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Glycobiology, 2001, Vol. 11, No. 10 791-802
© 2001 Oxford University Press

Characterization of human apolipoprotein B100 oligosaccharides in LDL subfractions derived from normal and hyperlipidemic plasma: deficiency of {alpha}-N-acetylneuraminyllactosyl-ceramide in light and small dense LDL particles

Brett Garner1,2, David J. Harvey2, Louise Royle2, Michael Frischmann3, Fabienne Nigon4, M. John Chapman4 and Pauline M. Rudd2

2Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; 3Institute of Medical Biology and Human Genetics, University of Innsbruck, 6020 Innsbruck, Austria; and 4INSERM Unit 321, Pavillon Benjamin Delessert, Hopital de la Pitie, 75651 Paris, Cedex 13, France

The carbohydrate composition of apolipoprotein (apo) B100, particularly its degree of sialylation, may contribute to the atherogenic properties of low-density lipoprotein (LDL). We analyzed LDL apoB100 glycans derived from normolipidemic, hypercholesterolemic, and hypertriglyceridemic diabetic subjects. Using exoglycosidase carbohydrate sequencing and matrix-assisted laser desorption/ionization mass spectrometry to analyze fluorescently labeled oligosaccharides, we report evidence for several carbohydrates not previously identified on apoB100, including truncated complex biantennary N-glycans and hybrid N-glycans. The distribution and diversity of the apoB100 glycans isolated from all individuals was highly conserved. The N-glycan composition of apoB100 derived from five LDL subpopulations (LDL1, d = 1.018–1.023; LDL2, d = 1.023–1.030; LDL3, d = 1.030–1.040; LDL4, d = 1.040–1.051; LDL5, d = 1.051–1.065 g/ml) did not vary in normolipidemic or hypercholesterolemic subjects. Furthermore, we found no evidence for "desialylated" apoB100 glycans in any of the samples analyzed. Analysis of the most abundant LDL ganglioside, {alpha}-N-acetylneuraminyllactosyl-ceramide, revealed a deficiency in small dense LDL and in the most buoyant subpopulation. These data provide a novel explanation for the apparent deficiency of sialic acid in small dense LDL and indicate that the global apoB100 N-glycan composition is invariable in the patient groups studied.

1 To whom correspondence should be addressed


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A. Harazono, N. Kawasaki, T. Kawanishi, and T. Hayakawa
Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS
Glycobiology, May 1, 2005; 15(5): 447 - 462.
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