| Autor: |
Takahashi, D., Fujihara, M., Azuma, H., Wakamoto, S., Sato, S., Kato, T., Ikeda, H. |
| Předmět: |
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| Zdroj: |
Vox Sanguinis; Apr2012, Vol. 102 Issue 3, p250-257, 8p, 5 Graphs |
| Abstrakt: |
Background: Activated platelets form heterogeneous aggregates of platelets and monocytes, which are involved in a variety of inflammatory disorders. Some anti-human leukocyte antigen (HLA) Class I antibodies have been shown to activate platelets. Materials and Methods: Human leukocyte antigen-A2-positive or HLA-A2-negative platelets were incubated with HLA-A2-negative peripheral blood mononuclear cells (PBMNCs) in the presence of anti-HLA-A2 serum at 37°C. The binding of platelets to monocytes was analysed by flow cytometry. The levels of IL-1 β and IL-8 in the culture supernatant were determined by ELISA. Results: Anti-HLA-A2 serum increased the formation of aggregates between monocytes and HLA-A2-positive platelets, but not HLA-A2-negative platelets, in a dose-dependent manner. Antiserum also increased the number of platelets bound to monocytes in a time-dependent manner. The addition of anti-P-selectin glycoprotein ligand (PSGL-1) mAb almost completely inhibited the formation of platelet-monocyte aggregates as well as the number of platelets bound to monocytes. When HLA-A2-positive or HLA-A2-negative platelets were incubated with HLA-A2-negative PBMNCs in the presence of anti-HLA-A2, the level of IL-1β and IL-8 in the supernatant of coculture was significantly higher in HLA-A2-positive platelets than in HLA-A2-negative platelets. The addition of anti-PSGL-1 mAb partially but significantly inhibited the production of both IL-1β and IL-8. Conclusions: The activation of platelets with anti-HLA Class I alloantibody caused the formation of platelet-monocyte aggregates, followed by the production of IL-1β and IL-8, in a cognate antigen-antibody manner. The adhesive interaction of P-selectin and PSGL-1 at least partially contributed to these phenomena. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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