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OLIGOSACCHARIDE STORAGE IN BRAINS FROM PATIENTS WITH FUCOSIDOSIS, G M1 ‐GANGLIOSIDOSIS AND G M2 ‐GANGLIOSIDOSIS (SANDHOFF'S DISEASE) 1
Author(s) -
Tsay Grace Chen,
Dawson Glyn
Publication year - 1976
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1976.tb10401.x
Subject(s) - oligosaccharide , glycolipid , fucose , ganglioside , ceramide , chemistry , sandhoff disease , biochemistry , glycosphingolipid , gangliosidosis , disaccharide , hexosaminidase , glycoprotein , neuraminic acid , enzyme , apoptosis
— Analysis of whole autopsy brain from a patient with fucosidosis (α‐fucosidase deficiency) revealed minor storage of H‐antigen glycolipid [Fuc (α, 1→2) Gal‐GlcNAc‐Gal‐Glc‐Ceramide] and a slightly abnormal ganglioside composition in the form of a two‐fold elevation of G M1 and the presence of a fucose‐containing glycolipid (a minor component) which co‐migrated with G D1a . The major storage materials in fucosidosis brain were an oligosaccharide (Fuc‐Gal‐GlcNAc‐Man[Fuc‐Gal‐GlcNAc‐Man]‐ManGlcNAc) and a disaccharide [Fuc(α, 1→6)‐GlcNAc] in the approximate ratio of 5:1. Lesser amounts of a related oligosaccharide (Gal‐GlcNAc‐Man[Gal‐GlcNAc‐Man]‐Man‐GlcNAc) were isolated from the brain of patients with G M1 ‐gangliosidosis (Types I and II) where the major storage material is known to be G M1 ‐ganglioside (Gal (β, 1→3)GalNAc( β , 1→4) [NeuNAcf(α, 2→3) Gal(β, 1→4)Glc‐Ceramide). Similarly, a related oligosaccharide (GlcNAc‐Man [GlcNAc‐Man]‐Man‐GlcNAc) was isolated from the brain of a patient with a total deficiency of N ‐acetyl‐ β ‐ d ‐hexosaminidase (Sandhoff variant of G M2 ‐gangliosidosis) where the major storage products are known to be G M2 ‐ganglioside (GalNAc ( β 1→4) [NeuNAc (α, 2→3)Gal( β , 1→4)Glc‐Ceramine) and its asialo derivative. These studies indicate that glycoproteins containing at least 2 mol of l ‐fucose per oligosaccharide unit are normally catabolized in human brain. Further, it appears that such glycoproteins are initially catabolized by an endo‐ N ‐acetylglucosaminidase to release an oligosaccharide which is then degraded by the sequential action of exo‐glycosidases.