Zobrazeno 1 - 10
of 93
pro vyhledávání: '"Gary E. Gilbert"'
A microengineered vascularized bleeding model that integrates the principal components of hemostasis
Autor:
Yumiko Sakurai, Elaissa T. Hardy, Byungwook Ahn, Reginald Tran, Meredith E. Fay, Jordan C. Ciciliano, Robert G. Mannino, David R. Myers, Yongzhi Qiu, Marcus A. Carden, W. Hunter Baldwin, Shannon L. Meeks, Gary E. Gilbert, Shawn M. Jobe, Wilbur A. Lam
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Hemostasis is a complex ensemble of events, but current bleeding assays only analyze single components like coagulation or platelet function. Here the authors present a comprehensive vascularized microfluidic mechanical injury bleeding model that add
Externí odkaz:
https://doaj.org/article/27d88574773748ba80530b1b1ef77b32
Autor:
Christopher V. Carman, Dessislava N. Nikova, Yumiko Sakurai, Jialan Shi, Valerie A. Novakovic, Jan T. Rasmussen, Wilbur A. Lam, Gary E. Gilbert
Publikováno v:
Blood advances. 7(1)
Prior reports indicate that the convex membrane curvature of phosphatidylserine (PS)-containing vesicles enhances formation of binding sites for factor Va and lactadherin. Yet, the relationship of convex curvature to localization of these proteins on
Autor:
Gary E. Gilbert
Publikováno v:
Blood
Antibody inhibitor development in hemophilia A represents the most significant complication resulting from factor VIII (fVIII) replacement therapy. Recent studies have demonstrated that epitopes present in the C1 domain contribute to a pathogenic inh
Autor:
Chunyan Gao, Rui Xie, Chengyuan Yu, Ruishuang Ma, Weijun Dong, Huan Meng, Yan Zhang, Yu Si, Zhuo Zhang, Valerie Novakovic, Yong Zhang, Junjie Kou, Yayan Bi, Baoxin Li, Rujuan Xie, Gary E Gilbert, Jin Zhou, Jialan Shi
Publikováno v:
PLoS ONE, Vol 10, Iss 11, p e0142835 (2015)
The mechanisms contributing to an increased risk of thrombosis in uremia are complex and require clarification. There is scant morphological evidence of membrane-dependent binding of factor Xa (FXa) and factor Va (FVa) on endothelial cells (EC) in vi
Externí odkaz:
https://doaj.org/article/73f8a42e25fb4b469c24cbe9f1cd8483
Autor:
Gary E. Gilbert
Publikováno v:
Blood Reviews. 33:1-5
Hemophilia A is caused by decreased or dysfunctional blood coagulation factor VIII (FVIII). Recent developments in the understanding of FVIII biology, in particular the nature of FVIII binding sites on platelets, may provide new insight into the limi
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77143 (2013)
Secretory phospholipase A2 (sPLA2) is a critical component of insect and snake venoms and is secreted by mammalian leukocytes during inflammation. Elevated secretory PLA2 concentrations are associated with autoimmune diseases and septic shock. Many s
Externí odkaz:
https://doaj.org/article/4d84030b8085433fac7d89e2b8ef7896
Publikováno v:
Journal of thrombosis and haemostasis : JTHREFERENCES. 18(12)
Background We recently reported that factor VIII (FVIII) binds to a macromolecular complex including fibrin on thrombin-stimulated platelets and that two antibodies against FVIII diminish platelet-supported FVIII activity more than vesicle-supported
Autor:
Gary E. Gilbert, Valerie A. Novakovic
Publikováno v:
Blood
Recent reports indicate that suspended skeletal and cardiac myosin, such as might be released during injury, can act as procoagulants by providing membrane-like support for factors Xa and Va in the prothrombinase complex. Further, skeletal myosin pro
Autor:
Qizhen Shi, Yingyu Chen, Feng Xue, Peter T. Sage, Gary E. Gilbert, Xin M. Liang, Christopher V. Carman
Publikováno v:
Blood Adv
Factor VIII (FVIII) replacement therapy for hemophilia A is complicated by development of inhibitory antibodies (inhibitors) in ∼30% of patients. Because endothelial cells (ECs) are the primary physiologic expression site, we probed the therapeutic
Publikováno v:
Blood. 136:3-4
Platelet activation supports procoagulant activity through phosphatidylserine exposure, secretion of procoagulant factors, and receptor conformational change. For example, thrombin-stimulated platelets bind factor VIII (fVIII) via a macromolecular co