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Article Open Access

Downregulation of sialyl‑transferases and their role in malignant meningioma cells

  • Authors:
    • Pitchanun Jaturutthaweechot
    • Phattrara Khuansonthi
    • Pundit Asavarittikrai
    • Krajang Talabnin
    • Chutima Talabnin
  • View Affiliations / Copyright

    Affiliations: School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand, School of Surgery, Institute of Medicine, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand, School of Pathology, Institute of Medicine, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand
    Copyright: © Jaturutthaweechot et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
  • Article Number: 5
    |
    Published online on: October 31, 2025
       https://doi.org/10.3892/br.2025.2078
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Abstract

Meningiomas are the most common primary intracranial tumors and are often curable with gross resection. However, surgery is not entirely effective, as recurrences are reported more frequently in patients with meningiomas with higher‑grade tumors, despite the extent of surgical resection. Therefore, elucidating tumor biology at the molecular level is needed. Aberrant sialylation, resulting from altered expression of sialyl‑transferases (STs), plays an important role in cancer development and progression. However, the role of altered sialylation in meningioma progression remains unclear. In the present study, downregulation of β‑galactoside α2,3‑ST (ST3Gals) and β‑galactoside α2,6‑ST (ST6Gals) genes was found in malignant meningioma tissues from four different Gene Expression Omnibus (GEO) datasets (GEO entries: GSE16581, GSE43290, GSE74385 and GSE136661). Moreover, suppression of sialylation using a pan‑sialylation inhibitor (3Fax‑peracetyl‑Neu5Ac, 3Fax) reduced the activity of STs in a malignant meningioma cell line, leading to an increase in cell migration and invasion capacities. Further investigation of epithelial‑mesenchymal transition (EMT) markers, AKT, and ERK signaling in the 3Fax‑treated cell lines revealed that high expression of EMT‑related transcription factors (Snail) and EMT‑related proteins (MMP9) were regulated via phosphorylation of AKT and ERK. Therefore, the present findings suggested that suppression of sialylation by 3Fax in malignant meningioma increases migration and invasion abilities by enhancing the EMT process.
View Figures

Figure 1

Expression profiles of β-galactoside
α2,3 and α2,6 sialyl-transferase family in meningiomas. Expression
data obtained from four GEO entries: (A) GSE16581, (B) GSE43290,
(C) GSE74385 and (D) GSE136661. Values expressed as the mean ±
standard deviation. *P≤0.05, **P≤0.01,
***P≤0.001 and ****P≤0.0001 vs. WHO Grade 1.
GEO, Gene Expression Omnibus.

Figure 2

Suppression of sialylation does not
affect the proliferation of meningioma cells. HKBMM cells were
treated with various concentrations of 3Fax (0, 15.6, 31.2, 62.5,
125.0, 250.0, 500.0 µM) for 5 days. (A) Cytotoxic effect of 3Fax
was assessed using the WST-8 viability. (B) Histogram plots and
mean fluorescence intensity from lectin flow cytometry showed
decreased expression of α2,3-linked MAL II and α2,6-linked SNA
lectin sialic acids in 3Fax-treated cells (500 µM) compared with
DMSO-treated control cells. (C and D) Cell proliferation and
survival were assessed using the (C) WST-8 viability and (D) colony
formation assays. Values are expressed as the mean ± standard
deviation from three independent experiments. ***P≤0.001
and ****P≤0.0001 vs. control. MAL II, Maackia
amurensis lectin II; SNA, Sambucus nigra lectin.

Figure 3

Suppression of sialylation promotes
meningioma cell migration. HKBMM cells were treated with 3Fax at
500 µM or DMSO for 5 days. Migration ability was assessed using a
wound-healing assay. Representative wound healing images of
3Fax-treated cells compared with control cells at 0, 18 and 24 h
were selected from three independent experiments. Values are
expressed as the mean ± standard deviation. *P≤0.05 and
**P≤0.01 vs. control. Scale bar, 50 µm.

Figure 4

Suppression of sialylation induces an
aggressive meningioma cell phenotype. HKBMM cells were treated with
3Fax at 500 µM or DMSO for 5 days. Cell migration and invasion were
assessed using Transwell assays. (A and B) Representative migratory
cells and invasive cells of 3Fax-treated cells compared with
control cells at 18 and 24 h were selected from three independent
experiments. Values are expressed as the mean ± standard deviation.
**P≤0.01 and ****P≤0.0001 vs. control. Scale
bar, 50 µm.

Figure 5

Suppression of sialylation induces
expression of Snail and MMP9 via the activation of
AKT and ERK signaling in meningiomas. HKBMM cells were treated with
3Fax at 500 µM or DMSO for 5 days. (A) mRNA expression levels of
EMT-related transcription factors and EMT-related proteins were
determined via reverse transcription-quantitative PCR. (B) Protein
expression levels of MMP9, Snail, AKT and ERK were determined via
western blotting. Values are expressed as the mean ± standard
deviation from three independent experiments. *P≤0.05
vs. control. MMP, matrix metalloproteinase; EMT,
epithelial-mesenchymal transition; CDH1, E-cadherin; CDH2,
N-cadherin; p-, phosphorylated.

Figure 6

Alteration of sialylation affects the
migratory and invasive capabilities of meningioma cells. MMP,
matrix metalloproteinase. Created with BioRender.com.
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Copy and paste a formatted citation
Spandidos Publications style
Jaturutthaweechot P, Khuansonthi P, Asavarittikrai P, Talabnin K and Talabnin C: Downregulation of sialyl‑transferases and their role in malignant meningioma cells. Biomed Rep 24: 5, 2026.
APA
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., & Talabnin, C. (2026). Downregulation of sialyl‑transferases and their role in malignant meningioma cells. Biomedical Reports, 24, 5. https://doi.org/10.3892/br.2025.2078
MLA
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., Talabnin, C."Downregulation of sialyl‑transferases and their role in malignant meningioma cells". Biomedical Reports 24.1 (2026): 5.
Chicago
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., Talabnin, C."Downregulation of sialyl‑transferases and their role in malignant meningioma cells". Biomedical Reports 24, no. 1 (2026): 5. https://doi.org/10.3892/br.2025.2078
Copy and paste a formatted citation
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Spandidos Publications style
Jaturutthaweechot P, Khuansonthi P, Asavarittikrai P, Talabnin K and Talabnin C: Downregulation of sialyl‑transferases and their role in malignant meningioma cells. Biomed Rep 24: 5, 2026.
APA
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., & Talabnin, C. (2026). Downregulation of sialyl‑transferases and their role in malignant meningioma cells. Biomedical Reports, 24, 5. https://doi.org/10.3892/br.2025.2078
MLA
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., Talabnin, C."Downregulation of sialyl‑transferases and their role in malignant meningioma cells". Biomedical Reports 24.1 (2026): 5.
Chicago
Jaturutthaweechot, P., Khuansonthi, P., Asavarittikrai, P., Talabnin, K., Talabnin, C."Downregulation of sialyl‑transferases and their role in malignant meningioma cells". Biomedical Reports 24, no. 1 (2026): 5. https://doi.org/10.3892/br.2025.2078
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