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 Scopus, Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 2 декабря 2015 г.

Работа с статьей

[1] Procoagulant platelets form an alpha-granule protein-covered cap on their surface that promotes their attachment to aggregates / A. A. Abaeva, M. Canault, Y. N. Kotova et al. // Journal of Biological Chemistry. — 2013. — Vol. 288, no. 41. — P. 29621–29632. 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. [ DOI ]

Публикация в формате сохранить в файл сохранить в файл сохранить в файл сохранить в файл сохранить в файл сохранить в файл скрыть