Interaction of lipoprotein lipase and apolipoprotein C-II with sonicated vesicles of 1,2-ditetradecylphosphatidylcholine: comparison of binding constants.

  title={Interaction of lipoprotein lipase and apolipoprotein C-II with sonicated vesicles of 1,2-ditetradecylphosphatidylcholine: comparison of binding constants.},
  author={Larry R. McLean and Richard L. Jackson},
  volume={24 15},
The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy. A complex of 320 molecules of C14-ether-PC per LpL was isolated by density gradient ultracentrifugation in KBr. The intrinsic tryptophan fluorescence emission spectrum of LpL was shifted from 336 nm in the absence of lipid to 330 nm in the LpL-lipid… 

Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure.

These data demonstrate that LpL binds to the surface of a lipid interface, without dramatic changes in lipid bilayer or protein structure.

Specificity of the lipid-binding domain of apoC-II for the substrates and products of lipolysis.

The difference in the extent of protein adsorption to lipid classes suggests that the distribution of apoC-II among lipoproteins will depend on their lipid composition and surface pressure.

Ether phosphatidylcholines: comparison of miscibility with ester phosphatidylcholines and sphingomyelin, vesicle fusion, and association with apolipoprotein A-I.

The fusion of small single bilayer vesicles of DMPC, DMPC-ether, DPPC, and DPPC- ether to larger aggregates as determined by gel filtration indicated that the ester PC vesicle were somewhat more stable, and little preference of cholesterol for either lipid.

Interaction of lipoprotein lipase with homogeneous lipid emulsions.

The binding of purified milk lipoprotein lipase to homogeneous synthetic lipid emulsions shows close packing of LpL on the lipid surface and is consistent with there being little disruption to the overall structure of the emulsion particle.

Interactions between fatty acids and lipoprotein lipase: specific binding and complex formation.

Examination of the binding of fatty acids to LpL and factors that must be considered when the dissociation constant of the acceptor-ligand equilibrium is close to the critical micelle concentration of the fatty acid indicates that at higher concentrations of fatty acid, large complexes are formed consisting of 260-310 molecules of fatty Acid per LPL monomer.

A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II*

The results suggest that apoC-II regulates the activity of LPL in a pressure-dependent manner and is provided as a component of triacylglycerol-rich lipoproteins and is the co-factor for LPL as pressure increases.

Effects of Nonsubstrate Lipids on Acylhydrolase Activities of Lipoprotein and Hepatic Lipases Using Defined Emulsion Particles

Hydrolysis of triolein and egg phosphatidylcholine in emulsion particles by purified bovine milk lipoprotein lipase and by rat hepatic lipase was studied and non-substrate lipids in chylomicrons may aid its catalysis by LPL while impeding HL.



Lipoprotein lipase-catalyzed hydrolysis of phosphatidylcholine of guinea pig very low density lipoproteins and discoidal complexes of phospholipid and apolipoprotein: effect of apolipoprotein C-II on the catalytic mechanism.

To elucidate the mechanism by which apolipoprotein C-II (apoC-II) enhances the activity of lipoprotein lipase (LpL), discoidal phospholipid complexes were prepared with apoC-III and

Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation.

: The reversibility of the binding of human apolipoprotein A-I (apo A-I) to phospholipid has been monitored through the influence of guanidine hydrochloride (Gdn-HCl) on the isothermal denaturation

Mechanism of action of milk lipoprotein lipase at substrate interfaces: effects of apolipoproteins.

The mechanism of action of bovine milk lipoprotein lipase was studied by using a monomolecular film of 1,2-didecanoylglycerol and all of the proteins, with the exception of colipase, gave increased enzyme activity compared to lipase alone; apoC-II gave maximal activation.

Hydrolysis of guinea pig nascent very low density lipoproteins catalyzed by lipoprotein lipase: activation by hjman apolipoprotein C-II.

Based on a simple kinetic model, the data suggest that apoC-II favors direct interaction between enzyme and triglyceride within the lipoprotein particle, as well as subsequent catalytic turnover.