Evidence map›Paper›PMID 27608845›Full record

ArticleOncotarget2016

Sialylation transmogrifies human breast and pancreatic cancer cells into 3D multicellular tumor spheroids using cyclic RGD-peptide induced self-assembly.

Roman Akasov, Sabah Haq, Fiona Haxho, Vanessa Samuel, Sergey V Burov, Elena Markvicheva, Ronald J Neufeld, Myron R Szewczuk

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. 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
2.3field-weighted citation impact, top 12% 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, 25 citations in OpenAlex.

  1. Aberrant Protein Glycosylation in Brain Cancers, with Emphasis on Glioblastoma.Advances in experimental medicine and biology · 2022
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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

8 authors at 3 institutions in 2 countries.

Roman AkasovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia.
Sabah HaqDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6 Canada.
Fiona HaxhoDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6 Canada.
Vanessa SamuelDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6 Canada.
Sergey V BurovInstitute of Macromolecular Compounds, Russian Academy of Sciences, Petersburg, 119004 Russia.
Elena MarkvichevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia.
Ronald J NeufeldDepartment of Chemical Engineering, Queen's University, Kingston, Ontario, K7L 3N6 Canada.
Myron R SzewczukDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6 Canada.
Queen's University · CAInstitute of Bioorganic Chemistry · RUInstitute of Macromolecular Compounds · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multicellular tumor spheroids (MTS) have been at the forefront of cancer research, designed to mimic tumor-like developmental patterns in vitro. Tumor growth in vivo is highly influenced by aberrant cell surface-specific sialoglycan structures on glycoproteins. Aberrant sialoglycan patterns that facilitate MTS formation are not well defined. Matrix-free spheroids from breast MCF-7 and pancreatic PANC1 cancer cell lines and their respective tamoxifen (TMX) and gemcitabine (Gem) resistant variants were generated using the RGD platform of cyclic Arg-Gly-Asp-D-Phe-Lys peptide modified with 4-carboxybutyl-triphenylphosphonium bromide (cyclo-RGDfK (TPP)). MCF-7 and MCF-7 TMX cells formed tight spheroids both in the classical agarose-and RGD-based platforms while all PANC1 cells formed loose aggregates. Using lectin histochemistry staining, sialidase assay, neuraminidase (Vibrio cholerae) and oseltamivir phosphate (OP) neuraminidase inhibitor treatments, MCF-7 and PANC1 cells and their drug-resistant variants expressed different sialic acid (SA) content on their cell surfaces. α-2,3- and α-2,6-sialic acid surface residues facilitated spheroid formation under cyclo-RGDfK(TPP)-induced self-assembly. Pretreatment with α-2,3- SA specific Maackia amurensis (MAL-II) lectin, α-2,6-SA specific Sambucus nigra (SNA) lectin, and exogenous α-2,6-SA specific neuraminidase (Vibrio cholerae) dose-dependently reduced spheroid volume. OP enhanced cell aggregation and compaction forming spheroids. PANC1 and MDA-MB231 xenograft tumors from untreated and OP-treated RAGxCγ double mutant mice expressed significantly higher levels of α-2,3- SA over α-2,6-SA. MCF-7 spheroids also expressed a high α-2,3-SA to α-2,6-SA ratio. These results suggest that the relative levels of specific sialoglycan structures on the cell surface correlate with the ability of cancer cells to form avascular multicellular tumor spheroids and in vivo xenograft tumors.

Indexed as

AnimalsBreast NeoplasmsCell AdhesionCell MovementCell ProliferationFemaleGlycoproteinsHumansMiceN-Acetylneuraminic AcidPancreatic NeoplasmsPeptides, CyclicSpheroids, CellularTumor Cells, CulturedXenograft Model Antitumor Assayscyclic arginine-glycine-aspartic acid peptideGlycoproteinsN-Acetylneuraminic AcidPeptides, Cyclicbreast canceroseltamivir phosphatepancreatic cancersialylationspheroids

Identifiers

PMID27608845
PMCPMC5323220
OpenAlexW2514539279

What OpenQuestion holds

Textmetadata
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.