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Gene Review:

VASP - vasodilator-stimulated phosphoprotein

Bos taurus

This record was replaced with 514902.

Price, C.J. et al., Jonckheere, V. et al., Mingone, C.J. et al., David, V. et al., Laursen, B.E. et al., et al.

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Disease relevance of VASP

Cell components known to play a role in the actin-based motility of Listeria are VASP (vasodilatator-stimulated phosphoprotein), the multiprotein Arp2/3 complex and cofilin [1].

High impact information on VASP

The force-depressing actions of 0.1 mM ALA were associated with increased cGMP-associated vasodilator-stimulated phosphoprotein (VASP) phosphorylation and increased sGC activity in homogenates of BPA cultured with ALA [2].
Profilin II dimers bind the (GP5)3 peptide derived from VASP with an affinity of approximately 0.5 microM [3].
Since a Pro17 peptide-profilin II complex only partially restores actin polymerization, the glycine residues in the VASP peptide appear important [3].
Thrombin-induced platelet aggregation was inhibited by GEA 3175 in a cyclic GMP- and vasodilator-stimulated phosphoprotein (VASP)-phosphorylation-dependent manner [4].
In this study, we have expressed wild-type and mutant forms of VASP in endothelial cells to determine in what aspects of cytoskeletal behavior this protein participates [5].

Biological context of VASP

Both PDE3 and PDE4 inhibitors stimulated intracellular PKA activation as seen from phosphorylation of vasodilator-stimulated phosphoprotein (VASP) [6].
These data provide a mechanism whereby VASP can influence endothelial migration and organization during capillary formation and modulate vascular permeability via effects on endothelial cell contractility [5].

Anatomical context of VASP

Expression of wild-type VASP induces marked membrane ruffling and formation of prominent stress fibers in bovine aortic endothelial cells [5].
The ability of distinct subdomains within VASP to bind adhesion proteins and induce F-actin bundling in vivo suggests that this protein could function in the aggregation and tethering of actin filaments during the formation of endothelial cell-substrate and cell-cell contacts [5].

Associations of VASP with chemical compounds

Deletion of the proline-rich domain of VASP abolishes its ability to bind profilin but does not affect ruffling or stress fiber formation [5].

References

Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach. David, V., Gouin, E., Troys, M.V., Grogan, A., Segal, A.W., Ampe, C., Cossart, P. J. Cell. Sci. (1998) [Pubmed]
Protoporphyrin IX generation from delta-aminolevulinic acid elicits pulmonary artery relaxation and soluble guanylate cyclase activation. Mingone, C.J., Gupte, S.A., Chow, J.L., Ahmad, M., Abraham, N.G., Wolin, M.S. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
Dimerization of profilin II upon binding the (GP5)3 peptide from VASP overcomes the inhibition of actin nucleation by profilin II and thymosin beta4. Jonckheere, V., Lambrechts, A., Vandekerckhove, J., Ampe, C. FEBS Lett. (1999) [Pubmed]
Potential Protective Properties of a Stable, Slow-releasing Nitric Oxide Donor, GEA 3175, in the Lung. Laursen, B.E., Stankevicius, E., Pilegaard, H., Mulvany, M., Simonsen, U. Cardiovascular drug reviews (2006) [Pubmed]
Vasodilator-stimulated phosphoprotein is involved in stress-fiber and membrane ruffle formation in endothelial cells. Price, C.J., Brindle, N.P. Arterioscler. Thromb. Vasc. Biol. (2000) [Pubmed]
Inhibition of platelet-derived growth factor-induced mitogenesis by phosphodiesterase 3 inhibitors: role of protein kinase A in vascular smooth muscle cell mitogenesis. Osinski, M.T., Schrör, K. Biochem. Pharmacol. (2000) [Pubmed]

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