Evidence map›Paper›PMID 32830507›Full record

ArticleJournal of proteome research2020

Comparative Analysis of the Extracellular Matrix Proteome across the Myotendinous Junction.

Kathryn R Jacobson, Sarah Lipp, Andrea Acuna, Yue Leng, Ye Bu, Sarah Calve

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.1field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 69 citations in OpenAlex.

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  12. Genes · 2025
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  16. Article
  17. Interfacial Tissue Regeneration with Bone.Current osteoporosis reports · 2024
    Review
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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

6 authors at 2 institutions in 1 country.

Kathryn R JacobsonPurdue University Interdisciplinary Life Science Program, 155 S. Grant Street, West Lafayette, Indiana 47907, United States.
Sarah LippWeldon School of Biomedical Engineering, Purdue University, 206 South Martin Jischke Drive, West Lafayette, Indiana 47907, United States.
Andrea AcunaWeldon School of Biomedical Engineering, Purdue University, 206 South Martin Jischke Drive, West Lafayette, Indiana 47907, United States.
Yue LengWeldon School of Biomedical Engineering, Purdue University, 206 South Martin Jischke Drive, West Lafayette, Indiana 47907, United States.
Ye BuWeldon School of Biomedical Engineering, Purdue University, 206 South Martin Jischke Drive, West Lafayette, Indiana 47907, United States.
Sarah CalvePurdue University Interdisciplinary Life Science Program, 155 S. Grant Street, West Lafayette, Indiana 47907, United States.ORCID 0000-0002-7887-6307
Purdue University West Lafayette · USUniversity of Colorado Boulder · US

Funding

Indiana Medical Scientist/Engineer Training ProgramT32GM077229 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI GASTON, BENJAMIN, HERBERT, BRITTNEY-SHEA · 2008 to 2022
$6.0M
Defining the mechanical link that unites the musculoskeletal system during limb developmentDP2AT009833 · NCCIH · UNIVERSITY OF COLORADO · PI CALVE, SARAH · 2017 to 2017
$2.2M
Biomechanical Influence of ECM Remodeling on the Developing EnthesisR01AR071359 · NIAMS · UNIVERSITY OF COLORADO · PI CALVE, SARAH · 2017 to 2021
$1.7M
NCCIH NIH HHS DP2 AT009833NIAMS NIH HHS R01 AR071359NIGMS NIH HHS T32 GM077229
6 · The paper itself

Abstract

The myotendinous junction is a highly interdigitated interface designed to transfer muscle-generated force to tendon. Understanding how this interface is formed and organized, as well as identifying tendon- and muscle-specific extracellular matrix (ECM), is critical for designing effective regenerative therapies to restore functionality to damaged muscle-tendon units. However, a comparative analysis of the ECM proteome across this interface has not been conducted. The goal of this study was to resolve the distribution of ECM proteins that are uniformly expressed as well as those specific to each of the muscle, tendon, and junction tissues. The soleus muscles from 5-month-old wild-type C57BL/6 mice were harvested and dissected into the central muscle (M) away from tendon, the junction between muscle and tendon (J) and the tendon (T). Tissues were processed by either homogenizing in guanidine hydrochloride or fractionating to isolate the ECM from more soluble intracellular components and then analyzed using liquid chromatography-tandem mass spectrometry. Overall, we found that both tissue processing methods generated similar ECM profiles. Many ECM were found across the muscle-tendon unit, including type I collagen and associated fibril-regulating proteins. The ECM identified exclusively in M were primarily related to the basal lamina, whereas those specific to T and J tissue included thrombospondins and other matricellular ECM. Type XXII collagen (COL22A1) was restricted to J, and we identified COL5A3 as a potential marker of the muscle-tendon interface. Immunohistochemical analysis of key proteins confirmed the restriction of some basal lamina proteins to M, tenascin-C to T, and COL22A1 to J. COL5A3, PRELP, and POSTN were visualized in the tissue surrounding the junction, suggesting that these proteins play a role in stabilizing the interface. This comparative map provides a guide for tissue-specific ECM that can facilitate the spatial visualization of M, J, and T tissues and inform musculoskeletal regenerative therapies.

Indexed as

ProteomeTendonsAnimalsCollagenExtracellular MatrixExtracellular Matrix ProteinsMiceMice, Inbred C57BLCollagenExtracellular Matrix ProteinsProteomemass spectrometrymatrisomemousemuscletendon

Identifiers

PMID32830507
PMCPMC8325396
OpenAlexW3081276404

What OpenQuestion holds

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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.