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Sensing adhesion forces between erythrocytes and γ' fibrinogen, modulating fibrin clot architecture and function

التفاصيل البيبلوغرافية
العنوان: Sensing adhesion forces between erythrocytes and γ' fibrinogen, modulating fibrin clot architecture and function
المؤلفون: Marco M. Domingues, Filomena A. Carvalho, Ana Filipa Guedes, Fraser L. Macrae, Helen R. McPherson, Nuno C. Santos, Robert A.S. Ariёns
المساهمون: Repositório da Universidade de Lisboa
المصدر: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Nanomedicine: Nanotechnology, Biology and Medicine
سنة النشر: 2017
مصطلحات موضوعية: 0301 basic medicine, Magnetic tweezers, Erythrocytes, Fibrin clot, Biomedical Engineering, Pharmaceutical Science, Medicine (miscellaneous), Bioengineering, 030204 cardiovascular system & hematology, Fibrinogen, Microscopy, Atomic Force, Fibrin, Hemostatics, 03 medical and health sciences, Atomic force microscopy, 0302 clinical medicine, medicine, Cell Adhesion, Humans, General Materials Science, Cell adhesion, Blood Coagulation, γ’ fibrinogen, biology, Chemistry, Fibrinogens, Abnormal, Force spectroscopy, Adhesion, medicine.disease, Thrombosis, 3. Good health, 030104 developmental biology, Permeability (electromagnetism), biology.protein, Biophysics, Microscopy, Electron, Scanning, Molecular Medicine, circulatory and respiratory physiology, medicine.drug
الوصف: © 2018 Elsevier Inc. All rights reserved.
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.
This work was supported by Fundação para a Ciência e a Tecnologia–Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal; PTDC/QUI-BIQ/119509/2010, PTDC/BBB-BMD/6307/2014 and SFRH/BD/84414/2012), the British Heart Foundation (RG/13/3/30104) and the Garfield Weston Trust.
وصف الملف: application/pdf
تدمد: 1549-9642
1549-9634
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c3c3c215c3c5d5a736fb3724b8d8963
https://pubmed.ncbi.nlm.nih.gov/29410160
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....3c3c3c215c3c5d5a736fb3724b8d8963
قاعدة البيانات: OpenAIRE
الوصف
تدمد:15499642
15499634