A group from Department of Pulmonary Medicine, Kagoshima University Graduate School of Medical and Dental Sciences, Kagoshima, Japan, etc. has reported about the difference in N-glycan modification of exosomes secreted from small-cell lung carcinomas and non-small-cell lung carcinomas.
Lung cancer is a histologically complex disease that arises from different types of cells in the lungs. Small-cell lung carcinomas (SCLCs) and non-small-cell lung carcinomas (NSCLCs) are the two major lung cancer types classified based upon their histological properties. NSCLCs are further divided into three subtypes, lung adenocarcinomas (LUADs), squamous-cell lung carcinomas (SCCs), and large-cell lung carcinomas (LCCs), in descending order of frequency.
Compared lung cancers are as follows,
SCLC (H446 and SBC-3),
NSCLC-SCC (H520, SK-MES-1, and LK-2), and
Interestingly, the core N-glycan structures showed striking differences between SCLC-small extracellular vesicles(sEVs) and NSCLC-sEVs. NSCLC-sEVs were commonly enriched in bi-antennary and tri-antennary N-glycans, the core fucosylated forms being the major glycan structures. In contrast, the N-glycan profiles of SCLC-sEVs showed considerable heterogeneity, with an enrichment of N-glycans with antennal fucose (73% of total) in H446-sEVs and those with LacdiNAc (40% of total) or bisecting GlcNAc (29% of total) in SBC-3-sEVs.
As almost all N-glycans were sialylated, glycoproteins from the detergent-solubilized sEVs with SSA-conjugated beads and WGA-conjugated beads were pulled down, and the proteins were subjected to shotgun proteomics. The analysis revealed that integrin αV was commonly expressed in sEVs of both cancer cell types, while the epithelium-specific integrin α6β4 heterodimer was selectively expressed in NSCLC-sEVs.