Evidence map›Paper›PMID 41216609›Full record

ArticleJBMR plus2025

Identification of novel collagen breakdown products by human osteoclasts in vitro and in vivo.

Brendan P Norman, Jane P Dillon, Sahem M Alkharabsheh, Francoise Congues, Peter J M Wilson, Andrew S Davison, Elinor Chapman, James Baker, Séamus Coyle, Chris Probert and 4 more

Abstract read
In one paragraph

Article in JBMR plus, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–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

1 citing paper in PubMed.

  1. Magnetic imprinted surface enhanced Raman scattering biosensor for the detection of bone loss biomarker CTX-I.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2026
    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

14 authors.

Brendan P NormanDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.ORCID https://orcid.org/0000-0001-9293-4852
Jane P DillonDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.
Sahem M AlkharabshehDepartment of Medical Laboratory Sciences, Faculty of Allied Medical Sciences, Mutah University, Alkarak 61710, Jordan.
Francoise ConguesDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.
Peter J M WilsonDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.
Andrew S DavisonDepartment of Clinical Biochemistry and Metabolic Medicine, Liverpool Clinical Laboratories, Royal Liverpool University Hospitals Trust, Mount Vernon Street, Liverpool, L7 8YE, United Kingdom.ORCID https://orcid.org/0000-0001-5501-4475
Elinor ChapmanInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7BE, United Kingdom.
James BakerInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7BE, United Kingdom.
Séamus CoyleLiverpool Head and Neck Cancer Centre, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.
Chris ProbertInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7BE, United Kingdom.
Paul E BeauléDepartment of Surgery, The Ottawa Hospital, Smyth Road, Ottawa, Ontario K1H 8L6, Canada.
Lakshminarayan R RanganathDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.
Jeremy M WilkinsonDepartment of Oncology and Metabolism, University of Sheffield, Beech Hill Road, Sheffield, S10 2RX, United Kingdom.
James A GallagherDepartment of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool, L7 8TX, United Kingdom.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bone resorption involves dissolution of minerals and enzymatic degradation of bone matrix. The primary enzyme is cathepsin K but other proteases including matrix metalloproteinases are involved. Some cathepsin K cleavage products have been partially identified, including cross-linked telopeptides of type I collagen. Here, we aimed to characterize the entire complement of bone breakdown products resulting from osteoclast action under controlled conditions in vitro. We analyzed extracellular media from human osteoclasts cultured on dentin substrates, using untargeted liquid chromatography mass spectrometry. We discovered 22 breakdown products resulting from osteoclastic action. These products were peptide fragment sequences that mapped to various collagen proteins present in bone and dentin. Nine peptide fragments mapped exclusively to collagen I alpha-1 chain (COL1A1), the most abundant protein in bone. We subsequently detected 21 of the fragment products, initially observed in vitro, in human serum and/or urine. Consistent positive correlations were observed between the COL1A1-specific peptide fragments and established bone biochemical markers in serum and urine. Ten urine fragments and two serum fragments markedly increased (

Indexed as

collagenosteoclastspeptide fragmentsresorption

Identifiers

PMID41216609
PMCPMC12596726

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.