Abstract
Factor VIII is a large, 2,332-residue plasma glycoprotein that acts as a regulatory cofactor in the process of blood coagulation [1–3]. It binds to activated factor IX (factor IXa) in the presence of calcium and negatively charged phospholipids at the surface of activated platelets to form a membrane-associated, proteolytically active complex. Upon complex formation, the V max of factor IXa is increased by approximately 200,000-fold, promoting the rapid activation of its substrate, the serine protease factor X. The proteolytic conversion of factor X to its active form, factor Xa, is a central control point in the coagulation cascade, leading to activation of thrombin, formation of a fibrin mesh, and establishment of a stable blood clot. The binding of factor VIIIc and other activated proteins to these membrane surfaces allows for localization of the procoagulation process to sites of vascular damage.
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Acknowledgments
The authors greatly appreciate the editorial assistance of Ms. Laura M. Bretaña. The authors also acknowledge the technical help provided by Mr. Jonathan Caldera Colón and Miss Maria Teresa Milán Mello. The authors are also indebted to Dr. Amitava Banerjee for his critical reading of the manuscript and for enhancing the quality of the images. The work has been supported in part by grants from the Department of Defense DAMD17-03-1-0754, the NIHU54-CA096297, and the Susan G. Komen Breast Cancer Foundation BCTR58206 (to Dipak K. Banerjee) and NIH/NCRR/RCMI grant G12-RR03035 (to Krishna Baksi).
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Banerjee, D.K. et al. (2011). Importance of a Factor VIIIc-Like Glycoprotein Expressed in Capillary Endothelial Cells (eFactor VIIIc) in Angiogenesis. In: Wu, A. (eds) The Molecular Immunology of Complex Carbohydrates-3. Advances in Experimental Medicine and Biology, vol 705. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7877-6_24
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