Evidence map›Paper›PMID 22401852›Full record

ArticleBiomaterials2012

Molecular mechanism of force induced stabilization of collagen against enzymatic breakdown.

Shu-Wei Chang, Brendan P Flynn, Jeffrey W Ruberti, Markus J Buehler

Open access · greenAbstract read
In one paragraph

Article in Biomaterials, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 75 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanochemistry of collagen.Acta biomaterialia · 2023
    Review
  8. Intra-Articular Collagen Injections for Osteoarthritis: A Narrative Review.International journal of environmental research and public health · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Collagen peptide simulated bending after applied axial deformation.Journal of the mechanical behavior of biomedical materials · 2020
    Article
  15. Article
  16. Article
  17. Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'.Matrix biology : journal of the International Society for Matrix Biology · 2020
    Review
  18. Article
  19. Review
  20. Models of tendon development and injury.BMC biomedical engineering · 2019
    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

4 authors at 2 institutions in 1 country.

Shu-Wei ChangLaboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
Brendan P Flynn
Jeffrey W Ruberti
Markus J Buehler
Massachusetts Institute of Technology · USNortheastern University · US

Funding

Mechanobiology of Matrix Production by Corneal FibroblastsR01EY015500 · NEI · NORTHEASTERN UNIVERSITY · PI RUBERTI, JEFFREY W · 2005 to 2014
$3.8M
NEI NIH HHS R01 EY015500PHS HHS NEIEY0155500
6 · The paper itself

Abstract

Collagen cleavage, facilitated by collagenases of the matrix metalloproteinase (MMP) family, is crucial for many physiological and pathological processes such as wound healing, tissue remodeling, cancer invasion and organ morphogenesis. Earlier work has shown that mechanical force alters the cleavage rate of collagen. However, experimental results yielded conflicting data on whether applying force accelerates or slows down the degradation rate. Here we explain these discrepancies and propose a molecular mechanism by which mechanical force might change the rate of collagen cleavage. We find that a type I collagen heterotrimer is unfolded in its equilibrium state and loses its triple helical structure at the cleavage site without applied force, possibly enhancing enzymatic breakdown as each chain is exposed and can directly undergo hydrolysis. Under application of force, the naturally unfolded region refolds into a triple helical structure, potentially protecting the molecule against enzymatic breakdown. In contrast, a type I collagen homotrimer retains a triple helical structure even without applied force, making it more resistant to enzyme cleavage. In the case of the homotrimer, the application of force may directly lead to molecular unwinding, resulting in a destabilization of the molecule under increased mechanical loading. Our study explains the molecular mechanism by which force may regulate the formation and breakdown of collagenous tissue.

Indexed as

Stress, MechanicalAmino Acid SequenceAnimalsCattleCollagenCollagenasesHumansMiceMolecular Sequence DataProtein MultimerizationProtein StabilityCollagenCollagenases

Identifiers

PMID22401852
PMCPMC3309414
OpenAlexW2085396608

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.