Phosphorylation of rap1B by protein kinase A is not involved in platelet inhibition by cyclic AMP.

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.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Siess W,Grünberg B

doi

10.1016/0898-6568(93)90071-s

subject

Has Abstract

pub_date

1993-03-01 00:00:00

pages

209-14

issue

2

eissn

0898-6568

issn

1873-3913

pii

0898-6568(93)90071-S

journal_volume

5

pub_type

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