Literature DB >> 27183056

Atomic force microscopy as a tool to evaluate the risk of cardiovascular diseases in patients.

Ana Filipa Guedes1, Filomena A Carvalho1, Inês Malho1, Nuno Lousada2, Luís Sargento2, Nuno C Santos1.   

Abstract

The availability of biomarkers to evaluate the risk of cardiovascular diseases is limited. High fibrinogen levels have been identified as a relevant cardiovascular risk factor, but the biological mechanisms remain unclear. Increased aggregation of erythrocytes (red blood cells) has been linked to high plasma fibrinogen concentration. Here, we show, using atomic force microscopy, that the interaction between fibrinogen and erythrocytes is modified in chronic heart failure patients. Ischaemic patients showed increased fibrinogen-erythrocyte binding forces compared with non-ischaemic patients. Cell stiffness in both patient groups was also altered. A 12-month follow-up shows that patients with higher fibrinogen-erythrocyte binding forces initially were subsequently hospitalized more frequently. Our results show that atomic force microscopy can be a promising tool to identify patients with increased risk for cardiovascular diseases.

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Year:  2016        PMID: 27183056     DOI: 10.1038/nnano.2016.52

Source DB:  PubMed          Journal:  Nat Nanotechnol        ISSN: 1748-3387            Impact factor:   39.213


  30 in total

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4.  Atherothrombosis and Thromboembolism: Position Paper from the Second Maastricht Consensus Conference on Thrombosis.

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5.  Transcriptome sequencing of Eospalax fontanierii to determine hypoxia regulation of cardiac fibrinogen.

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6.  A genetic modifier of venous thrombosis in zebrafish reveals a functional role for fibrinogen AαE in early hemostasis.

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7.  The 95RGD97 sequence on the Aα chain of fibrinogen is essential for binding to its erythrocyte receptor.

Authors:  Filomena A Carvalho; Ana Filipa Guedes; Cedric Duval; Fraser L Macrae; Luke Swithenbank; David H Farrell; Robert As Ariëns; Nuno C Santos
Journal:  Int J Nanomedicine       Date:  2018-04-03

8.  West Nile Virus Capsid Protein Interacts With Biologically Relevant Host Lipid Systems.

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9.  Mechanical Properties of Human Bronchial Epithelial Cells Expressing Wt- and Mutant CFTR.

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