Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 15, Issue 11, Pages 3461-3472Publisher
ELSEVIER
DOI: 10.1074/mcp.M116.059154
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Funding
- Multi-omics Research Program [NRF-2012M3A9B9036675]
- Institute for Basic Science [IBS-R013-G1-2015-a00]
- Korean Ministry of Science, ICT AMP
- Future Planning [NRF-2014M3C7A1046047]
- Korea Health Industry Development Institute - Ministry of Health AMP
- Welfare, Republic of Korea [HI13C2098]
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Sarpogrelate is an antiplatelet agent widely used to treat arterial occlusive diseases. Evaluation of platelet aggregation is essential to monitor therapeutic effects of sarpogrelate. Currently, no molecular signatures are available to evaluate platelet aggregation. Here, we performed comprehensive proteome profiling of platelets collected from 18 subjects before and after sarpogrelate administration using LC-MS/MS analysis coupled with extensive fractionation. Of 5423 proteins detected, we identified 499 proteins affected by sarpogrelate and found that they strongly represented cellular processes related to platelet activation and aggregation, including cell activation, coagulation, and vesicle-mediated transports. Based on the network model of the proteins involved in these processes, we selected three proteins (cut-like homeobox 1; coagulation factor XIII, B polypeptide; and peptidylprolyl isomerase D) that reflect the platelet aggregation-related processes after confirming their alterations by sarpogrelate in independent samples using Western blotting. Our proteomic approach provided a protein profile predictive of therapeutic effects of sarpogrelate.
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