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J. Biol. Chem., Vol. 265, Issue 6, 3088-3093, Feb, 1990
M Halbrugge, C Friedrich, M Eigenthaler, P Schanzenbacher and U Walter
Recently, we reported the purification of a 46-kDa membrane-associated
platelet protein which is phosphorylated in intact platelets and platelet
membranes by cGMP- and cAMP-dependent protein kinases (Halbrugge, M., and
Walter, U. (1989) Eur. J. Biochem. 185, 41-50). Here we demonstrate that
both cGMP- and cAMP-dependent protein kinases catalyze the rapid
incorporation of up to 1.4 mol of phosphate/mol of this purified
vasodilator-stimulated phosphoprotein (VASP). A specific rabbit antiserum
was prepared which recognized both the 46-kDa dephospho form and the 50-kDa
phospho form of VASP in Western blots. In untreated washed platelets, VASP
was found to be present primarily as a 46-kDa dephosphoprotein. Sodium
nitroprusside (100 microM) raised the intracellular platelet cGMP
concentration from approximately 0.44 to 4.1 microM, without a significant
effect on the cAMP level, and converted up to 50% of VASP to the 50-kDa
phospho form. Prostaglandin E1 (10 microM) raised the platelet cAMP
concentration from approximately 4.4 to 28.4 microM, without a significant
effect on the cGMP level, and shifted up to 67% of VASP to the 50-kDa
phospho form. Removal of the vasodilators sodium nitroprusside and
prostaglandin E1 from the platelet suspension was followed by a return of
the cyclic nucleotide concentration to basal levels and subsequent
conversion of the 50-kDa phospho form of VASP to the 46-kDa dephospho form.
The results support the hypothesis that VASP phosphorylation is an
important component of the intracellular mechanism of action of these
vasodilators in human platelets.
Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators
Medizinische Universitatsklinik, Labor fur Klinische Biochemie, Wurzburg, Federal Republic of Germany.
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D. W. Lawrence, K. M. Comerford, and S. P. Colgan Role of VASP in reestablishment of epithelial tight junction assembly after Ca2+ switch Am J Physiol Cell Physiol, June 1, 2002; 282(6): C1235 - C1245. [Abstract] [Full Text] [PDF]
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