Characterization of human apolipoprotein B100 oligosaccharides in LDL subfractions derived from normal and hyperlipidemic plasa: deficiency of alpha-N-acetylneuraminyllactosyl-ceramide in light and small dense LDL particles
B. Garner et al., Characterization of human apolipoprotein B100 oligosaccharides in LDL subfractions derived from normal and hyperlipidemic plasa: deficiency of alpha-N-acetylneuraminyllactosyl-ceramide in light and small dense LDL particles, GLYCOBIOLOG, 11(10), 2001, pp. 791-802
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 no
rmolipidemic, hypercholesterolemic, and hypertriglyceridemic diabetic subje
cts. Using exoglycosidase carbohydrate sequencing and matrix-assisted laser
desorption/ionization mass spectrometry to analyze fluorescently labeled o
ligosaccharides, we report evidence for several carbohydrates not previousl
y 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 compositi
on 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 hypercholesterolemi
c subjects. Furthermore, we found no evidence for "desialylated" apoB100 gl
ycans in any of the samples analyzed. Analysis of the most abundant LDL gan
glioside, alpha-N-acetylneuraminyllactosyl-ceramide, revealed a deficiency
in small dense LDL and in the most buoyant subpopulation. These data provid
e a novel explanation for the apparent deficiency of sialic acid in small d
ense LDL and indicate that the global apoB100 N-glycan composition is invar
iable in the patient groups studied.