Aggregates Dramatically Alter Fibrin Ultrastructure

García, Xabel; Seyve, Landry; Tellier, Z.; Chevreux, Guillaume; Bihoreau, Nicolas; Polack, Benoı̂t; Caton, François

doi:10.1016/j.bpj.2019.10.034

Cited by 8 publications

(12 citation statements)

References 27 publications

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“…What is more, the apparently slow unraveling of clusters by thrombin ( Fig. 2H and I ) raised the possibility that the reported distinct regions of network structure of thrombin induced clots of soluble fibrin 45 possibly reflect incompletely unraveled clusters and associated protofibrils that did not mature into normally organized fiber networks. Admittedly, our examples of such areas ( Figs.…”

Section: Discussionmentioning

confidence: 98%

Fibers Generated by Plasma Des-AA Fibrin Monomers and Protofibril/Fibrinogen Clusters Bind Platelets: Clinical and Nonclinical Implications

Galanakis

Protopopova

Zhang

et al. 2021

TH Open

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Objective Soluble fibrin (SF) is a substantial component of plasma fibrinogen (fg), but its composition, functions, and clinical relevance remain unclear. The study aimed to evaluate the molecular composition and procoagulant function(s) of SF. Materials and Methods Cryoprecipitable, SF-rich (FR) and cryosoluble, SF-depleted (FD) fg isolates were prepared and adsorbed on one hydrophilic and two hydrophobic surfaces and scanned by atomic force microscopy (AFM). Standard procedures were used for fibrin polymerization, crosslinking by factor XIII, electrophoresis, and platelet adhesion. Results Relative to FD fg, thrombin-induced polymerization of FR fg was accelerated and that induced by reptilase was markedly delayed, attributable to its decreased (fibrinopeptide A) FpA. FR fg adsorption to each surface yielded polymeric clusters and co-cryoprecipitable solitary monomers. Cluster components were crosslinked by factor XIII and comprised ≤21% of FR fg. In contrast to FD fg, FR fg adsorption on hydrophobic surfaces resulted in fiber generation enabled by both clusters and solitary monomers. This began with numerous short protofibrils, which following prolonged adsorption increased in number and length and culminated in surface-linked three-dimensional fiber networks that bound platelets. Conclusion The abundance of adsorbed protofibrils resulted from (1) protofibril/fg clusters whose fg was dissociated during adsorption, and (2) adsorbed des-AA monomers that attracted solution counterparts initiating protofibril assembly and elongation by their continued incorporation. The substantial presence of both components in transfused plasma and cryoprecipitate augments hemostasis by accelerating thrombin-induced fibrin polymerization and by tightly anchoring the resulting clot to the underlying wound or to other abnormal vascular surfaces.

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Section: Discussionmentioning

confidence: 98%

Fibers Generated by Plasma Des-AA Fibrin Monomers and Protofibril/Fibrinogen Clusters Bind Platelets: Clinical and Nonclinical Implications

Galanakis

Protopopova

Zhang

et al. 2021

TH Open

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“…In support of this explanation, the presence of fibrinogen aggregates in the clotting mixture has been shown to alter the kinetics of polymerization, impair the assembly of monomers into protofibrils and fibers 42 and reduce the protein density of fiber fibers and lessen coherency of the 22.5 nm axial packing. 69 Another possible source of variability in the fibrin fiber packing and their structural arrangement is that the presence of the fibrinogen g 0 chain splicing variant in plasma and plasma-derived fibrinogen preparations affects the number of protofibrils and protein density within fibers. 70 Whether protofibrils within a fibrin fiber are ordered or disordered in the direction transverse to the fiber axis has been a matter of debate.…”

Section: Discussionmentioning

confidence: 99%

Molecular packing structure of fibrin fibers resolved by X-ray scattering and molecular modeling

et al. 2020

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“…Carr and Hermans used the wavelength range of 350–650 nm because it is the most linear portion of the

versus

plots, as can be seen in Figure S4 in the Supporting Information . Although Yeromonahos does not explain the reasoning for using a wavelength range of 500–800 nm, it was argued by García et al [ 33 ] that by using this wavelength range, it is not as necessary to correct for the wavelength dependence of n and dn/dc, as it results in less than a 5% change in the data. We investigate this claim further in the Supporting Information Section S.3 .…”

Section: Methodsmentioning

confidence: 99%

“…They also compared the Taylor series approximations used in the Carr–Hermans and Yeromonahos approaches, claiming the one used by Carr and Hermans leads to more accurate results. This claim was debated in a later paper [ 33 ]. Finally, they proposed a new framework for analyzing turbidimetry data by using a combination of experimental approaches to incorporate the fractal nature of the networks in the analysis.…”

Section: Introductionmentioning

confidence: 99%

The Applicability of Current Turbidimetric Approaches for Analyzing Fibrin Fibers and Other Filamentous Networks

et al. 2022

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Turbidimetry is an experimental technique often used to study the structure of filamentous networks. To extract structural properties such as filament diameter from turbidimetric data, simplifications to light scattering theory must be employed. In this work, we evaluate the applicability of three commonly utilized turbidimetric analysis approaches, each using slightly different simplifications. We make a specific application towards analyzing fibrin fibers, which form the structural scaffold of blood clots, but the results are generalizable. Numerical simulations were utilized to assess the applicability of each approach across a range of fiber lengths and diameters. Simulation results indicated that all three turbidimetric approaches commonly underestimate fiber diameter, and that the “Carr-Hermans” approach, utilizing wavelengths in the range of 500–800 nm, provided <10% error for the largest number of diameter/length combinations. These theoretical results were confirmed, under select conditions, via the comparison of fiber diameters extracted from experimental turbidimetric data, with diameters obtained using super-resolution microscopy.

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Aggregates Dramatically Alter Fibrin Ultrastructure

Cited by 8 publications

References 27 publications

Fibers Generated by Plasma Des-AA Fibrin Monomers and Protofibril/Fibrinogen Clusters Bind Platelets: Clinical and Nonclinical Implications

Fibers Generated by Plasma Des-AA Fibrin Monomers and Protofibril/Fibrinogen Clusters Bind Platelets: Clinical and Nonclinical Implications

Molecular packing structure of fibrin fibers resolved by X-ray scattering and molecular modeling

The Applicability of Current Turbidimetric Approaches for Analyzing Fibrin Fibers and Other Filamentous Networks

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