Evidence map›Paper›PMID 27028649›Full record

ArticleBiophysical journal2016

Fibrin Fiber Stiffness Is Strongly Affected by Fiber Diameter, but Not by Fibrinogen Glycation.

Wei Li, Justin Sigley, Marlien Pieters, Christine Carlisle Helms, Chandrasekaran Nagaswami, John W Weisel, Martin Guthold

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

75 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  8. Molecular Creep Induced Fatigue Rupture of Fibrin Clots.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Wei LiDepartment of Physics, Wake Forest University, Winston-Salem, North Carolina.
Justin SigleyDepartment of Physics, Wake Forest University, Winston-Salem, North Carolina.
Marlien PietersCentre of Excellence for Nutrition, North-West University, Potchefstroom, South Africa.
Christine Carlisle HelmsDepartment of Physics, University of Richmond, Richmond, Virginia.
Chandrasekaran NagaswamiDepartment of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania.
John W WeiselDepartment of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania.
Martin GutholdDepartment of Physics, Wake Forest University, Winston-Salem, North Carolina. Electronic address: gutholdm@wfu.edu.

Funding

Multiscale modeling and empirical study of a mechanism limiting blood clot growthU01HL116330 · NHLBI · UNIVERSITY OF NOTRE DAME · PI ALBER, MARK · 2014 to 2018
$3.5M
Structural origin of fibrin clot mechanical propertiesR01HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2009 to 2012
$1.6M
Structural origin of fibrin clot mechanical propertiesR56HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2014 to 2014
$408k
NHLBI NIH HHS HL090774NHLBI NIH HHS R01 HL090774NHLBI NIH HHS R56 HL090774NHLBI NIH HHS U01 HL116330
6 · The paper itself

Abstract

The major structural component of a blood clot is a mesh of fibrin fibers. Our goal was to determine whether fibrinogen glycation and fibrin fiber diameter have an effect on the mechanical properties of single fibrin fibers. We used a combined atomic force microscopy/fluorescence microscopy technique to determine the mechanical properties of individual fibrin fibers formed from blood plasma. Blood samples were taken from uncontrolled diabetic patients as well as age-, gender-, and body-mass-index-matched healthy individuals. The patients then underwent treatment to control blood glucose levels before end blood samples were taken. The fibrinogen glycation of the diabetic patients was reduced from 8.8 to 5.0 mol glucose/mol fibrinogen, and the healthy individuals had a mean fibrinogen glycation of 4.0 mol glucose/mol fibrinogen. We found that fibrinogen glycation had no significant systematic effect on single-fiber modulus, extensibility, or stress relaxation times. However, we did find that the fiber modulus, Y, strongly decreases with increasing fiber diameter, D, as Y∝D(-1.6). Thin fibers can be 100 times stiffer than thick fibers. This is unusual because the modulus is a material constant and should not depend on the sample dimensions (diameter) for homogeneous materials. Our finding, therefore, implies that fibrin fibers do not have a homogeneous cross section of uniformly connected protofibrils, as is commonly thought. Instead, the density of protofibril connections, ρPb, strongly decreases with increasing diameter, as ρPb∝D(-1.6). Thin fibers are denser and/or have more strongly connected protofibrils than thick fibers. This implies that it is easier to dissolve clots that consist of fewer thick fibers than those that consist of many thin fibers, which is consistent with experimental and clinical observations.

Indexed as

AdultAgedBiomechanical PhenomenaCrystallography, X-RayElastic ModulusFemaleFibrinFibrinogenGlycosylationHumansMiddle AgedViscoelastic SubstancesFibrinFibrinogenViscoelastic Substances

Identifiers

PMID27028649
PMCPMC4816776

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.