Related Experiment Videos
Sensing adhesion forces between erythrocytes and γ' fibrinogen, modulating fibrin clot architecture and function
Ana Filipa Guedes1, Filomena A Carvalho2, Marco M Domingues1
1Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal; Thrombosis and Tissue Repair Group, Division of Cardiovascular and Diabetes Research, Leeds Institute of Cardiovascular and Metabolic Medicine and Multidisciplinary Cardiovascular Centre, Faculty of Medicine and Health, University of Leeds, Leeds, United Kingdom.
None:
Plasma fibrinogen includes an alternatively spliced γ-chain variant (γ'), which mainly exists as a heterodimer (γAγ') and has been associated with thrombosis. We tested γAγ' fibrinogen-red blood cells (RBCs) interaction using atomic force microscopy-based force spectroscopy, magnetic tweezers, fibrin clot permeability, scanning electron microscopy and laser scanning confocal microscopy. Data reveal higher work necessary for RBC-RBC detachment in the presence of γAγ' rather than γAγA fibrinogen. γAγ' fibrinogen-RBCs interaction is followed by changes in fibrin network structure, which forms an heterogeneous clot structure with areas of denser and highly branched fibrin fibers. The presence of RBCs also increased the stiffness of γAγ' fibrin clots, which are less permeable and more resistant to lysis than γAγA clots. The modifications on clots promoted by RBCs-γAγ' fibrinogen interaction could alter the risk of thrombotic disorders.