Targeting the cancer glycocalyx in salivary duct carcinoma: tumor‐associated mucin 1 (Tn‐<scp>MUC1</scp>) as a novel cell surface marker

Despite the use of targeted drugs for human epidermal growth factor receptor type 2 (HER2)-positive salivary duct carcinoma (SDC) treatment, the overall prognosis for SDC remains poor. In this study, we aimed to investigate whether the glycocalyx of SDC cells serves as a potential cell surface marker. To understand the complex structure of the glycocalyx of salivary gland tumors, we used a lectin with glycan-specific binding properties. Lectin staining was performed for five types of common salivary gland tumors. We determined the expression of the transmembrane glycoprotein mucin 1 with Tn antigen (GalNAc), Tn-MUC1, using 20 clinical SDC specimens. Vicia villosa lectin (VVL) was not stained in the vascular endothelium but specifically stained in the SDC tumor cells. GalNAc, to which VVL binds, formed Tn-MUC1 via glycosylation with N-acetylgalactosaminyltransferases (GALNTs). GALNT7 was highly expressed in SDC. Analysis of clinical SDC specimens revealed that Tn-MUC1 was also positive in the SDC tumor cells, suggesting its potential as a cell surface target for SDC.

Authors

Institutions

Publication Details

Journal
The Journal of Pathology Clinical Research
Published
2025-08-22
DOI
https://doi.org/10.1002/2056-4538.70042
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Targeting the cancer glycocalyx in salivary duct carcinoma: tumor‐associated mucin 1 (Tn‐MUC1) as a novel cell surface marker

Akira Hara, Hideshi Okada, Hiroyuki Tomita, Masashi Kuroki et al.
The Journal of Pathology Clinical Research
Glycosylation and Glycoproteins Research
article

Targeting the cancer glycocalyx in salivary duct carcinoma: tumor‐associated mucin 1 (Tn‐MUC1) as a novel cell surface marker

Akira Hara, Hideshi Okada, Hiroyuki Tomita, Masashi Kuroki, Takenori Ogawa, Hirofumi Shibata, Ryo Kawaura, Tomohiko Ishikawa, Toshimitsu Ohashi
article en

Abstract

Despite the use of targeted drugs for human epidermal growth factor receptor type 2 (HER2)-positive salivary duct carcinoma (SDC) treatment, the overall prognosis for SDC remains poor. In this study, we aimed to investigate whether the glycocalyx of SDC cells serves as a potential cell surface marker. To understand the complex structure of the glycocalyx of salivary gland tumors, we used a lectin with glycan-specific binding properties. Lectin staining was performed for five types of common salivary gland tumors. We determined the expression of the transmembrane glycoprotein mucin 1 with Tn antigen (GalNAc), Tn-MUC1, using 20 clinical SDC specimens. Vicia villosa lectin (VVL) was not stained in the vascular endothelium but specifically stained in the SDC tumor cells. GalNAc, to which VVL binds, formed Tn-MUC1 via glycosylation with N-acetylgalactosaminyltransferases (GALNTs). GALNT7 was highly expressed in SDC. Analysis of clinical SDC specimens revealed that Tn-MUC1 was also positive in the SDC tumor cells, suggesting its potential as a cell surface target for SDC.

The Journal of Pathology Clinical ResearchVol. 11(5)
Tohoku University (JP), Ogaki Municipal Hospital (JP), Gifu University (JP)
Japan Society for the Promotion of Science, Japan Science and Technology Agency
Openalex Percentile: Top 81%
Glycosylation and Glycoproteins Research
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.