Evidence map›Paper›PMID 34070747›Full record

ReviewInternational journal of molecular sciences2021

The Role of Glycosyltransferases in Colorectal Cancer.

Cecilia Fernández-Ponce, Noelia Geribaldi-Doldán, Ismael Sánchez-Gomar, Roberto Navarro Quiroz, Linda Atencio Ibarra, Lorena Gomez Escorcia, Ricardo Fernández-Cisnal, Gustavo Aroca Martinez, Francisco García-Cózar, Elkin Navarro Quiroz

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 54 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

10 authors at 6 institutions in 3 countries.

Cecilia Fernández-PonceDepartment of Biomedicine, Biotechnology and Public Health, Faculty of Medicine, University of Cadiz, 11003 Cádiz, Spain.ORCID 0000-0002-0027-1703
Noelia Geribaldi-DoldánInstitute of Biomedical Research Cadiz (INIBICA), 11009 Cádiz, Spain.ORCID 0000-0003-2149-9050
Ismael Sánchez-GomarDepartment of Biomedicine, Biotechnology and Public Health, Faculty of Medicine, University of Cadiz, 11003 Cádiz, Spain.
Roberto Navarro QuirozCenter of Mathematics, Computing and Cognition (CMCC) Laboratory of Computational Biology and Bioinformatics-LBCB, Federal University of ABC, Sao Paulo 09210-580, Brazil.
Linda Atencio IbarraFaculty of Medicine, Simón Bolívar University, Barranquilla 080001, Colombia.
Lorena Gomez EscorciaClínica de la Costa, Barranquilla 080001, Colombia.
Ricardo Fernández-CisnalInstitute of Biomedical Research Cadiz (INIBICA), 11009 Cádiz, Spain.
Gustavo Aroca MartinezFaculty of Medicine, Simón Bolívar University, Barranquilla 080001, Colombia.
Francisco García-CózarDepartment of Biomedicine, Biotechnology and Public Health, Faculty of Medicine, University of Cadiz, 11003 Cádiz, Spain.
Elkin Navarro QuirozCentro de Investigación e Innovación en Biomoléculas, Care4you S.A.S., Barranquilla 080001, Colombia.ORCID 0000-0001-7567-6409
Universidad de Cádiz · ESUniversity of the Coast · COBiomedical Research and Innovation Institute of Cadiz · ESSaint Martin University · COUniversidade Federal do ABC · BRUniversidad Simón Bolívar · CO

Funding

Agencia de Innovación y Desarrollo de Andalucía PI-0030-2017Departamento Administrativo de Ciencia, Tecnología e Innovación (COLCIENCIAS) 125380763038, 125380763188 and SGR code BPIN 2020000100144.
6 · The paper itself

Abstract

Colorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression in CRC and its impact in cell function and in several biological pathways associated with CRC pathogenesis, prognosis and therapeutic approaches. Glycan structures act as interface molecules between cells and their environment and in several cases facilitate molecule function. CRC tissue shows alterations in glycan structures decorating molecules, such as annexin-1, mucins, heat shock protein 90 (Hsp90), β1 integrin, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, decorin, sorbin and SH3 domain-containing protein 1 (SORBS1), CD147 and glycosphingolipids. All of these are described as key molecules in oncogenesis and metastasis. Therefore, glycosylation in CRC can affect cell migration, cell-cell adhesion, actin polymerization, mitosis, cell membrane repair, apoptosis, cell differentiation, stemness regulation, intestinal mucosal barrier integrity, immune system regulation, T cell polarization and gut microbiota composition; all such functions are associated with the prognosis and evolution of the disease. According to these findings, multiple strategies have been evaluated to alter oligosaccharide processing and to modify glycoconjugate structures in order to control CRC progression and prevent metastasis. Additionally, immunotherapy approaches have contemplated the use of neo-antigens, generated by altered glycosylation, as targets for tumor-specific T cells or engineered CAR (Chimeric antigen receptors) T cells.

Indexed as

Protein Processing, Post-TranslationalAnnexin A1Colorectal NeoplasmsDecorinErbB Receptorsfas ReceptorGene Expression Regulation, NeoplasticGlycosphingolipidsGlycosylationGlycosyltransferasesHumansImmunotherapy, AdoptiveInsulin-Like Growth Factor Binding Protein 3Integrin beta1Microfilament ProteinsMucinsAnnexin A1DCN protein, humanDecorinEGFR protein, humanErbB ReceptorsFAS protein, humanfas ReceptorGlycosphingolipidsGlycosyltransferasesIGFBP3 protein, humanInsulin-Like Growth Factor Binding Protein 3Integrin beta1Itgb1 protein, humanMicrofilament ProteinsMucinsNeoplasm ProteinsSORBS1 protein, humancolorectal cancer (CRC)glycosylationglycosyltransferasepost-translational modification

Identifiers

PMID34070747
PMCPMC8198577
OpenAlexW3164566232

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.