Evidence map›Paper›PMID 33139851›Full record

ArticleScientific reports2020

Mass spectrometric quantitation of AGEs and enzymatic crosslinks in human cancellous bone.

Shoutaro Arakawa, Ryusuke Suzuki, Daisaburo Kurosaka, Ryo Ikeda, Hiroteru Hayashi, Tomohiro Kayama, Rei-Ichi Ohno, Ryoji Nagai, Keishi Marumo, Mitsuru Saito

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery of Glycation-Derived Cross-links at Arginine.Journal of the American Chemical Society · 2026
    Article
  4. Article
  5. Pentosidine as a biomarker for bone fragility: Molecular mechanisms, clinical relevance, and detection strategies.Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Increased Advanced Glycation Endproducts, Stiffness, and Hardness in Iliac Crest Bone From Postmenopausal Women With Type 2 Diabetes Mellitus on Insulin.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2023
    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

10 authors at 2 institutions in 1 country.

Shoutaro ArakawaDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan. s.arakawa@jikei.ac.jp.ORCID 0000-0002-8932-8357
Ryusuke SuzukiDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Daisaburo KurosakaDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Ryo IkedaDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Hiroteru HayashiDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Tomohiro KayamaDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Rei-Ichi OhnoLaboratory of Food and Regulation Biology, School of Agriculture, Tokai University, 9-1-1, Toroku, Higashi-ku, Kumamoto, 862-8652, Japan.
Ryoji NagaiLaboratory of Food and Regulation Biology, School of Agriculture, Tokai University, 9-1-1, Toroku, Higashi-ku, Kumamoto, 862-8652, Japan.
Keishi MarumoDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Mitsuru SaitoDepartment of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo, 105-8461, Japan.
Jikei University School of Medicine · JPKyushu Tokai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Advanced glycation end-products (AGEs) deteriorate bone strength. Among over 40 species identified in vivo, AGEs other than pentosidine were roughly estimated as total fluorescent AGEs (tfAGEs) due to technical difficulties. Using LC-QqTOF-MS, we established a system that enabled the quantitation of five AGEs (CML, CEL, MG-H1, CMA and pentosidine) as well as two mature and three immature enzymatic crosslinks. Human bone samples were collected from 149 patients who underwent total knee arthroplasty. Their clinical parameters were collected to investigate parameters that may be predictive of AGE accumulation. All the analytes were quantitated and showed significant linearity with high sensitivity and precision. The results showed that MG-H1 was the most abundant AGE, whereas pentosidine was 1/200-1/20-fold less abundant than the other four AGEs. The AGEs were significantly and strongly correlated with pentosidine, while showing moderate correlation with tfAGEs. Interestingly, multiple linear regression analysis revealed that gender contributed most to the accumulation of all the AGEs, followed by age, tartrate-resistant acid phosphatase-5b and HbA1c. Furthermore, the AGEs were negatively correlated with immature crosslinks. Mass spectrometric quantitation of AGEs and enzymatic crosslinks is crucial to a better understanding of ageing- and disease-related deterioration of bone strength.

Indexed as

AgedAged, 80 and overAgingArginineBone and BonesBone DiseasesFemaleGlycated HemoglobinGlycation End Products, AdvancedHumansImidazolesLysineMaleMass SpectrometryOrnithineSex CharacteristicsArginineGlycated HemoglobinGlycation End Products, Advancedhemoglobin A1c protein, humanImidazolesLysineNdelta-(5-hydro-5-methyl-4-imidazolon-2-yl)ornithineOrnithinepentosidineTartrate-Resistant Acid Phosphatase

Identifiers

PMID33139851
PMCPMC7606603
OpenAlexW3096859646

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Registered trials

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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.