Evidence map›Paper›PMID 27624935›Full record

ArticleThe Journal of biological chemistry2016

Ring-Mesh Model of Proteoglycan Glycosaminoglycan Chains in Tendon based on Three-dimensional Reconstruction by Focused Ion Beam Scanning Electron Microscopy.

Takafumi Watanabe, Kiyokazu Kametani, Yoh-Ichi Koyama, Daisuke Suzuki, Yasutada Imamura, Kazushige Takehana, Kohzy Hiramatsu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Glycosaminoglycans and Their Role in Capillary Walls.Advances in experimental medicine and biology · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. The Ehlers-Danlos syndromes.Nature reviews. Disease primers · 2020
    Review
  11. Review
  12. Article
  13. Glycosaminoglycans and Proteoglycans.Pharmaceuticals (Basel, Switzerland) · 2018
    Article
  14. Article
  15. 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

7 authors at 5 institutions in 1 country.

Takafumi WatanabeFrom the Faculty of Agriculture, Shinshu University, Minami-minowa, Kami-ina, Nagano 399-4598, Japan, yosenabe@shinshu-u.ac.jp.
Kiyokazu KametaniDepartment of Instrumental Analysis, Research Center for Human and Environmental Science, Shinshu University, Asahi, Matsumoto, Nagano 390-8621, Japan.
Yoh-Ichi KoyamaResearch Institute of Biomatrix, Nippi Inc., Kuwabara, Toride, Ibaraki 302-0017, Japan.
Daisuke SuzukiDepartment of Musculoskeletal Biomechanics and Surgical Development, School of Medicine, Sapporo Medical University, Sapporo, Hokkaido 060-8556, Japan.
Yasutada ImamuraDepartment of Chemistry and Life Science, School of Advanced Engineering, Kogakuin University, Hachioji, Tokyo 192-0015, Japan, and.
Kazushige TakehanaSchool of Veterinary Medicine, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan.
Kohzy HiramatsuFrom the Faculty of Agriculture, Shinshu University, Minami-minowa, Kami-ina, Nagano 399-4598, Japan.
Shinshu University · JPJapan Institute of Leather Research · JPKogakuin University · JPRakuno Gakuen University · JPSapporo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tendons are composed of collagen fibrils and proteoglycan predominantly consisting of decorin. Decorin is located on the d-band of collagen fibrils, and its glycosaminoglycan (GAG) chains have been observed between collagen fibrils with transmission electron microscopy. GAG chains have been proposed to interact with each other or with collagen fibrils, but its three-dimensional organization remains unclear. In this report, we used focused ion beam scanning electron microscopy to examine the three-dimensional organization of the GAG chain in the Achilles tendon of mature rats embedded in epoxy resin after staining with Cupromeronic blue, which specifically stains GAG chains. We used 250 serial back-scattered electron images of longitudinal sections with a 10-nm interval for reconstruction. Three-dimensional images revealed that GAG chains form a ring mesh-like structure with each ring surrounding a collagen fibril at the d-band and fusing with adjacent rings to form the planar network. This ring mesh model of GAG chains suggests that more than two GAG chains may interact with each other around collagen fibrils, which could provide new insights into the roles of GAG chains.

Indexed as

Achilles TendonAnimalsGlycosaminoglycansImaging, Three-DimensionalMaleMicroscopy, Electron, ScanningModels, MolecularProteoglycansRatsRats, Sprague-DawleyGlycosaminoglycansProteoglycanschondroitin sulfatecollagendecorindermatan sulfatefocused ion beam scanning electron microscopeproteoglycan structurering meshtendon

Identifiers

PMID27624935
PMCPMC5095423
OpenAlexW2518931328

What OpenQuestion holds

Textmetadata
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.