%0 Journal Article
%T Proteome changes in platelets activated by arachidonic acid, collagen, and thrombin
%A Pavel M¨¢jek
%A Zuzana Reicheltov¨¢
%A Jana £¿tikarov¨¢
%A Ji£¿¨ª Suttnar
%A Al£¿b¨§ta Sobotkov¨¢
%A Jan E Dyr
%J Proteome Science
%D 2010
%I BioMed Central
%R 10.1186/1477-5956-8-56
%X 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.Platelets are small anucleated blood particles derived from megakaryocytes in the bone marrow. They play a key role in the control of bleeding (hemostasis) by the formation of a vascular plug and the release of stimulatory molecules participating in hemostasis. Platelets circulating in the blood are normally maintained in a resting state; but upon a disruption of the integrity of the vascular endothelium or an alternation in the shear stress of the blood flow, platelets become activated. Platelets adhere to the damaged endothelium, coadhere (aggregate), and release both low molecular weight compounds and proteins [1]. This process of activation is accompanied by vast protein reorganization and posttranslational modifications. These platelet proteome changes are not yet fully understood and can lead either to thrombotic or bleeding disorders [1,2]. Therefore, understanding the mechanisms of platelet activation is crucial for the treatment of platelet-involved diseases.Although the number of identified platelet proteins increases every year, there is still a lack of the supplemental data necessary to clearly establish the role of these p
%U http://www.proteomesci.com/content/8/1/56