Concept

N-Acetylgalactosamine

N-Acetylgalactosamine (GalNAc), is an amino sugar derivative of galactose. In humans it is the terminal carbohydrate forming the antigen of blood group A. It is typically the first monosaccharide that connects serine or threonine in particular forms of protein O-glycosylation. N-Acetylgalactosamine is necessary for intercellular communication, and is concentrated in sensory nerve structures of both humans and animals. GalNAc is also used as a targeting ligand in investigational antisense oligonucleotides and siRNA therapies targeted to the liver, where it binds to the asialoglycoprotein receptors on hepatocytes.

Official source

https://en.wikipedia.org/wiki/N-Acetylgalactosamine

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Related publications (2)

N-glycosylation modulates the inactivation kinetics of the Kv3.4 ion channel

In our previous study, when mapping the kinetics of all 40 genetic subtypes of the voltage-gated potassium (Kv) family of ion channels, we observed significant heterogeneity in the inactivation delay of Kv3.4. Kv3.4 enables high-frequency firing in excitable cells and is linked to disorders such as Alzheimer's disease, epilepsy, chronic pain, and cardiovascular disease. In this study, we found that N-glycosylation, a co- and post-translational process of adding glycans branches to proteins, is a key mechani

2025

Differential dependence on N-glycosylation of anthrax toxin receptors CMG2 and TEM8

ANTXR 1 and 2, also known as TEM8 and CMG2, are two type I membrane proteins, which have been extensively studied for their role as anthrax toxin receptors, but with a still elusive physiological function. Here we have analyzed the importance of N-glycosylation on folding, trafficking and ligand binding of these closely related proteins. We find that TEM8 has a stringent dependence on N-glycosylation. The presence of at least one glycan on each of its two extracellular domains, the vWA and Ig-like domains,

Public Library of Science2015

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