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Effect of sphingomyelinase-mediated generation of ceramide on aggregation of low-density lipoprotein
Journal article   Peer reviewed

Effect of sphingomyelinase-mediated generation of ceramide on aggregation of low-density lipoprotein

Michael J Walters and Steven P Wrenn
Langmuir, v 24(17), pp 9642-9647
02 Sep 2008
PMID: 18671414

Abstract

Lipoproteins, LDL - chemistry Sphingomyelin Phosphodiesterase - chemistry Models, Chemical Ceramides - chemistry Models, Statistical Magnesium - chemistry Time Factors Light Surface Properties Phosphorylcholine - chemistry Sphingomyelins - chemistry Scattering, Radiation Kinetics Biophysics - methods
This study addresses the response-to-retention hypothesis, which states that the subendothelial retention of atherogenic lipoproteins is the necessary and sufficient condition for the initiation of atherosclerosis. Here we focus on the relationship between the generation of ceramide in the low-density lipoprotein (LDL) phospholipid monolayer and the resulting aggregation of LDL particles. This study provides the first measurement of neutral, Mg (2+)-dependent Sphingomyelinase (Smase)-mediated ceramide formation from LDL-sphingomyelin and does so for a range of enzyme concentrations (0-0.22 units Smase/mL). The kinetics of ceramide generation was measured using a fluorescence assay for the above enzyme concentrations with a fixed substrate concentration (0.33 mg LDL/mL). The kinetics of LDL aggregate formation was measured by dynamic light scattering (DLS, method of cumulants) for identical enzyme concentrations. Ceramide concentration profiles were fit with a modification of the Michaelis-Menten model ( k a = 1.11 x 10 (-1) microM (-1) min (-1), k -a = 6.54 x 10 (2) microM (-1) min (-1), k 1 = 3.33 x 10 (1) microM (-1) min (-1), k -1 = 1.41 x 10 (-2) min (-1), k cat = 8.05 x 10 (1) min (-1), K M = 2.418 microM, k deact = 4.66 x 10 (-2) microM (-1) min (-1)) that accounts for the effects of enzyme attachment to the LDL monolayer and for deactivation of Smase due to product inhibition. LDL aggregation is described by a mass action model as explained in previous studies. A key result of this work is the finding that LDL aggregate size depends directly on ceramide concentration and is independent of enzyme concentration. This study demonstrates how principles of colloid science are relevant to important biomedical problems.

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Web of Science research areas
Chemistry, Multidisciplinary
Chemistry, Physical
Materials Science, Multidisciplinary
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