Evidence map›Paper›PMID 33010516›Full record

ArticleActa biomaterialia2020

Dependence of tendon multiscale mechanics on sample gauge length is consistent with discontinuous collagen fibrils.

Benjamin E Peterson, Spencer E Szczesny

Abstract read
In one paragraph

Article in Acta biomaterialia, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

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

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Focal adhesion kinase regulates tendon cell mechanoresponse and physiological tendon development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  7. Article
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  10. Review
  11. Review
  12. Article
  13. Review
  14. Mechanical StimulationFrontiers in cell and developmental biology · 2021
    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

2 authors.

Benjamin E PetersonDepartment of Biomedical Engineering, Pennsylvania State University, University Park PA.
Spencer E SzczesnyDepartment of Biomedical Engineering, Pennsylvania State University, University Park PA; Department of Orthopaedics and Rehabilitation, Pennsylvania State University, Hershey PA. Electronic address: ses297@psu.edu.

Funding

Studying Mechanotransduction in Late Embryonic Development to Inform Tendon Tissue EngineeringR21AR075941 · NIAMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI SZCZESNY, SPENCER · 2019 to 2020
$346k
NIAMS NIH HHS R21 AR075941
6 · The paper itself

Abstract

While collagen fibrils are understood to be the primary load-bearing elements in tendon, controversy still exists on how fibrils functionally transmit load from muscle to bone. Specifically, it's unclear whether fibrils are structurally continuous along the tendon length and bear load independently, or if they are discontinuous and transfer load through interfibrillar shear forces. To address this question, we investigated whether the multiscale mechanics of rat tail tendon fascicles is dependent on sample gauge length. We hypothesized that as the grip-to-grip length is reduced and approaches the length of the collagen fibrils, tendon fascicles will adopt a multiscale mechanical response consistent with structurally continuous fibrils. Our findings show that, for gauge lengths of 20 mm or greater, the local fibril strains are less than the bulk tissue strains, which can be explained by relative sliding between discontinuous collagen fibrils. In contrast, at a 5 mm gauge length, the fibril strains are equivalent to the applied tissue strains, suggesting that the collagen fibrils are structurally continuous between the grips. Additionally, the macroscale tissue modulus is increased at gauge lengths of 5 and 10 mm. Together, these data support the hypothesis that collagen fibrils in rat tail tendon fascicles are discontinuous and also suggest that their length is between 5 and 10 mm. This fundamental information regarding tendon structure-function relationships underscores the importance of the tissue components that transmit load between fibrils and is critical for understanding tendon pathology as well as establishing structural benchmarks for suitable tissue engineered replacements.

Indexed as

CollagenTendonsAnimalsBiomechanical PhenomenaExtracellular MatrixRatsTailWeight-BearingCollagenFibril lengthGauge lengthMultiscale mechanicsTendon

Identifiers

PMID33010516
PMCPMC8500354

What OpenQuestion holds

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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.