Guedes, AF, Carvalho, FA, Domingues, MM et al. (7 more authors) (2018) Impact of γ'γ' fibrinogen interaction with red blood cells on fibrin clots. Nanomedicine, 13 (19). pp. 2491-2505. ISSN 1743-5889
Abstract
AIM:γ' fibrinogen has been associated with thrombosis. Here the interactions between γ'γ' or γAγA fibrinogen and red blood cells (RBCs), and their role on fibrin clot properties were studied. MATERIALS & METHODS:Atomic Force microscopy (AFM)-based force spectroscopy, rheological, electron and confocal microscopy, and computational approaches were conducted for both fibrinogen variants. RESULTS & CONCLUSION:AFM shows that the recombinant human (rh)γ'γ' fibrinogen increases the binding force and the frequency of the binding to RBCs compared with rhγAγA, promoting cell aggregation. Structural changes in rhγ'γ' fibrin clots, displaying a nonuniform fibrin network were shown by microscopy approaches. The presence of RBCs decreases the fibrinolysis rate and increases viscosity of rhγ'γ' fibrin clots. The full length of the γ' chain structure, revealed by computational analysis, occupies a much wider surface and is more flexible, allowing an increase of the binding between γ' fibers, and eventually with RBCs.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | fibrin clot; fibrinolysis; red blood cell; thrombosis; γ′ fibrinogen |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Medicine (Leeds) > Leeds Institute of Cardiovascular and Metabolic Medicine (LICAMM) > Discovery & Translational Science Dept (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Nov 2018 11:38 |
Last Modified: | 21 Nov 2018 11:38 |
Status: | Published |
Publisher: | Future Medicine Ltd. |
Identification Number: | 10.2217/nnm-2018-0136 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:138868 |