Vasodilator-stimulated phosphoprotein
| Vasodilator-stimulated phosphoprotein | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 379 amino acids | |
| Precursor | Homotetramer | |
| Identifier | ||
| Gene name | VASP | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Mammals | |
The VASP ( VA sodilatator- S timuliertes P hosphoprotein) is a regulatory actin -binding protein and substrate of cGMP -dependent protein kinase . In the phosphorylated form it is also called P-VASP. It belongs to the group of Ena / VASP proteins, which in addition to VASP also include Ena and EVL. These play a role in cancer research and cell research , as they are involved in the processes of cell adhesion and the cytoskeleton .
Platelets and other cells in the blood vessels contain particularly high levels of VASP, but ultimately it is detectable in almost all cells. VASP can be phosphorylated in three places. Current results support the assumption that VASP inhibits the activation of blood platelets and the aggregation and crosslinking of the adhesion molecule glycoprotein IIb-IIIa. These effects are amplified by the phosphorylation of VASP.
discovery
The scientists F. Murad and L. Ignarro discovered that the neurotransmitter nitrogen monoxide (NO) itself and cardiovascular drugs containing NO stimulate the formation of the signaling molecule cGMP and inhibit human platelets . While looking for proteins that are phosphorylated in the blood platelets after treatment with substances containing NO (depending on the signaling molecule cGMP), scientists found the protein VASP in 1987.
Individual evidence
Web links
- M. Krause: The Ena / VASP enigma. In: J Cell Sci. 115, 2002, pp. 4721-4726. doi: 10.1242 / jcs.00218