Platelets are small anucleated blood particles that play a key role in the control of bleeding. Platelets need to be activated to perform their functions and participate in hemostasis. The process of activation is accompanied by vast protein reorganization and posttranslational modifications. The goal of this study was to identify changes in proteins in platelets activated by different agonists. Platelets were activated by three different agonists - arachidonic acid, collagen, and thrombin. 2D SDS-PAGE (pI 4-7) was used to separate platelet proteins. Proteomes of activated and resting platelets were compared with each other by Progenesis SameSpots statistical software; and proteins were identified by nanoLC-MS/MS. 190 spots were found to be significantly different. Of these, 180 spots were successfully identified and correspond to 144 different proteins. Five proteins were found that had not previously been identified in platelets: protein CDV3 homolog, protein ETHE1, protein LZIC, FGFR1 oncogene partner 2, and guanine nucleotide-binding protein subunit beta-5. Using spot expression profile analysis, we found two proteins (WD repeat-containing protein 1 and mitochondrial glycerol-3-phosphate dehydrogenase) that may be part of thrombin specific activation or signal transduction pathway(s). Our results, characterizing the differences within proteins in both activated (by various agonists) and resting platelets, can thus contribute to the basic knowledge of platelets and to the understanding of the function and development of new antiplatelet drugs.

The aim of this proteomic study was to look for changes taking place in plasma proteomes of patients with acute myocardial infarction (AMI), unstable angina pectoris (UAP), and stable angina pectoris (SAP).

Abnormal coagulation properties indicative of a dysfibrinogen were found in the plasma of a 72-year-old male with multiple myeloma (IgGĸ, stage IIIA). The patient had high paraprotein concentration (85.75 g/l) and prolonged thrombin time (76.8 s), activated partial thromboplastin time (39.5 s), prothrombin time (23.5 s) and reptilase time (72.0 s). The fibrinogen level was increased. The fibrin polymerization induced by both thrombin and reptilase was impaired. Scanning electron microscopy revealed abnormal clot morphology. After six months of treatment, the paraprotein level decreased (19.48 g/l) and coagulation normalized as well as fibrin polymerization and fibrin clot morphology. It was found that the paraprotein interacts with the γ-chain of fibrinogen. Acquired dysfibrinogenemia associated with multiple myeloma was diagnosed in the 72-year-old patient.

Early and late thrombosis remain the most frequent reasons for the failure of synthetic cardiovascular grafts. Long-term hemocompatibility of implanted synthetic grafts can be achieved if a natural living endothelium is formed over its blood-contacting surface. Here we present a modification of a standard expanded polytetrafluorethylene (ePTFE) vessel prosthesis by a controlled preparation of a fibrin mesh enriched with covalently bound heparin and noncovalently bound vascular endothelial growth factor (VEGF) and fibroblast growth factor (FGF). Compared to a bare prosthesis, the coated prosthesis showed excellent antithrombogenic properties after contact with heparinized fresh human blood. Human umbilical vein endothelial cells seeded on the inner surface of the coated prosthesis formed a confluent layer in 5 days, whereas only small colonies of cells were scattered on the bare prosthesis. Viability of the cells was promoted mainly by FGF immobilized on the coating. These findings suggest that the coating may prevent acute thrombus formation and support the self-endothelialization of an implanted ePTFE vascular graft in vivo.