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Correspondence to:
Daniel L. Sparks, To whom correspondence should be addressed.
The effects of different acylglycerides on the conformation and charge of apolipoprotein A-I (apoA-I) have been investigated in reconstituted high density lipoproteins (LpA-I). Various amounts of diacylglycerol (DG) and triacylglycerol (TG) were incorporated into sonicated spherical LpA-I particles containing 2 molecules of apoA-I and 80 molecules of phospholipid. Inclusion of 30 molecules of TG into the LpA-I particle increases the net negative charge of apoA-I (-8.5 to -9.3 mV), but has little effect on the amount and thermodynamic stability of the
The data show that TG and DG have different effects on apoA-I structure and function and this suggests that the TG-to-DG ratio in HDL may directly affect the metabolism of this lipoprotein class. Braschi, S., C. R. Coffill, T. A-M. Neville, D. M. Hutt, and D. L. Sparks. Effect of acylglyceride content on the structure and function of reconstituted high density lipoprotein particles. J. Lipid Res. 2001. 42: 79;87.
Supplementary key words:
HDL, apolipoprotein A-I, diglyceride, triglyceride, charge, stability, conformation, immunochemistry, LCAT
Copyright © 2001 by Lipid Research, Inc.
Original Article
Effect of acylglyceride content on the structure and function of reconstituted high density lipoprotein particles
Sylvie Braschib,
Cynthia R. Coffillc,
Tracey A-M. Nevillea,
Darren M. Huttd, and
Daniel L. Sparksa
a Lipoprotein and Atherosclerosis Research Group, University of Ottawa Heart Institute, Ottawa, Ontario, K1Y 4W7, Canada
b Université de Paris XII and Service de Medecine Interne V, Hôpital Henri Mondor, 94010 Creteil, France
c Molecular Genetics Laboratory, Research Institute, CHEO, Ottawa, Ontario, K1H 8L1, Canada
d Loeb Medical Research Institute, Civic Hospital, Ottawa, Ontario, K1Y 4E9, Canada
helices in apoA-I. Incorporation of 30 molecules of DG into the lipoprotein complex promotes a small increase in the
-helix content and stability, but greatly increases the net negative charge of apoA-I (-8.5 to -11.2 mV). Inclusion of DG increases the immunoreactivity of two epitopes in the N terminus of apoA-I, but decreases the exposure of a domain closer to the C terminus (residues 148;186) of the apoprotein. In contrast, TG increases the exposure of epitopes over the entire apoA-I molecule; TG increases the immunoreactivity of epitopes for 13 different monoclonal antibodies to apoA-I. Incubations with purified lecithin:cholesterol acyltransferase show that cholesterol esterification is stimulated by DG, but inhibited by TG. ![]()
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