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A more recent version of this article appeared on August 1, 2005

Papers In Press, published online ahead of print June 1, 2005
J. Lipid Res., doi:10.1194/jlr.M400434-JLR200
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Submitted on October 30, 2004
Revised on May 6, 2005
Accepted on May 23, 2005

Integral apolipoproteins increase surface-located triacylglycerol in intact native apo-protein B100 containing lipoproteins

Elizabeth L. Boyle-Roden and Rosemary L. Walzem

Department of Chemistry, Ohio State University, Columbus, OH 43120

Corresponding Author: eboyle-r{at}chemistry.ohio-state.edu

High resolution NMR was used to measure the presence and quantity of triacylglycerol (TAG) in the surface of intact native apoB-100-containing lipoprotein particles that are made by chickens in response to estrogen treatment, and which in hens are deposited in yolk follicles (VLDLy). Integation of 13C NMR resonances shows that intact VLDLy particles contain more surface TAG (5.1 ± 0.6 mol %, 6.7 ± 0.8 wt %) than predicted by apoprotein-free models using similarly acyl-heterogenous TAG. Change in downfield chemical shift values (delta delta ) of surface to core TAG in VLDLy was 0.8 ppm as compared to 1.3 ppm in vesicles prepared with purified egg PC and TAG isolated from the VLDLy and indicates that reduced surface TAG hydration may contribute to the resistance to lipase hydrolysis characteristic of this lipoprotein species. Apolipoprotein-mediated changes in surface lipid composition and lipid hydration provide possible general mechanisms for selectivity in lipoprotein substrate characteristics.


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[Abstract] [Full Text] [PDF]


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