Evidence map›Paper›PMID 26632656›Full record

ArticleJournal of proteome research2016

Elucidating the Molecular Composition of Cartilage by Proteomics.

Ming-Feng Hsueh, Areej Khabut, Sven Kjellström, Patrik Önnerfjord, Virginia Byers Kraus

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 70 citations in OpenAlex.

  1. Pooled it
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  18. In Vitro Models and Proteomics in Osteoarthritis Research.Advances in experimental medicine and biology · 2023
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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

5 authors at 2 institutions in 2 countries.

Ming-Feng HsuehDuke Molecular Physiology Institute, ‡Departments of Medicine, and §Pathology, Duke University School of Medicine, Duke University , Durham, North Carolina 27701, United States.
Areej KhabutDuke Molecular Physiology Institute, ‡Departments of Medicine, and §Pathology, Duke University School of Medicine, Duke University , Durham, North Carolina 27701, United States.
Sven KjellströmDuke Molecular Physiology Institute, ‡Departments of Medicine, and §Pathology, Duke University School of Medicine, Duke University , Durham, North Carolina 27701, United States.
Patrik ÖnnerfjordDuke Molecular Physiology Institute, ‡Departments of Medicine, and §Pathology, Duke University School of Medicine, Duke University , Durham, North Carolina 27701, United States.
Virginia Byers KrausDuke Molecular Physiology Institute, ‡Departments of Medicine, and §Pathology, Duke University School of Medicine, Duke University , Durham, North Carolina 27701, United States.
Duke University · USLund University · SE

Funding

Resource Core 3 - Metabolomics CoreP30AG028716 · NIA · DUKE UNIVERSITY · PI Virginia B Kraus · 2006 to 2026
$24.6M
NIA NIH HHS P30 AG028716
6 · The paper itself

Abstract

Articular cartilage consists of chondrocytes and two major components, a collagen-rich framework and highly abundant proteoglycans. Most prior studies defining the zonal distribution of cartilage have extracted proteins with guanidine-HCl. However, an unextracted collagen-rich residual is left after extraction. In addition, the high abundance of anionic polysaccharide molecules extracted from cartilage adversely affects the chromatographic separation. In this study, we established a method for removing chondrocytes from cartilage sections with minimal extracellular matrix protein loss. The addition of surfactant to guanidine-HCl extraction buffer improved protein solubility. Ultrafiltration removed interference from polysaccharides and salts. Almost four-times more collagen peptides were extracted by the in situ trypsin digestion method. However, as expected, proteoglycans were more abundant within the guanidine-HCl extraction. These different methods were used to extract cartilage sections from different cartilage layers (superficial, intermediate, and deep), joint types (knee and hip), and disease states (healthy and osteoarthritic), and the extractions were evaluated by quantitative and qualitative proteomic analyses. The results of this study led to the identifications of the potential biomarkers of osteoarthritis (OA), OA progression, and the joint specific biomarkers.

Indexed as

BiomarkersCartilage, ArticularChondrocytesChromatographyExtracellular Matrix ProteinsGuanidinesHip JointHumansKnee JointMass SpectrometryOsteoarthritisProteoglycansProteomeProteomicsReproducibility of ResultsSurface-Active AgentsBiomarkersExtracellular Matrix ProteinsGuanidinesProteoglycansProteomeSurface-Active Agentscartilageextracellular matrix proteinsguanidine-HCl extractionin situ trypsin digestionmultiple reaction monitoringproteomics

Identifiers

PMID26632656
PMCPMC4917199
OpenAlexW2268595126

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.