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Levels of anti-GM1 antibodies are especially elevated in patients with prodromal diarrhea. [7] Titers to GM1 in other diseases (rheumatoid arthritis, primary Sjögren's syndrome and systemic lupus erythematosus) was also elevated. [8] Additionally highly significant association was found with rheumatoid arthritis and peripheral neuropathies. [9]
The GM1 gangliosidoses, usually shortened to GM1, are gangliosidoses caused by mutation in the GLB1 gene resulting in a deficiency of beta-galactosidase.The deficiency causes abnormal storage of acidic lipid materials in cells of the central and peripheral nervous systems, but particularly in the nerve cells, resulting in progressive neurodegeneration.
Structure of GM1 ganglioside. A ganglioside is a molecule composed of a glycosphingolipid (ceramide and oligosaccharide) with one or more sialic acids (e.g. N-acetylneuraminic acid, NANA) linked on the sugar chain.
GM1 has important physiological properties and impacts neuronal plasticity and repair mechanisms, and the release of neurotrophins in the brain. Besides its function in the physiology of the brain, GM1 acts as the site of binding for both cholera toxin and E. coli heat-labile enterotoxin ( Traveller's diarrhea ).
Autoimmune autonomic ganglionopathy is a type of immune-mediated autonomic failure that is associated with antibodies against the ganglionic nicotinic acetylcholine receptor present in sympathetic, parasympathetic, and enteric ganglia.
Bacterial neuraminidase is type of neuraminidase and a virulence factor for many bacteria including Bacteroides fragilis and Pseudomonas aeruginosa.Its function is to cleave a sialic acid residue off ganglioside-GM1 (a modulator of cell surface and receptor activity) turning it into asialo-GM1 to which type 4 pili (attachment factors) bind preferentially.
The asialoglycoprotein receptor was first characterized in 1968 by Morell et al. and was the first mammalian lectin identified. [1] The researchers transferred radioactively-labeled ceruloplasmin that had undergone a reaction via the enzyme neuraminidase to remove the protein's terminal sialic acid, [6] generating an asialoglycoprotein.
Structures of GM1, GM2, GM3 gangliosides. References External links. Ganglioside+GM2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH ...