Phosphorylation of rap1B by protein kinase A is not involved in platelet inhibition by cyclic AMP.
Cell Signal
; 5(2): 209-14, 1993 Mar.
Article
em En
| MEDLINE
| ID: mdl-7684600
ABSTRACT
The functional consequence of cyclic AMP-dependent phosphorylation of rap1B for stimulus-induced platelet activation is not known. Platelets were pretreated with the stable prostacyclin-analogue iloprost and resuspended in plasma without iloprost. Western blot analysis showed that rap1B was completely converted into its phosphorylated form in the iloprost-pretreated platelets. Surprisingly, the platelets that contained phosphorylated rap1B were found to respond fully to activation by a wide variety of stimuli aggregation upon stimulation by collagen, phorbol ester, vasopressin, ADP, epinephrine, and ATP-secretion from dense granules induced by collagen, thrombin-receptor activating peptide, vasopressin and phorbol ester were unchanged as compared to control. The results indicate that cyclic AMP-dependent phosphorylation of rap1B does not play a role in the inhibition of the various signal transduction pathways that lead to platelet aggregation and dense granule secretion.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Inibidores da Agregação Plaquetária
/
Ativação Plaquetária
/
AMP Cíclico
/
Proteínas de Ligação ao GTP
/
Proteínas rab1 de Ligação ao GTP
Limite:
Humans
Idioma:
En
Revista:
Cell Signal
Ano de publicação:
1993
Tipo de documento:
Article