Chromatograms and Mass Spectra of High-Mannose and Paucimannose -Glycans for Rapid Isomeric Identifications.

-Linked glycosylation is one of the most essential post-translational modifications of proteins. However, -glycan structural determination remains challenging because of the small differences in structures between isomers. In this study, we constructed a database containing collision-induced dissociation MS mass spectra and chromatograms of high-performance liquid chromatography for the rapid identification of high-mannose and paucimannose -glycan isomers.

Identification of the High Mannose -Glycan Isomers Undescribed by Conventional Multicellular Eukaryotic Biosynthetic Pathways.

-linked glycosylation is one of the most important post-translational modifications of proteins. Current knowledge of multicellular eukaryote -glycan biosynthesis suggests high mannose -glycans are generated in the endoplasmic reticulum and Golgi apparatus through conserved biosynthetic pathways. According to conventional biosynthetic pathways, four ManGlcNAc isomers, three ManGlcNAc isomers, and one ManGlcNAc isomer are generated during this process.

Membrane Protein Modification Modulates Big and Small Extracellular Vesicle Biodistribution and Tumorigenic Potential in Breast Cancers In Vivo.

Extracellular vesicles (EVs) are released by cells to mediate intercellular communication under pathological and physiological conditions. While small EVs (sEVs; <100-200 nm, exosomes) are intensely investigated, the properties and functions of medium and large EVs (big EVs (bEVs); >200 nm, microvesicles) are less well explored. Here, bEVs and sEVs are identified as distinct EV populations, and it is determined that bEVs are released in a greater bEV:sEV ratio in the aggressive human triple-negative breast cancer (TNBC) subtype.