What is the diameter of a fibrin fiber?

Belcher, Heather A.; Guthold, Martin; Hudson, Nathan E.

doi:10.1016/j.rpth.2023.100285

Cited by 3 publications

(3 citation statements)

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“…Super-resolution microscopy is likely the most accurate method to measure fibrin fiber diameters but is not widely available. Although we did not utilize superresolution microscopy in this work, it has been found that SEM and super-resolution microscopy result in very similar diameters across the range of physiologically relevant fibrinogen concentrations [35]. These results suggest that there are not significant structural changes to the fibers due to the SEM sample preparation process or that any shrinkage is compensated for by metal deposited during sputter coating.…”

Section: Methodsmentioning

confidence: 86%

“…However, much of the previous work did not explore concentrations higher than 1 mg/mL, whereas physiological concentrations range from 2 to 5 mg/mL and can be even higher in the presence of inflammation [47], COVID-19 [23,24,75], diabetes mellitus [22,69], and smoking [76][77][78]. It has been previously shown that as the fibrinogen concentration increases above 1 mg/mL, the corrected Yeromonahos approach is the most accurate in comparison to SEM imaging [35], and we find the same results for purified fibrinogen samples here. However, it appears from our results that as the fibrinogen concentration is increased, the variability between the reported diameters using the different methods increases, especially for the plasma samples.…”

Section: Discussionmentioning

confidence: 99%

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Comprehensive Analysis of the Role of Fibrinogen and Thrombin in Clot Formation and Structure for Plasma and Purified Fibrinogen

Risman,

Belcher,

Ramanujam

et al. 2024

Biomolecules

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Altered properties of fibrin clots have been associated with bleeding and thrombotic disorders, including hemophilia or trauma and heart attack or stroke. Clotting factors, such as thrombin and tissue factor, or blood plasma proteins, such as fibrinogen, play critical roles in fibrin network polymerization. The concentrations and combinations of these proteins affect the structure and stability of clots, which can lead to downstream complications. The present work includes clots made from plasma and purified fibrinogen and shows how varying fibrinogen and activation factor concentrations affect the fibrin properties under both conditions. We used a combination of scanning electron microscopy, confocal microscopy, and turbidimetry to analyze clot/fiber structure and polymerization. We quantified the structural and polymerization features and found similar trends with increasing/decreasing fibrinogen and thrombin concentrations for both purified fibrinogen and plasma clots. Using our compiled results, we were able to generate multiple linear regressions that predict structural and polymerization features using various fibrinogen and clotting agent concentrations. This study provides an analysis of structural and polymerization features of clots made with purified fibrinogen or plasma at various fibrinogen and clotting agent concentrations. Our results could be utilized to aid in interpreting results, designing future experiments, or developing relevant mathematical models.

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Section: Methodsmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Comprehensive Analysis of the Role of Fibrinogen and Thrombin in Clot Formation and Structure for Plasma and Purified Fibrinogen

Risman,

Belcher,

Ramanujam

et al. 2024

Biomolecules

Self Cite

View full text Add to dashboard Cite

show abstract

“…This action removes two fibrinopeptides, exposing 'knobs' and 'holes', and leading to a remarkable self-assembly in which fibrin monomers polymerise to make staggered oligomers, which themselves lengthen into protofibrils that aggregate laterally to make fibres, finally branching to create a three-dimensional network which represents the clots. Typical fibre diameters are a few hundred nm (say, 100-400 nm [84][85][86][87]), with a fractal morphology [88], meaning that a 'unit' of fibrin fibre contains many hundreds of fibrinogen monomers contributing to its diameter at any point. Clots are then degraded by plasmin, which itself has a variety of activators and inhibitors (Figure 3).…”

Section: What Are Fibrinaloid Microclots?mentioning

confidence: 99%

Fibrinaloid Microclots and Atrial Fibrillation

Kell,

Lip,

Pretorius

2024

Biomedicines

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Atrial fibrillation (AF) is a comorbidity of a variety of other chronic, inflammatory diseases for which fibrinaloid microclots are a known accompaniment (and in some cases, a cause, with a mechanistic basis). Clots are, of course, a well-known consequence of atrial fibrillation. We here ask the question whether the fibrinaloid microclots seen in plasma or serum may in fact also be a cause of (or contributor to) the development of AF. We consider known ‘risk factors’ for AF, and in particular, exogenous stimuli such as infection and air pollution by particulates, both of which are known to cause AF. The external accompaniments of both bacterial (lipopolysaccharide and lipoteichoic acids) and viral (SARS-CoV-2 spike protein) infections are known to stimulate fibrinaloid microclots when added in vitro, and fibrinaloid microclots, as with other amyloid proteins, can be cytotoxic, both by inducing hypoxia/reperfusion and by other means. Strokes and thromboembolisms are also common consequences of AF. Consequently, taking a systems approach, we review the considerable evidence in detail, which leads us to suggest that it is likely that microclots may well have an aetiological role in the development of AF. This has significant mechanistic and therapeutic implications.

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Variability in Individual Native Fibrin Fiber Mechanics

Helms

2024

Preprint

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Fibrin fibers are important structural elements in blood coagulation. They form a mesh network that acts as a scaffold and imparts mechanical strength to the clot. A review of published work measuring the mechanics of fibrin fibers reveals a range of values for fiber extensibility. This study investigates fibrinogen concentration as a possible variable responsible for variability in fibrin fiber mechanics. It expands previous work to describe the modulus, strain hardening, extensibility, and the force required for fiber failure when fibers are formed with different fibrinogen concentrations. Lateral force atomic force microscopy was used to create stress-strain curves for individual nanofibers and data was obtained from fibers formed from 0.5 NIH U/ml thrombin, 55 Loewy U/ml FXIII, and 1 mg/ml or 2 mg/ml fibrinogen. Analysis of the mechanical properties showed fiber formed from 1 mg/ml fibrinogen and 2 mg/ml fibrinogen had significantly different mechanical properties. To help clarify our findings we developed two behavior profiles to describe individual fiber mechanics. The first describes a fiber with low initial modulus and high extensible, that undergoes strain hardening around 100 % strain, and has moderate strength. A majority of fibers formed with 1 mg/ml fibrinogen showed this behavior profile. The second profile describes a fiber with a high initial modulus, minimal strain hardening, high strength, and low extensibility. Most fibrin fibers formed with 2 mg/ml fibrinogen were described with this second behavior profile. In conclusion, we see a range of behaviors from fibers formed from native fibrinogen molecules but various fibrinogen concentrations. Potential differences in fiber formation are investigated with SEM. It is likely this range of behaviors also occurs in vivo. Understanding the variability in mechanical properties could contribute to a deeper understanding of pathophysiology of coagulative disorders.

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What is the diameter of a fibrin fiber?

Cited by 3 publications

References 32 publications

Comprehensive Analysis of the Role of Fibrinogen and Thrombin in Clot Formation and Structure for Plasma and Purified Fibrinogen

Comprehensive Analysis of the Role of Fibrinogen and Thrombin in Clot Formation and Structure for Plasma and Purified Fibrinogen

Fibrinaloid Microclots and Atrial Fibrillation

Variability in Individual Native Fibrin Fiber Mechanics

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