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Transglutaminase-mediated oligomerization of the fibrin(ogen) αC domains promotes integrin-dependent cell adhesion and signaling by Alexey M. Belkin, Galina Tsurupa, Evgeny Zemskov, Yuri Veklich, John W. Weisel, and Leonid Medved Blood Volume 105(9):3561-3568 May 1, 2005 ©2005 by American Society of Hematology Preparation and characterization of αC(FXIII) and αC(tTG) oligomers. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Oligomerization of the αC domains stimulates RGD-dependent adhesion of endothelial cells via αVβ3, αVβ5, and α5β1 integrins. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Binding of purified αVβ3 integrin to immobilized αC monomers and αC(FXIII) or αC(tTG) oligomers. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Oligomerization of the αC domains facilitates endothelial cell spreading. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Endothelial cells assemble prominent focal adhesions on αC(FXIII) and αC(tTG) oligomers but not on αC monomers. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Oligomerization of the αC domains increases the amounts of αVβ3, αVβ5, and α5β1 integrins chemically cross-linked to substrate. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology Oligomerization of the αC domains amplifies adhesion-dependent activation of FAK and ERK. HUVECs were either kept in suspension or plated in serum-free DMEM for 2 hours on tissue culture plates coated with 20 μg/mL αC monomers or αC(FXIII) oligomers. Alexey M. Belkin et al. Blood 2005;105:3561-3568 ©2005 by American Society of Hematology