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. 2024 Apr 10;24(1):443.
doi: 10.1186/s12885-024-12161-5.

Identification of stemness-related glycosylation changes in head and neck squamous cell carcinoma

Affiliations

Identification of stemness-related glycosylation changes in head and neck squamous cell carcinoma

E Routila et al. BMC Cancer. .

Abstract

Background: Altered glycosylation is a hallmark of cancer associated with therapy resistance and tumor behavior. In this study, we investigated the glycosylation profile of stemness-related proteins OCT4, CIP2A, MET, and LIMA1 in HNSCC tumors.

Methods: Tumor, adjacent normal tissue, and blood samples of 25 patients were collected together with clinical details. After tissue processing, lectin-based glycovariant screens were performed.

Results: Strong correlation between glycosylation profiles of all four stemness-related proteins was observed in tumor tissue, whereas glycosylation in tumor tissue, adjacent normal tissue, and serum was differential.

Conclusions: A mannose- and galactose-rich glycosylation niche associated with stemness-related proteins was identified.

Keywords: Bioaffinity assay; Glycosylation; HNSCC; Lectin; Stemness.

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Conflict of interest statement

No potential conflicts of interest were disclosed by other authors.

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
Signal-to-background (S/B) ratios from glycovariant screening of (A) UT-SCC-14, and (B) UT-SCC-60B cell lines using antibodies for stemness-related proteins LIMA1, OCT4, MET, and CIP2A. Lectin binding properties are summarized as italic headings, with SBA binding both galactose and GalNAc and MAA binding both sialic acid and GlcNAc.
Fig. 2
Fig. 2
Tumor vs. normal signal-to-background (S/B) ratios from glycovariant screening of HNSCC tissue lysates (N = 25) (A) as a ratio of S/B ratios and (B) as a difference between S/B ratios
Fig. 3
Fig. 3
The correlations of tumor vs. tumor, tumor vs. normal and normal vs. normal samples from glycovariant screening of HNSCC tissue lysates (N = 25) (A) between six lectins and (B) between four stemness-related proteins

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