title: Role of diacylglycerol and apolipophorin-III in regulation of physiochemical properties of the lipophorin surface: metabolic implications.
abstract: Manduca Sexta adults insects have two defined lipophorin species of densities 1.09 g/mL, [high-density lipophorin (HDLp)] and 1.02 g/mL [low-density lipophorin (LDLp)], respectively, and a continuous broad range of lipophorin particles of intermediate size and density, intermediate-density lipophorin (IDLp). The transformation of HDLp into IDLp and LDLp is the result of the progressive loading of HDLp with diacylglycerol (DG) and an exchangeable apolipoprotein, apolipophorin-III (apoLp-III). In this paper, we describe the physiochemical changes which occur in the lipophorin surface as a result of the transformation of HDLp into LDLp. (1) The increase in apoLp-III content, from 0 to 16 molecules per particle, is accompanied by a gradual increase in the zeta-potential which, at pH 8.6 ranges from /1.02 mV for lipophorins without apoLp-III to -7.76 mV for lipophorins containing 16 molecules of apoLp-III. (2) As judged by the changes in the partition constant for trimethylammonium diphenylhexatriene and oleic acid, an average 2-fold increase in the size of the lipophorin lipid surface takes place when HDLp is loaded with Dg and transformed into LDLp. (3) These data, as well as the results obtained by end point lipolysis with a triacylglycerol (TG) lipase, indicated that the accessible DG content increases 4-7 times when HDLp is converted in LDLp. (4) Fluorescence polarization of the cationic and anionic lipid probes, trimethylammonium diphenylhexatriene and cis-parinaric acid, embedded in eight different subspecies of lipophorin, containing from 12 to 50% DG, showed a small decrease in the surface lipid order when going from HDLp (25% DG) to LDLp (50% DG). (5) Porcine pancreatic phospholipase A2 was used as a probe of the lipoprotein surface. As the DG content of the lipoprotein increased, a higher enzyme activity against the lipoprotein-phospholipids was observed, with a maximum activity 5-fold higher against LDLp than against HDLp. Overall, the changes observed as the lipoprotein particles are loaded with DG and apoLp-III provide a link between the structure and properties of the lipophorin surface and the physiological roles of HDLp and LDLp particles.
authors.affiliation: Department of Biochemistry, University of Arizona, Tuscon 85721, USA.
authors.forename: J L
authors.initials: JL
authors.lastname: Soulages
authors.forename: R
authors.initials: R
authors.lastname: van Antwerpen
authors.forename: M A
authors.initials: MA
authors.lastname: Wells
mesh_terms: D000818:Animals; D001053:Apolipoproteins / Q000097:blood / Q000737:chemistry* / Q000494:pharmacology / Q000648:ultrastructure; D002352:Carrier Proteins / Q000097:blood / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure; D004075:Diglycerides / Q000097:blood / Q000737:chemistry* / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006458:Hemolymph / Q000737:chemistry*; D008074:Lipoproteins / Q000097:blood / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure; D018402:Manduca / Q000737:chemistry; D011199:Potentiometry; D013499:Surface Properties
chemical_list: D001053:Apolipoproteins; D002352:Carrier Proteins; D004075:Diglycerides; D008074:Lipoproteins; C032830:lipophorin