Gangliosides are major constituents of neuronal cell membranes and endoplasmic reticulum; contain a sialated polysaccharide chain linked to ceramide through a β-glycosidic linkage; for classification of gangliosides see Svennerholm, L., et al. (eds.), Structure and Function of Gangliosides, New York, Plenum, 1980.
Biochem/physiol Actions
Degraded form of Asialoganglioside-GM1 ganglioside.
The glycosphingolipids (GSLs) gangliotriaosylceramide (Gg(3)) and gangliotetraosylceramide (Gg(4)) have been implicated as receptors for type IV pili (T4P)-mediated Pseudomonas aeruginosa epithelial cell attachment. Since P. aeruginosa T4P are divided into five groups, the authors determined whether GSLs in general, and
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 47(8), 1005-1014 (1999-07-29)
A radioactive and biotin-labeled analogue of GM1 (biotin-GM1) was synthesized which enabled us to analyze its intracellular distribution in the compartments of the endocytic route by electron microscopic immunocytochemistry using thin sections of human skin fibroblasts labeled with gold-conjugated antibiotin
Medical microbiology and immunology, 191(1), 5-10 (2002-07-26)
Moraxella catarrhalis is an important pathogen of respiratory and middle ear infections. We previously reported that the attachment of M. catarrhalis to pharyngeal epithelial cells is mediated by ganglioside M2 (GM2). Several sets of adhesins or receptors are involved in
European journal of biochemistry, 230(3), 971-976 (1995-06-15)
Glycosphingolipids were extracted from the brain of house musk shrew (Suncus murinus). Neutral glycosphingolipids were purified by QAE-Sephadex column chromatography followed by high-performance liquid chromatography using an Iatrobeads column. Purified glycosphingolipids were identified by high-performance thin-layer chromatography, carbohydrate analysis, fast-atom
Archives of biochemistry and biophysics, 374(1), 93-99 (2000-01-21)
Cell adhesion and spreading on solid phase fibronectin (FN), coated on plate or presented in extracellular matrix, are mediated by integrin receptors alpha5beta1, alpha4beta1, etc., although binding of "soluble-form FN" to cell surface varies extensively depending on glycosylation status of
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