Evidence map›Paper›PMID 19800998›Full record

ArticleOsteoarthritis and cartilage2010

Phenotype-related differential alpha-2,6- or alpha-2,3-sialylation of glycoprotein N-glycans in human chondrocytes.

S Toegel, M Pabst, S Q Wu, J Grass, M B Goldring, C Chiari, A Kolb, F Altmann, H Viernstein, F M Unger

Abstract read
In one paragraph

Article in Osteoarthritis and cartilage, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

22 citing papers in PubMed, 64 citations in OpenAlex.

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  12. Isomer-Specific Monitoring of SialylatedFrontiers in molecular biosciences · 2021
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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

10 authors at 5 institutions in 2 countries.

S ToegelMedical University Vienna, Vienna, Austria. stefan.toegel@meduniwien.ac.at
M Pabst
S Q Wu
J Grass
M B Goldring
C Chiari
A Kolb
F Altmann
H Viernstein
F M Unger
BOKU University · ATUniversity of Vienna · ATMedical University of Vienna · ATCornell University · USHospital for Special Surgery · US

Funding

Role of ESE1 Regulation of Type II Collagen in CartilageR01AG022021 · NIA · HOSPITAL FOR SPECIAL SURGERY · PI GOLDRING, MARY B · 2002 to 2014
$3.4M
NIA NIH HHS R01 AG022021NIA NIH HHS R01-AG022021
6 · The paper itself

Abstract

objectiveSialic acids frequently occur at the terminal positions of glycoprotein N-glycans present at chondrocyte surfaces or in the cartilage matrix. Sialic acids are transferred to glycoproteins in either alpha-2,3 or alpha-2,6 linkage by specific sialyltransferases (SiaTs) and can potentially affect cell functions and cell-matrix interactions. The present study aimed to assess the relationship between the expression of the human chondrocyte phenotype and the sialylation of chondrocyte glycoprotein N-glycans.

methodsThe transcription of 5 SiaT was quantified using real-time Reverse transcription polymerase chain reaction (RT-PCR) assays. N-glycan analysis was performed using LC-ESI-MS. Primary human chondrocytes were cultured in monolayer or alginate beads and compared to the chondrocyte cell lines C-28/I2 and SW1353. In addition, effects of interleukin-1beta (IL-1beta) or tumour necrosis factor-alpha (TNF-alpha) on primary cells were assessed.

resultsPrimary human chondrocytes predominantly express alpha-2,6-specific SiaTs and accordingly, alpha-2,6-linked sialic acid residues in glycoprotein N-glycans. In contrast, the preponderance of alpha-2,3-linked sialyl residues and, correspondingly, reduced levels of alpha-2,6-specific SiaTs are associated with the altered chondrocyte phenotype of C-28/I2 and SW1353 cells. Importantly, a considerable shift towards alpha-2,3-linked sialic acids and alpha-2,3-specific SiaT mRNA levels occurred in primary chondrocytes treated with IL-1beta or tumour necrosis factor-alpha (TNF-alpha).

conclusionThe expression of the differentiated chondrocyte phenotype is linked to the ratio of alpha-2,6- to alpha-2,3-linked sialic acids in chondrocyte glycoprotein N-glycans. A shift towards altered sialylation might contribute to impaired cell-matrix interactions in disease conditions.

Indexed as

Cell DifferentiationCell ProliferationCells, CulturedChondrocytesCytokinesGene ExpressionGlycoproteinsHumansInterleukin-1betaPhenotypeReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSialyltransferasesTumor Necrosis Factor-alphaCytokinesGlycoproteinsInterleukin-1betaRNA, MessengerSialyltransferasesTumor Necrosis Factor-alpha

Identifiers

PMID19800998
PMCPMC2818349
OpenAlexW2091889824

What OpenQuestion holds

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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.