O-GlcNAc glycans in the mammalian extracellular environment.

Extracellular O-GlcNAc is a unique post-translational modification that occurs in the epidermal growth factor-like (EGF) domain of the endoplasmic reticulum (ER) lumen. The EGF domain-specific O-GlcNAc transferase (EOGT), catalyzes the transfer of O-GlcNAc to serine/threonine residues of the C-terminal EGF domain. Thus, EOGT-dependent O-GlcNAc modifications are mainly found in selective proteins that are localized in the extracellular spaces or extracellular regions of membrane proteins.

Clinical implications of cerebral microbleeds in patients who undergo transcatheter aortic valve replacement.

Background: The prognostic implications of cerebral microbleeds (CMBs) in patients who undergo transcatheter aortic valve replacement (TAVR) have not been fully elucidated. Therefore, we aimed to investigate the association between the presence of CMBs and adverse outcomes post-TAVR.

Methods: In this single-center retrospective study, we included 124 patients who underwent brain magnetic resonance imaging before TAVR.

Bidirectional signals generated by Siglec-7 and its crucial ligand tri-sialylated T to escape of cancer cells from immune surveillance.

Siglec-7, an inhibitory receptor expressed on natural killer (NK) cells, recognizes sialic acid-containing glycans. However, the ligand glycan structures of Siglec-7 and its carrier proteins have not been comprehensively investigated. Here, we identified four sialyltransferases that are used for the synthesis of ligand glycans of Siglec-7 and two ligand O-glycan-carrier proteins, PODXL and MUC13, using a colon cancer line.