Evidence map›Paper›PMID 22185486›Full record

ArticleBiomacromolecules2012

Strain tunes proteolytic degradation and diffusive transport in fibrin networks.

Arjun S Adhikari, Armen H Mekhdjian, Alexander R Dunn

Open access · bronzeAbstract read
In one paragraph

Article in Biomacromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 24% of its field
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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Blood clot contraction: Mechanisms, pathophysiology, and disease.Research and practice in thrombosis and haemostasis · 2023
    Article
  3. Article
  4. Structural control of fibrin bioactivity by mechanical deformation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Biophysical Mechanisms Mediating Fibrin Fiber Lysis.BioMed research international · 2017
    Review
  10. Article
  11. Article
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

3 authors at 1 institution in 1 country.

Arjun S AdhikariDepartment of Chemical Engineering, Stanford University, Stanford, California 94305, United States.
Armen H Mekhdjian
Alexander R Dunn
Stanford University · US

Funding

Uncovering New Roles for Mechanical Force in Tissue Development and RemodelingDP2OD007078 · OD · STANFORD UNIVERSITY · PI DUNN, ALEXANDER R · 2010 to 2010
$2.4M
NIH HHS 1-DP2-OD007078-01NIH HHS DP2 OD007078Wellcome Trust
6 · The paper itself

Abstract

Proteolytic degradation of fibrin, the major structural component in blood clots, is critical both during normal wound healing and in the treatment of ischemic stroke and myocardial infarction. Fibrin-containing clots experience substantial strain due to platelet contraction, fluid shear, and mechanical stress at the wound site. However, little is understood about how mechanical forces may influence fibrin dissolution. We used video microscopy to image strained fibrin clots as they were degraded by plasmin, a major fibrinolytic enzyme. Applied strain causes up to 10-fold reduction in the rate of fibrin degradation. Analysis of our data supports a quantitative model in which the decrease in fibrin proteolysis rates with strain stems from slower transport of plasmin into the clot. We performed fluorescence recovery after photobleaching (FRAP) measurements to further probe the effect of strain on diffusive transport. We find that diffusivity perpendicular to the strain axis decreases with increasing strain, while diffusivity along the strain axis remains unchanged. Our results suggest that the properties of the fibrin network have evolved to protect mechanically loaded fibrin from degradation, consistent with its function in wound healing. The pronounced effect of strain upon diffusivity and proteolytic susceptibility within fibrin networks offers a potentially useful means of guiding cell growth and morphology in fibrin-based biomaterials.

Indexed as

Blood CoagulationAnimalsBiological TransportDiffusionFibrinFibrinolysinFluorescence Recovery After PhotobleachingHumansMicroscopy, VideoProteolysisStress, MechanicalFibrinFibrinolysin

Identifiers

PMID22185486
PMCPMC3737078
OpenAlexW2092415110

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.