Journal
BLOOD
Volume 123, Issue 5, Pages E1-E10Publisher
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2013-07-512384
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Funding
- Ministerium fur Innovation, Wissenschaft und Forschung des Landes Nordrhein-Westfalen
- Bundesministerium fur Bildung und Forschung [31P5800, 01E010003]
- Deutsche Forschungsgemeinschaft [SFB688/TPA2, SPP1335]
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One of the most important physiological platelet inhibitors is endothelium-derived prostacyclin which stimulates the platelet cyclic adenosine monophosphate/protein kinase A (cAMP/PKA)-signaling cascade and inhibits virtually all platelet-activating key mechanisms. Using quantitative mass spectrometry, we analyzed time-resolved phosphorylation patterns in human platelets after treatment with iloprost, a stable prostacyclin analog, for 0, 10, 30, and 60 seconds to characterize key mediators of platelet inhibition and activation in 3 independent biological replicates. We quantified over 2700 different phosphorylated peptides of which 360 were significantly regulated upon stimulation. This comprehensive and time-resolved analysis indicates that platelet inhibition is a multi-pronged process involving different kinases and phosphatases as well as many previously unanticipated proteins and pathways.
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