Increased α-2,6 sialic acid on microglia in amyloid pathology is resistant to oseltamivir.

ABSTRACT: Terminal sialic acid residues are present on most glycoproteins and glycolipids, but levels of sialylation are known to change in the brain throughout the lifespan as well as during disease. Sialic acids are important for numerous cellular processes including cell adhesion, neurodevelopment, and immune regulation as well as pathogen invasion into host cells. Neuraminidase enzymes, also known as sialidases, are responsible for removal of terminal sialic acids in a process known as desialylation. Neuraminidase 1 (Neu1) cleaves the α-2,6 bond of terminal sialic acids. Aging individuals with dementia are often treated with the antiviral medication oseltamivir, which is associated with induction of adverse neuropsychiatric side effects; this drug inhibits both viral and mammalian Neu1. The pres

SUBMITTER: Fastenau C 

PROVIDER: S-EPMC10400525 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature