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. 2023 Apr 8;13(1):5752.
doi: 10.1038/s41598-023-32597-2.

Expression and localisation of MUC1 modified with sialylated core-2 O-glycans in mucoepidermoid carcinoma

Affiliations

Expression and localisation of MUC1 modified with sialylated core-2 O-glycans in mucoepidermoid carcinoma

Takanori Sugiura et al. Sci Rep. .

Abstract

Mucoepidermoid carcinoma (MEC) is the most frequent of the rare salivary gland malignancies. We previously reported high expression of Mucin 1 (MUC1) modified with sialylated core-2 O-glycans in MEC by using tissue homogenates. In this study, we characterised glycan structures of MEC and identified the localisation of cells expressing these distinctive glycans on MUC1. Mucins were extracted from the frozen tissues of three patients with MEC, and normal salivary glands (NSGs) extracted from seven patients, separated by supported molecular matrix electrophoresis (SMME) and the membranes stained with various lectins. In addition, formalin-fixed, paraffin-embedded sections from three patients with MEC were subjected to immunohistochemistry (IHC) with various monoclonal antibodies and analysed for C2GnT-1 expression by in situ hybridisation (ISH). Lectin blotting of the SMME membranes revealed that glycans on MUC1 from MEC samples contained α2,3-linked sialic acid. In IHC, MUC1 was diffusely detected at MEC-affected regions but was specifically detected at apical membranes in NSGs. ISH showed that C2GnT-1 was expressed at the MUC1-positive in MEC-affected regions but not in the NSG. MEC cells produced MUC1 modified with α2,3-linked sialic acid-containing core-2 O-glycans. MUC1 containing these glycans deserves further study as a new potential diagnostic marker of MEC.

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Conflict of interest statement

The authors declare no competing interests.

Figures

Figure 1
Figure 1
Lectin blotting of the SMME membranes separating salivary gland homogenates. (A) MAL-II; (B) SSA; (C) BC2LCN; (D) AAL. Sample numbers 1–3: MEC and 4–10: NSGs. Sample properties are summarised in Table 3. Partially purified porcine gastric mucin (PGM) was used as a reference mixture of chondroitin sulphate (CS), hyaluronic acid (HA), acidic mucin (AM) and neutral mucin (NM). The migrating positions of these components of PGM were estimated from a previous report. The original, unprocessed versions of full-length lectin blotting images are included in the supplemental (Supplemental Fig. S1).
Figure 2
Figure 2
Comparison of the expression patterns of MUC1 and sialoglycans between MEC and its surrounding normal salivary gland. The representative images (original magnification, × 400) of H&E staining (A), staining with anti-MUC1 antibody (B), staining with anti-Sialyl-Tn antibody (C) and staining with MAL-II (D) are shown. Ducts (a), serous acini (b) and mucous acini (c) are indicated by H&E staining of the normal salivary gland, and mucous cells (d) and non-mucous cells (e) are indicated in H&E staining of the MEC (A). Scale bars indicate 100 µm.
Figure 3
Figure 3
Comparison of the expression patterns of C2GnT-1 between MEC and its surrounding normal salivary gland. The representative images (original magnification, × 100 (A) and × 400 (B)) of ISH of C2GnT-1 are shown. Scale bars indicate 100 µm.
Figure 4
Figure 4
C2GnTs are the key enzyme for core-2 O-glycan biosynthesis. C2GnTs transfer a GlcNAc residue to the 6-position of GalNAc in core-1 disaccharide to form a core-2 trisaccharide. The core-2 trisaccharide is further modified by glycosyltransferases, including sialyltransferases and fucosyltransferases to turn various meaningful structures, such as the sialyl Lewis type, into a determinant.

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