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Procoagulant platelets form an alpha-granule protein-covered "cap" on their surface that promotes their attachment to aggregatesстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 2 декабря 2015 г.
- Авторы: Abaeva A.A., Canault M., Kotova Y.N., Obydennyy S.I., Yakimenko A.O., Podoplelova N.A., Kolyadko V.N., Chambost H., Mazurov A.V., Ataullakhanov F.I., Nurden A.T., Alessi M.C., Panteleev M.A.
- Журнал: Journal of Biological Chemistry
- Том: 288
- Номер: 41
- Год издания: 2013
- Издательство: American Society for Biochemistry and Molecular Biology Inc.
- Местоположение издательства: United States
- Первая страница: 29621
- Последняя страница: 29632
- DOI: 10.1074/jbc.M113.474163
- Аннотация: Strongly activated "coated" platelets are characterized by increased phosphatidylserine (PS) surface expression, alpha-granule protein retention, and lack of active integrin alphaIIbbeta3. To study how they are incorporated into thrombi despite a lack of free activated integrin, we investigated the structure, function, and formation of the alpha-granule protein "coat." Confocal microscopy revealed that fibrin(ogen) and thrombospondin colocalized as "cap," a single patch on the PS-positive platelet surface. In aggregates, the cap was located at the point of attachment of the PS-positive platelets. Without fibrin(ogen) retention, their ability to be incorporated in aggregates was drastically reduced. The surface fibrin(ogen) was strongly decreased in the presence of a fibrin polymerization inhibitor GPRP and also in platelets from a patient with dysfibrinogenemia and a fibrinogen polymerization defect. In contrast, a fibrinogen-clotting protease ancistron increased the amount of fibrin(ogen) and thrombospondin on the surface of the PS-positive platelets stimulated with collagen-related peptide. Transglutaminases are also involved in fibrin(ogen) retention. However, platelets from patients with factor XIII deficiency had normal retention, and a pan-transglutaminase inhibitor T101 had only a modest inhibitory effect. Fibrin(ogen) retention was normal in Bernard-Soulier syndrome and kindlin-3 deficiency, but not in Glanzmann thrombasthenia lacking the platelet pool of fibrinogen and alphaIIbbeta3. These data show that the fibrin(ogen)-covered cap, predominantly formed as a result of fibrin polymerization, is a critical mechanism that allows coated (or rather "capped") platelets to become incorporated into thrombi despite their lack of active integrins
- Добавил в систему: Атауллаханов Фазоил Иноятович