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Single-cell mapping of the glycocalyx in the adult human and mouse ocular surface

ABSTRACT: The glycocalyx is a critical but often underappreciated modulator of cellular behavior. Its diversity across cell types within tissues remains poorly understood, but recent advances in single-cell profiling now enable more precise analysis of cell surface composition. Here, we applied single-cell glycan and RNA sequencing to profile glycocalyx diversity across human and mouse ocular surface cell types. Glycocalyx patterns effectively distinguished epithelial subtypes, with corneal epithelial cells enriched in complex and high-mannose N-glycans, conjunctival cells in fucosylated structures, and goblet cells in O-glycans. We also observed dynamic changes during epithelial maturation, marked by regulated shifts in sialic acid structures. In the mouse ocular surface, glycocalyx patterns distinguished major cell types, but the glycan profiles differed from those in humans, pointing to species-specific features. These findings demonstrate that glycocalyx composition is closely linked to cell identity and maturation and provide a foundation for exploring its roles in tissue organization and disease.

ORGANISM(S): Mus musculus Homo sapiens

PROVIDER: GSE299152 | GEO | 2025/11/18

REPOSITORIES: GEO

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			Action	DRS
		Other
	GSE299152_Donor2046_filtered_feature_bc_matrix.h5	Other
	GSE299152_Donor2206_filtered_feature_bc_matrix.h5	Other
	GSE299152_Donor3748_filtered_feature_bc_matrix.h5	Other
	GSE299152_Mice1_filtered_feature_bc_matrix.h5	Other

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Project description:Various cancers such as colorectal cancer (CRC) are associated with alterations in protein glycosylation. CRC cell lines are frequently used to study these (glyco)biological changes and their mechanisms. However, differences between CRC cell lines with regard to their glycosylation have hitherto been largely neglected. Here, we comprehensively characterized the N-glycan profiles of 25 different CRC cell lines, derived from primary tumors and metastatic sites, in order to investigate their potential as glycobiological tumor model systems and to reveal glycans associated with cell line phenotypes. We applied an optimized, high-throughput membrane-based enzymatic glycan release for small sample amounts. Released glycans were derivatized to stabilize and differentiate between a2,3- and a2,6-linked N-acetylneuraminic acids, followed by N-glycosylation analysis by MALDI-TOF(/TOF)-MS. Our results showed pronounced differences between the N-glycosylation patterns of CRC cell lines. CRC cell line profiles differed from tissue-derived N-glycan profiles with regard to their high-mannose N-glycan content but showed a large overlap for complex type N-glycans, supporting their use as a glycobiological cancer model system. Importantly, we could show that the high-mannose N-glycans did not only occur as intracellular precursors but were also present at the cell surface. The obtained CRC cell line N-glycan features were not clearly correlated with mRNA expression levels of glycosyltransferases, demonstrating the usefulness of performing the structural analysis of glycans. Finally, correlation of CRC cell line glycosylation features with cancer cell markers and phenotypes revealed an association between highly fucosylated glycans and CDX1 and/or villin mRNA expression that both correlate with cell differentiation. Together, our findings provide new insights into CRC-associated glycan changes and setting the basis for more in-depth experiments on glycan function and regulation.

Project description:This data set was downloaded from MetaboLights (http://www.ebi.ac.uk/metabolights/) accession number MTBLS227 Abstract:"Various cancers such as colorectal cancer (CRC) are associated with alterations in protein glycosylation. CRC cell lines are frequently used to study these (glyco)biological changes and their mechanisms. However, differences between CRC cell lines with regard to their glycosylation have hitherto been largely neglected. Here, we comprehensively characterized the N-glycan profiles of 25 different CRC cell lines, derived from primary tumors and metastatic sites, in order to investigate their potential as glycobiological tumor model systems and to reveal glycans associated with cell line phenotypes. We applied an optimized, high-throughput membrane-based enzymatic glycan release for small sample amounts. Released glycans were derivatized to stabilize and differentiate between a2,3- and a2,6-linked N-acetylneuraminic acids, followed by N-glycosylation analysis by MALDI-TOF(/TOF)-MS. Our results showed pronounced differences between the N-glycosylation patterns of CRC cell lines. CRC cell line profiles differed from tissue-derived N-glycan profiles with regard to their high-mannose N-glycan content but showed a large overlap for complex type N-glycans, supporting their use as a glycobiological cancer model system. Importantly, we could show that the high-mannose N-glycans did not only occur as intracellular precursors but were also present at the cell surface. The obtained CRC cell line N-glycan features were not clearly correlated with mRNA expression levels of glycosyltransferases, demonstrating the usefulness of performing the structural analysis of glycans. Finally, correlation of CRC cell line glycosylation features with cancer cell markers and phenotypes revealed an association between highly fucosylated glycans and CDX1 and/or villin mRNA expression that both correlate with cell differentiation. Together, our findings provide new insights into CRC-associated glycan changes and setting the basis for more in-depth experiments on glycan function and regulation."

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Single-cell mapping of the glycocalyx in the adult human and mouse ocular surface

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