Guedes, AF, Carvalho, FA, Domingues, MM et al. (4 more authors) (2018) Sensing adhesion forces between erythrocytes and γ’ fibrinogen, modulating fibrin clot architecture and function. Nanomedicine: Nanotechnology, Biology and Medicine, 14 (3). pp. 909-918. ISSN 1549-9634
Abstract
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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2018 Elsevier Inc. This is an author produced version of a paper published in Nanomedicine: Nanotechnology, Biology and Medicine. Uploaded in accordance with the publisher's self-archiving policy |
Keywords: | Cell adhesion; Atomic force microscopy; Magnetic tweezers; Fibrin clotγ’ fibrinogen |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Medicine (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 14 Aug 2018 15:05 |
Last Modified: | 02 Feb 2019 01:39 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.nano.2018.01.006 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:134589 |