Evidence map›Paper›PMID 33580901›Full record

ArticleProteomics. Clinical applications2021

N-Glycan profiling of chondrocytes and fibroblast-like synoviocytes: Towards functional glycomics in osteoarthritis.

Johannes Fuehrer, Katharina M Pichler, Anita Fischer, Alexander Giurea, Daniela Weinmann, Friedrich Altmann, Reinhard Windhager, Hans-Joachim Gabius, Stefan Toegel

Open access · hybridAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-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

8 citing papers in PubMed, 20 citations in OpenAlex.

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  5. Iridoid fromEvidence-based complementary and alternative medicine : eCAM · 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

9 authors at 4 institutions in 2 countries.

Johannes FuehrerDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Katharina M PichlerKarl Chiari Lab for Orthopaedic Biology, Department of Orthopedics and Trauma Surgery, Medical University of Vienna, Vienna, Austria.ORCID 0000-0001-9944-9999
Anita FischerKarl Chiari Lab for Orthopaedic Biology, Department of Orthopedics and Trauma Surgery, Medical University of Vienna, Vienna, Austria.
Alexander GiureaDepartment of Orthopedics and Trauma Surgery, Division of Orthopedics, Medical University of Vienna, Vienna, Austria.
Daniela WeinmannKarl Chiari Lab for Orthopaedic Biology, Department of Orthopedics and Trauma Surgery, Medical University of Vienna, Vienna, Austria.ORCID 0000-0002-6298-4709
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0002-0112-7877
Reinhard WindhagerKarl Chiari Lab for Orthopaedic Biology, Department of Orthopedics and Trauma Surgery, Medical University of Vienna, Vienna, Austria.ORCID 0000-0002-6321-1804
Hans-Joachim GabiusFaculty of Veterinary Medicine, Institute of Physiological Chemistry, Ludwig-Maximilians University Munich, Munich, Germany.ORCID 0000-0003-3467-3900
Stefan ToegelKarl Chiari Lab for Orthopaedic Biology, Department of Orthopedics and Trauma Surgery, Medical University of Vienna, Vienna, Austria.ORCID 0000-0003-4317-1769
Medical University of Vienna · ATBOKU University · ATLudwig Boltzmann Institute for Traumatology, The Research Center in Cooperation with AUVA · ATLudwig-Maximilians-Universität München · DE

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

purposeN-Glycan profiling provides an indicator of the cellular potential for functional pairing with tissue lectins. Following the discovery of galectin expression by chondrocytes as a factor in osteoarthritis pathobiology, mapping of N-glycans upon their phenotypic dedifferentiation in culture and in fibroblast-like synoviocytes is a step to better understand glycobiological contributions to disease progression. EXPERIMENTAL

designThe profiles of cellular N-glycans of human osteoarthritic chondrocytes and fibroblast-like synoviocytes were characterized by mass spectrometry. RT-qPCR experiments determined mRNA levels of 16 glycosyltransferases. Responsiveness of cells to galectins was quantified by measuring the mRNA level for interleukin-1β.

resultsThe shift of chondrocytes to a fibroblastic phenotype (dedifferentiation) is associated with changes in N-glycosylation. The N-glycan profile of chondrocytes at passage 4 reflects characteristics of synoviocytes. Galectins-1 and -3 enhance expression of interleukin-1β mRNA in both cell types, most pronounced in primary culture. Presence of interleukin-1β leads to changes in sialylation in synoviocytes that favor galectin binding. CONCLUSIONS AND CLINICAL RELEVANCE: N-Glycosylation reflects phenotypic changes of osteoarthritic cells in vitro. Like chondrocytes, fibroblast-like synoviocytes express N-glycans that are suited to bind galectins, and these proteins serve as inducers of pro-inflammatory markers in these cells. Synoviocytes can thus contribute to disease progression in osteoarthritis in situ.

Indexed as

ChondrocytesFibroblastsGlycomicsOsteoarthritisPolysaccharidesSynoviocytesAgedCells, CulturedGalectinsGlycosylationHumansInterleukin-1betaMaleGalectinsInterleukin-1betaPolysaccharideschondrocytesgalectinsglycomicsosteoarthritissialylation

Identifiers

PMID33580901
PMCPMC8548877
OpenAlexW3127716119

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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.