Synergistic phosphorylation of platelet rap1B by SIN-1 and iloprost.
Eur J Pharmacol
; 288(3): 329-33, 1995 Feb 15.
Article
em En
| MEDLINE
| ID: mdl-7539769
ABSTRACT
Human platelets suspended in plasma or buffer were incubated with low concentrations of the nitric oxide (NO)-donor 3-morpholino-syndnonime (SIN-1; 100 nM to 1 microM) and the stable prostacyclin analogue iloprost (50 or 100 pM) and analyzed for cyclic nucleotide levels and protein phosphorylation. SIN-1 and iloprost synergistically stimulated the phosphorylation of rap1B and the 50 kDa vasodilator-stimulated phosphoprotein. SIN-1 stimulated platelet cyclic GMP and cAMP-levels and enhanced the increase in cyclic AMP elicited by iloprost. It was found that the mechanism underlying the synergistic phosphorylation of the 50 kDa protein and rap1B was different synergistic phosphorylation of the 50 kDa protein seemed to be mediated by activation of both protein kinases A and G, whereas the synergistic rap1B phosphorylation could be attributed entirely to activation of protein kinase A. Measurement of rap1B phosphorylation might be a useful tool to monitor the action of systemically applied prostacyclin-analogues and nitrovasodilators in pharmacological studies.
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Base de dados:
MEDLINE
Assunto principal:
Plaquetas
/
Molsidomina
/
Inibidores da Agregação Plaquetária
/
Iloprosta
/
Proteínas de Ligação ao GTP
Limite:
Humans
Idioma:
En
Revista:
Eur J Pharmacol
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Alemanha