TY  - JOUR
A1  - Reinhard, Matthias
A1  - Halbrügge, Maria
A1  - Scheer, Ulrich
A1  - Wiegand, Christiane
A1  - Jockusch, Brigitte M.
A1  - Walter, Ulrich
T1  - The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
N2  - Vasoactive agents which elevate either cGMP or cAMP inhibit platelet activation by pathways sharing at least one component, the 46/50 kDa vasodilator-stimulated phosphoprotein (V ASP). V ASP is stoichiometrically phosphorylated by both cGMP-dependent and cAMPdependent protein kinases in intact human platelets, and its phosphorylation correlates very well with platelet inhibition caused by cGMP- and cAMP-elevating agents. Here we report that in human platelets spread on glass, V ASP is associated predominantly with the distal parts of radial micro filament bundles and with microfilaments outlining the periphery, whereas less V ASP is associated with a central microfilamentous ring. V ASP is also detectable in a variety of different cell types including fibroblasts and epithelial cells. In fibroblasts, V ASP is concentrated at focal contact areas, along microfilament bundles (stress fibres) in a punctate pattern, in the periphery of protruding lamellae, and is phosphorylated by cGMP- and cAMP-dependent protein kinases in response to appropriate stimuli. Evidence for the direct binding of V ASP to F -actin is also presented. The data demonstrate that V ASP is a novel phosphoprotein associated with actin filaments and focal contact areas, i.e. transmembrane junctions between microfilaments and the extracellular matrix.
KW  - cAMP / cGMP / cytoskeleton / phosphorylation / protein kinase
Y1  - 1992
UR  - https://opus.bibliothek.uni-wuerzburg.de/frontdoor/index/index/docId/3132
UR  - https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-34246
ER  -