Evidence map›Paper›PMID 29115405›Full record

ArticleInternational journal of molecular medicine2018

Alterations of protein glycosylation in embryonic stem cells during adipogenesis.

Wenguang Liu, Xingrong Yan, Wei Liu, Yangyang Wang, Yang Rao, Hanjie Yu, Jihong Cui, Xin Xie, Mei Sun, Lu Yin and 2 more

Open access · hybridAbstract read
In one paragraph

Article in International journal of molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

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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

12 authors at 1 institution in 1 country.

Wenguang LiuFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Xingrong YanFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Wei LiuFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Yangyang WangFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Yang RaoFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Hanjie YuFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Jihong CuiFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Xin XieFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Mei SunFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Lu YinFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Hongmin LiFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Fulin ChenFaculty of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Northwest University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The understanding of adipose tissue development is crucial for the treatment of obesity-related diseases. Adipogenesis has been extensively investigated at the gene and protein levels in recent years. However, the alterations in protein glycosylation during this process remains unknown, particularly that of parthenogenetic embryonic stem cells (pESCs), a type of ESCs with low immunogenicity and no ethical concerns regarding their use. Protein glycosylation markedly affects cell growth and development, cell-to-cell communication, tumour growth and metastasis. In the present study, the adipogenic potentials of J1 ESCs and pESCs were first compared and the results demonstrated that pESCs had lower adipogenic potential compared with J1 ESCs. Lectin microarray was then used to screen the alteration of protein glycosylation during adipogenesis. The results revealed that protein modification of GlcNAc and α-1-2-fucosylation increased, whereas α-1-6‑fucosylation, α-2-6-sialylation and α-1-6-mannosylation decreased in J1 ESCs and pESCs during this process. In addition, α-1-3-mannosylation decreased only in pESCs. Lectin histochemistry and quantitative polymerase chain reaction of glycosyltransferase confirmed the results obtained by lectin microarray. Therefore, protein glycosylation of ESCs was significantly altered during adipogenesis, indicating that protein glycosylation analysis is not only helpful for studying the mechanism of adipogenesis, but may also be used as a marker to monitor adipogenic development.

Indexed as

AdipogenesisCell DifferentiationCell LineCell ProliferationEmbryonic Stem CellsGlycosylationHumansLectinsParthenogenesisProtein Array AnalysisProtein Processing, Post-TranslationalProteinsLectinsProteins

Identifiers

PMID29115405
PMCPMC5746299
OpenAlexW2768046709

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.