Evidence map›Paper›PMID 33543029›Full record

ArticleMatrix biology plus2020

Serglycin activates pro-tumorigenic signaling and controls glioblastoma cell stemness, differentiation and invasive potential.

Dimitra Manou, Panagiotis Bouris, Dimitris Kletsas, Martin Götte, Burkhard Greve, Aristidis Moustakas, Nikos K Karamanos, Achilleas D Theocharis

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Matrix biology plus, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Glycosylation Gene Signatures as Prognostic Biomarkers in Glioblastoma.Annals of clinical and translational neurology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Proteoglycans as Mediators of Cancer Tissue Mechanics.Frontiers in cell and developmental biology · 2020
    Review
  18. Article
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 4 institutions in 3 countries.

Dimitra ManouBiochemistry, Biochemical Analysis & Matrix Pathobiology Research Group, Laboratory of Biochemistry, Department of Chemistry, University of Patras, Greece.
Panagiotis BourisBiochemistry, Biochemical Analysis & Matrix Pathobiology Research Group, Laboratory of Biochemistry, Department of Chemistry, University of Patras, Greece.
Dimitris KletsasLaboratory of Cell Proliferation & Ageing, Institute of Biosciences & Applications, National Centre for Scientific Research 'Demokritos', Athens, Greece.
Martin GötteDepartment of Gynecology and Obstetrics, University Hospital, Muenster, Germany.
Burkhard GreveDepartment of Radiotherapy-Radiooncology, University Hospital, Muenster, Germany.
Aristidis MoustakasDepartment of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Sweden.
Nikos K KaramanosBiochemistry, Biochemical Analysis & Matrix Pathobiology Research Group, Laboratory of Biochemistry, Department of Chemistry, University of Patras, Greece.
Achilleas D TheocharisBiochemistry, Biochemical Analysis & Matrix Pathobiology Research Group, Laboratory of Biochemistry, Department of Chemistry, University of Patras, Greece.
University of Patras · GRUniversity Hospital Münster · DENational Centre of Scientific Research "Demokritos" · GRScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the functional role of serglycin as an intracellular proteoglycan, a variety of malignant cells depends on its expression and constitutive secretion to advance their aggressive behavior. Serglycin arose to be a biomarker for glioblastoma, which is the deadliest and most treatment-resistant form of brain tumor, but its role in this disease is not fully elucidated. In our study we suppressed the endogenous levels of serglycin in LN-18 glioblastoma cells to decipher its involvement in their malignant phenotype. Serglycin suppressed LN-18 (LN-18

Indexed as

ALDH1, aldehyde dehydrogenase 1Astrocytic differentiationCXCR, C-X-C chemokine receptorECM, extracellular matrixEMT, epithelial to mesenchymal transitionERK, extracellular-signal-regulated kinaseGFAP, glial fibrillary acid proteinGlioblastomaIL, interleukinInterleukinsMAPK, mitogen-activated protein kinaseMMPs, metalloproteinasesPGs, proteoglycansPI3K, phosphoinositide 3-kinaseProteoglycansProteolytic enzymesSerglycinSignalingSRGN, serglycinSTAT-3, signal transducer and activator of transcription 3StemnessTIMPs, tissue inhibitors of metalloproteinasesuPA, urokinase plasminogen activator

Identifiers

PMID33543029
PMCPMC7852318
OpenAlexW3011378613

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.