Vasodilator-stimulated phosphoprotein

The VASP ( vasodilator - Paced phosphoprotein ) is an actin -binding regulatory protein (protein ), and the substrate of the cGMP-dependent protein kinase. In the phosphorylated form, it is also P- VASP called. It belongs to the Ena / VASP proteins, which also include Ena VASP and EVL next. These play in cancer research and cell research a role as they are involved in the processes of cell adhesion ( bond between cells) and the cytoskeleton (internal cellular " scaffolding ").

Platelets and other cells of the blood vessels contain particularly high concentrations of VASP, but ultimately it is detectable in almost all cells. VASP is phosphorylated at three points. Current results corroborate the assumption that VASP inhibits platelet activation and aggregation and networking of the adhesion molecule glycoprotein IIb -IIIa. These effects are exacerbated by the phosphorylation of VASP.

Discovery

The scientists F. Murad and L. Ignarro discovered that the neurotransmitter nitric oxide ( NO) and NO itself containing cardiovascular drugs stimulate the formation of the signaling molecule cGMP and inhibit platelet of man. While searching for proteins that are phosphorylated in platelets after treatment with NO -containing substances ( depending on the signal molecule cGMP), scientists found in 1987, the protein VASP.

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