhibit A549 cell proliferation and adhesion. Inhibition of transplanted tumor growth was associated with downregulation of VASP expression in nude mice. Bioinformatics analysis indicated that expression levels of VASP or HIF1alpha lead to differential outcomes of overall survival in lung carcinoma.
Silencing of stathmin-1 altered the expression, subcellular localization and phosphorylation status of VASP, which suggested that it might be associated with remodeling of the cell cytoskeleton in colorectal cancer metastasis.
VASP may be involved in the pathophysiology of bronchopulmonary dysplasia via dysregulation of actin binding proteins
VASP role in the actin filament elongation
Our results reveal a dual role of VASP in endothelial permeability. In addition to its well-documented function in barrier integrity, we show that S-nitrosylation of VASP contributes to the onset of endothelial permeability.
findings have uncovered a PKG/VASP signaling pathway in Vascular Smooth Muscle Cells as a key molecular mechanism underlying T3-induced vascular relaxation.
This study provides the first evidence of VASP manipulation by an intravacuolar bacterial pathogen
VASP silencing downregulated Migfilin, beta-catenin and uPA and impaired spheroid invasion.
VASP phosphorylation assay could be useful in studies aimed at investigating relations between clopidogrel active metabolite bioavailability and clinical events.
VASP, zyxin and TES are tension-dependent members of focal adherens junctions independent of the alpha-catenin-vinculin module.
Data show that the phosphorylation status of vasodilator-stimulated phosphoprotein (VASP) at serine S322 can be predictive for breast cancer progression to an aggressive phenotype.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Data show that tumor necrosis factor-alpha (TNF-alpha) increased A549 lung adenocarcinoma cell permeability by repressing vasodilator-stimulated phosphoprotein (VASP) expression through the activation of hypoxia inducible factor 1 alpha subunit (HIF-1alpha).
The authors demonstrate that vasodilator-stimulated phosphoprotein (VASP), which is critical for regulation of actin assembly, cell adhesion and motility, is a direct substrate of Yersinia pestis YpkA kinase activity.
Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary.
In clinical practice,LCR and CYP2C19 gene polymorphism should be assessed in NCIS patients receiving clopidogrel treatment.
VASP phosphorylation at Ser(157) mediates its localization at the membrane, but that VASP Ser(157) phosphorylation and membrane localization are not sufficient to activate its actin catalytic activity
PKA regulates VASP phosphorylation in Ras-transformed cells in a non-cell-autonomous manner.
Serine phosphorylation of vasodilator-stimulated phosphoprotein (VASP) regulates colon cancer cell survival and apoptosis.
VASP is a major regulator of leukocyte recruitment and polarization in postischemic revascularization and data support a novel role of VASP in chemokine receptor trafficking.
Myocardial ischemic preconditioning-induced VASP phosphorylation in platelets is a protective mechanism against the deleterious effects of ischemia.
VASP selectively mediate activated T-cell trafficking by promoting the diapedesis step of transendothelial migration in a alpha4 integrin-dependent manner.
We identified a phosphorylation-dependent mechanism that regulates selective recruitment of these effectors to Lamellipodin: Abl-mediated Lamellipodin phosphorylation promotes its association with both Scar/WAVE and Ena/VASP, whereas Src-dependent phosphorylation enhances binding to Scar/WAVE but not to Ena/VASP
Thus, unlike host proteins characterized in Shigella pathogenesis that promote bacterial spread, VASP and EVL function to limit it.
Data show that the hypoxia inducible factor 1 alpha subunit (HIF-1alpha) protein level in lung tissues increased significantly at four hours and eight hours, whereas the vasodilator-stimulated phosphoprotein (VASP) protein level decreased significantly.
Collectively, our studies highlighted that the CuB-induced actin aggregation and cofilin-actin rod formation was mediated via the Ga13/RhoA/PKA/VASP pathway.
Ena/VASP regulates mDia2-initiated filopodial morphology, dynamics, and function.
cancer cells reaching liver sinusoids induced up-regulation of VASP
Low VASP activation was associated with high fat diet (HFD). Effects of HFD on aortic inflammation and insulin resistance were recapitulated by VASP knockout, implying a role for VASP to constrain inflammatory signaling and maintain insulin sensitivity.
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy.
CDC42 activation inhibits this activity and promotes IRSp53-dependent recruitment and clustering of VASP to drive actin assembly.
VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation.
A VASP to Rac to soluble guanylyl cyclase negative feedback loop limited cGMP production, thereby regulating adipogenesis and energy homeostasis.
The results of this study suggested that that PI(3,4)P2, Lpd, and Ena/VASP are involved in the process movement of multipolar migrating cells.
study demonstrate that endothelial VASP holds significant importance for endothelial barrier properties during hypoxia
studies identified VASP and VASP phosphorylation as crucial target for future hepatoprotective strategies
Data indicate that VASP is a critical downstream mediator of the anti-inflammatory effects induced by the NO/cGMP pathway. Targeted deletion of VASP predisposes to Kupffer cell inflammation.
phosphorylation of VASP by AMPK occurs at a novel site, serine 322, and phosphorylation at this site alters actin filament binding.
VASP binding to actin, elevated Rac activity, and elevated formation of actin free barbed ends, thus restoring normal beta(2) integrin function.
Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.
, Vasodilator-stimulated phosphoprotein