Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2024 Oct 21;46(6):16. doi: 10.1007/s00281-024-01025-6

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 1 — Schematic representation of aberrant glycan structures expressed in ovarian cancer cells (gray box) in modified IUPAC-condensed nomenclature via the web application GlycoGlyph [167]. The corresponding glycan-binding receptors on the endothelium (blue) and immune cells (green) are depicted, along with the cellular effects they mediate. Double-headed arrows indicate interactions between glycans and glycoreceptors. Terminal Lewis structures on N-glycans interact with E- and P-selectins on endothelial cells, playing a crucial role in shaping both local and systemic immune responses. High-mannose glycans are recognized by CD206 on macrophages and, like O-glycosidic Tn and STn antigens, contribute to an immunosuppressive environment through engagement of CD301 on CDC2 and M2 macrophages. In ovarian carcinoma, tumor-specific glycosphingolipids induce T-cell arrest by interacting with Siglec-9 and Siglec-10 on CD8+ T cells, further promoting immune evasion. Additionally, glycosaminoglycans (GAGs) expressed in ovarian carcinoma, such as keratan sulfate (KS-III), contribute to immunosuppression. The heterogeneous sulfation patterns of these GAGs serve as further examples of their complexity. Cytosolic proteins from ovarian carcinoma cells, modified by O-GlcNAc, can be transported to the tumor microenvironment via exosomes and subsequently internalized by immune cells. This mechanism supports immune evasion and further undermines the host immune response against the tumor. Fuc, fucose; Gal, galactose; GalNAc, N-acetylgalactosamine; Glc, glucose; GlcA, glucuronic acid; GlcNAc, N-acetylglucosamine; IdoA, iduronic acid; Man, mannose; Neu5Ac, N-acetylneuraminic acid (sialic acid); Xyl, xylose; S, sulfate group; KS, keratan sulfate; HS, heparan sulfate; DS, dermatan sulfate; CS, chondroitin sulfate; HA, hyaluronic acid; Cer, ceramide