Abstract:
:Several protein kinase C (PKC) isoforms are expressed in human platelets. We report that PKC-delta is tyrosine phosphorylated within 30 s of platelet activation by thrombin. This correlated with a 2-3-fold increase in the kinase activity of PKC-delta relative to unstimulated platelets. The tyrosine phosphorylated PKC-delta isoform was associated with the platelet particulate (100,000 x g insoluble) fraction. Alpha(IIb)beta3 integrin mediated platelet adhesion to fibrinogen did not significantly affect PKC-delta activity. Tyrosine phosphorylation of PKC-delta was similarly not detected in fibrinogen adherent platelet lysates. Treatment of the platelets with mAb 7E3 prior to the addition of thrombin blocked aggregation having no effect on the thrombin induced PKC-delta activation. We conclude that PKC-delta is activated in platelets by an alpha(IIb)beta3 independent pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Moussazadeh M,Haimovich Bdoi
10.1016/s0014-5793(98)01302-7subject
Has Abstractpub_date
1998-11-06 00:00:00pages
225-30issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01302-7journal_volume
438pub_type
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