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Transcript
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