Intracellular Trafficking, Localization, and Mobilization of Platelet-Borne Thiol Isomerases
نویسندگان
چکیده
منابع مشابه
Intracellular Trafficking, Localization, and Mobilization of Platelet-Borne Thiol Isomerases.
OBJECTIVE Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet aggregation, blood coagulation, and thrombus formation. In this study, we examined the synthesis and trafficking of thiol isomerases in megakaryocytes,...
متن کاملIntracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases
Crescente, M., Pluthero , F. G., Li, L., Lo, R. W., Walsh, T. G., Schenk, M. P., Holbrook, L. M., Loureiro, S., Ali, M. S., Vaiyapuri, S., Falet, H., Jones, I. M., Poole, A. W., Kahr, W. H. A. and Gibbins, J. M. (2016) Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases. Arteriosclerosis Thrombosis and Vascular Biology, 36 (6). pp. 1164-1173. ISSN 1079-5...
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Protein disulfide isomerase (PDI), ERp5, and ERp57, among perhaps other thiol isomerases, are important for the initiation of thrombus formation. Using the laser injury thrombosis model in mice to induce in vivo arterial thrombus formation, it was shown that thrombus formation is associated with PDI secretion by platelets, that inhibition of PDI blocked platelet thrombus formation and fibrin ge...
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OBJECTIVE Staphylococcus aureus can induce platelet aggregation. The rapidity and degree of this correlates with the severity of disseminated intravascular coagulation, and depends on platelet peptidoglycans. Surface-located thiol isomerases play an important role in platelet activation. The staphylococcal extracellular adherence protein (Eap) functions as an adhesin for host plasma proteins. T...
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ژورنال
عنوان ژورنال: Arteriosclerosis, Thrombosis, and Vascular Biology
سال: 2016
ISSN: 1079-5642,1524-4636
DOI: 10.1161/atvbaha.116.307461