Evidence map›Paper›PMID 26029999›Full record

ArticleOncotarget2015

Mutation of N-linked glycosylation at Asn548 in CD133 decreases its ability to promote hepatoma cell growth.

Ying Liu, Shifang Ren, Liqi Xie, Chunhong Cui, Yang Xing, Chanjuan Liu, Benjin Cao, Fan Yang, Yinan Li, Xiaoning Chen and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

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  12. Can CD133 Be Regarded as a Prognostic Biomarker in Oncology: Pros and Cons.International journal of molecular sciences · 2023
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  17. The Journal of biological chemistry · 2020
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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

13 authors at 2 institutions in 1 country.

Ying LiuKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Shifang RenKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Liqi XieInstitutes of Biomedical Sciences of Fudan University, Shanghai, People's Republic of China.
Chunhong CuiKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Yang XingKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Chanjuan LiuKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Benjin CaoKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Fan YangKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Yinan LiKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Xiaoning ChenKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Yuanyan WeiKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Haojie LuInstitutes of Biomedical Sciences of Fudan University, Shanghai, People's Republic of China.
Jianhai JiangKey Laboratory of Glycoconjuates Research, Ministry of Public Health and Gene Research Center, Department of Biochemistry and Molecular Biology, Shanghai Medical College of Fudan University, Shanghai, People's Republic of China.
Shanghai Medical College of Fudan University · CNFudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane glycoprotein CD133 is a popular marker for cancer stem cells and contributes to cancer initiation and invasion in a number of tumor types. CD133 promotes tumorigenesis partly through an interaction between its phosphorylated Y828 residue and the PI3K regulatory subunit p85, and the interaction with β-catenin. Although CD133 glycosylation is supposed to be associated with its function, the contribution of N-glycosylation to its functions remains unclear. Here we analyzed the exact site(s) of N-glycosylation in CD133 by mass spectrometry and found that all eight potential N-glycosylation sites of CD133 could be indeed occupied by N-glycans. Loss of individual N-glycosylation sites had no effect on the level of expression or membrane localization of CD133. However, mutation at glycosylation site Asn548 significantly decreased the ability of CD133 to promote hepatoma cell growth. Furthermore, mutation of Asn548 reduced the interaction between CD133 and β-catenin and inhibited the activation of β-catenin signaling by CD133 overexpression. Our results identified the characteristics and function of CD133 glycosylation sites. These data could potentially shed light on molecular regulation of CD133 by glycosylation and enhance our understanding of the utility of glycosylated CD133 as a target for cancer therapies.

Indexed as

AC133 AntigenAmino Acid SequenceAntigens, CDAsparagineCarcinoma, HepatocellularCell Growth ProcessesGlycoproteinsGlycosylationHep G2 CellsHumansLiver NeoplasmsMolecular Sequence DataMutationPeptidesAC133 AntigenAntigens, CDAsparagineGlycoproteinsPeptidesPROM1 protein, humanCD133cell growthhepatomaN-linked glycosylation

Identifiers

PMID26029999
PMCPMC4653032
OpenAlexW1594725275

What OpenQuestion holds

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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.