Abstract:
:p38 MAP kinase in human platelets is activated by platelet agonists including thrombin, thromboxane A2 (TxA2), ADP, and others. However, both upstream mechanisms of p38 MAP kinase activation, and their downstream sequelae, are presently controversial and essentially unclear. Certain studies report sequential activation of cGMP-dependent protein kinase (PKG) and p38/ERK pathways by platelet agonists, leading to integrin activation and secretion, whereas others establish an essential role of Src/ERK-mediated TxA2 generation for fibrinogen receptor activation in human platelets. Here, we show that ADP secreted from platelet-dense granules, and subsequent activation of P2Y12 receptors, as well as TxA2 release are important upstream mediators of p38 MAP kinase activation by thrombin. However, p38 MAP kinase activation did not significantly contribute to calcium mobilization, P-selectin expression, alphaIIbbeta3 integrin activation, and aggregation of human platelets in response to thrombin. Finally, PKG activation did not stimulate, but rather inhibited, p38 MAP kinase in human platelets.
journal_name
Bloodjournal_title
Bloodauthors
Begonja AJ,Geiger J,Rukoyatkina N,Rauchfuss S,Gambaryan S,Walter Udoi
10.1182/blood-2006-07-038158subject
Has Abstractpub_date
2007-01-15 00:00:00pages
616-8issue
2eissn
0006-4971issn
1528-0020pii
blood-2006-07-038158journal_volume
109pub_type
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