Premium
Red blood cell–derived microparticles isolated from blood units initiate and propagate thrombin generation
Author(s) -
Rubin Olivier,
Delobel Julien,
Prudent Michel,
Lion Niels,
Kohl Kid,
Tucker Erik I.,
Tissot JeanDaniel,
AngelilloScherrer Anne
Publication year - 2013
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1111/trf.12008
Subject(s) - tissue factor , thrombin generation , coagulation , flow cytometry , chemistry , thrombin , phospholipid , thromboplastin , platelet poor plasma , red blood cell , whole blood , thrombomodulin , microbiology and biotechnology , platelet , immunology , biochemistry , medicine , biology , membrane
Background Red blood cell–derived microparticles ( RMP s) are small phospholipid vesicles shed from RBCs in blood units, where they accumulate during storage. Because microparticles are bioactive, it could be suggested that RMP s are mediators of posttransfusion complications or, on the contrary, constitute a potential hemostatic agent. Study Design and Methods This study was performed to establish the impact on coagulation of RMP s isolated from blood units. Using calibrated automated thrombography, we investigated whether RMP s affect thrombin generation ( TG ) in plasma. Results We found that RMP s were not only able to increase TG in plasma in the presence of a low exogenous tissue factor ( TF ) concentration, but also to initiate TG in plasma in absence of exogenous TF . TG induced by RMP s in the absence of exogenous TF was neither affected by the presence of blocking anti‐ TF nor by the absence of Factor (F)VII. It was significantly reduced in plasma deficient in FVIII or F IX and abolished in FII‐, FV‐, FX‐, or FXI‐deficient plasma. TG was also totally abolished when anti‐ XI 01 A 6 was added in the sample. Finally, neither Western blotting, flow cytometry, nor immunogold labeling allowed the detection of traces of TF antigen. In addition, RMP s did not comprise polyphosphate, an important modulator of coagulation. Conclusions Taken together, our data show that RMP s have FXI ‐dependent procoagulant properties and are able to initiate and propagate TG . The anionic surface of RMP s might be the site of FXI ‐mediated TG amplification and intrinsic tenase and prothrombinase complex assembly.