The peripheral myelin glycoprotein P0 expresses the L2/HNK-1 and L3 carbohydrate structures shared by neural adhesion molecules
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Cited by (119)
Evaluation of nanoplastics toxicity to the human placenta in systems
2023, Journal of Hazardous MaterialsCitation Excerpt :It adds a glucuronic residue to the terminal lactosamine residue of a glycoprotein or glycolipid, and can be further sulfated to give the HNK1 epitope. The HNK1 carbohydrate epitope is expressed on a series of cell adhesion molecules where it is involved in cell-cell and cell-substratum interaction during the nervous system development [5]. The binding affinities of all the plastics except PC (–10.4 kcal/mol) were markedly lower than the value obtained by the cocrystallized ligand (–8.7 kcal/mol).
Biological macromolecules acting on central nervous system
2021, Biological Macromolecules: Bioactivity and Biomedical ApplicationsThe role of human natural killer-1 (HNK-1) carbohydrate in neuronal plasticity and disease
2017, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :However, later studies revealed that the HNK-1 epitope is predominantly expressed in the nervous system and is functionally involved in cell adhesion, recognition, and migration [11,13]. During the investigation of HNK-1 epitope function, several glycoproteins carrying the HNK-1 epitope have been identified, such as GPI-anchored proteins including contactin-1, cell adhesion molecules including P0 and NCAM, and extracellular proteins including tenascin-R and tenascin-C [14–18]. To examine the physiological roles of the HNK-1 epitope in mammals, we generated gene-deficient mice of GlcAT-P, a major enzyme in the HNK-1 biosynthetic pathway in the brain.
Anti-myelin associated glycoprotein antibodies recognize HNK-1 epitope on CNS
2011, Journal of NeuroimmunologyCitation Excerpt :In the adult brain, HNK-1 expression is thought to contribute to the maintenance of the perineuronal net, which plays significant roles in neuronal protection, synaptic plasticity, and local ion homeostasis (Celio and Blümcke, 1994). In humans, anti-HNK-1 antibodies cause peripheral nerve damage by binding to MAG and, possibly, to other peripheral nerve HNK-1 bearing components, such as P0, PMP-22, and SGPG (Chou et al., 1986; Bollensen et al., 1987; Burger et al., 1992). Nonetheless, it would be interesting to verify whether these antibodies are also able to recognize HNK-1 within central perineuronal net and possibly cause neuronal dysfunction.
cDNA cloning, genomic structure and chromosomal mapping of the mouse glucuronyltransferase-S involved in the biosynthesis of the HNK-1 carbohydrate epitope
2002, GeneCitation Excerpt :The HNK-1 carbohydrate epitope, which is recognized by an HNK-1 monoclonal antibody, was originally described as a marker of human natural killer cells (Abo and Balch, 1981). The HNK-1 carbohydrate is characteristically expressed in the nervous system on many cell adhesion molecules, such as neural cell adhesion molecules (NCAM), L1 (Kruse et al., 1984), myelin-associated glycoprotein (MAG) (McGarry et al., 1983), telencephalin (Yoshihara et al., 1994), P0 (Bollensen and Schachner, 1987), and others. The epitope is also expressed on two sulfoglucuronyl glycolipids (SGGL-1 and -2) in the nervous system (Chou et al., 1986; Ariga et al., 1987).