Effect of acidic phospholipids on apolipoprotein binding by artificial lipid particles in vivo.

Abstract

Soybean triacylglycerol particles stabilized with soybean phosphatidylinositol (PI), bovine brain phosphatidylserine (PS), egg yolk phosphatidylcholine (PC) or mixtures of these acidic and neutral phospholipids were prepared with diameters ranging from 250 to 520 nm. Binding of apoproteins to the lipid particles was studied using the strategy of Connelly and Kuksis. The recoveries of the injected particles, which had undergone minimal changes in lipid composition, ranged rom 57% for the PC-stabilized emulsions to 21% for the emulsions stabilized with PS and 8% for the emulsions stabilized with PI. The apoprotein (apo) composition of the recovered particles showed characteristic qualitative and quantitative differences. The particles stabilized with PI and PS or PI-phosphatidylethanolamine contained an unknown protein of molecular weight 117,000 (43-48%) and albumin (9-13%) as major components. The apoC-II, apoC-III, apoA-I, apoE, and apoA-IV were present as minor components in ratios that were the reverse of those seen for the PC-stabilized particles, which contained these proteins as major components. The relative strength of the binding of the proteins, which was determined by washing the particles with saline under standard conditions, also showed variations among the different particles and different apoproteins. The lipid particles stabilized with the acidic phospholipids had less total apoprotein and held it less tightly than the particles stabilized with PC. It is concluded that the binding of apoproteins by lipid particles stabilized with acidic phospholipids involves hydrophobic and ionic interactions, both of which may be physiologically important.