Biological Activity
Ganglioside GM1 is a monosialylated ganglioside and the prototypic ganglioside for those containing one sialic acid residue.1,2 It is found in a large variety of cells, including immune cells and neurons, and is enriched in lipid rafts in the cell membrane.3 It associates with growth factor receptors, including TrkA, TrkB, and the GDNF receptor complex containing Ret and GFRα, and is required for TrkA expression on the cell surface. Ganglioside GM1 interacts with other proteins to increase calcium influx, affecting various calcium-dependent processes, including inducing neuronal outgrowth during differentiation. Ganglioside GM1 acts as a receptor for cholera toxin, which binds to its oligosaccharide group, facilitating toxin cell entry into epithelial cells of the jejunum.4,5 Similarly, it is bound by the heat-labile enterotoxin from E. coli in the pathogenesis of traveler's diarrhea.6 Ganglioside GM1 gangliosidosis, characterized by a deficiency in GM1-β-galactosidase, the enzyme that degrades ganglioside GM1, leads to accumulation of the gangliosides GM1 and GA1 in neurons and can be fatal in infants.1 Levels of ganglioside GM1 are decreased in the substantia nigra pars compacta in postmortem brain from patients with Parkinson's disease.3 Ganglioside GM1 mixture contains a mixture of ovine ganglioside GM1 molecular species with primarily C18:0 fatty acyl chain lengths, among various others. [Matreya, LLC. Catalog No. 1544]
References
1.Kolter, T.Ganglioside biochemistryISRN Biochem.506160(2012)
2.Mocchetti, I.Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophinsCell Mol. Life Sci.62(19-20)2283-2294(2005)
3.Ledeen, R.W., and Wu, G.The multi-tasked life of GM1 ganglioside, a true factotum of natureTrends Biochem. Sci.40(7)407-418(2015)
4.Turnbull, W.B., Precious, B.L., and Homans, S.W.Dissecting the cholera toxin-ganglioside GM1 interaction by isothermal titration calorimetryJ. Am. Chem. Soc.126(4)1047-1054(2004)
5.Blank, N., Schiller, M., Krienke, S., et al.Cholera toxin binds to lipid rafts but has a limited specificity for ganglioside GM1Immunol. Cell Biol.85(5)378-382(2007)
6.Minke, W.E., Roach, C., Hol, W.G., et al.Structure-based exploration of the ganglioside GM1 binding sites of Escherichia coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonistsBiochemistry38(18)5684-5692(1999)
