Original Article

Influence of the electrostatic charge of lipoprotein particles on the activity of the human plasma phospholipid transfer protein

Correspondence to: Laurent Lagrost.

The aim of the present study was to determine the effect of the electrostatic charge of lipoproteins on the phospholipid transfer activity of the plasma phospholipid transfer protein (PLTP). Progressive decreases in the PLTP-mediated phospholipid transfer rates were observed when the surface potential of isolated high density lipoproteins (HDL) was either reduced from -11.7 mV down to -15.7 mV by succinylation of apolipoprotein lysyl residues, or increased from -11.6 mV up to -10.9 mV by replacing apolipoprotein (apo) A-I by apoA-II. When succinylated low density lipoprotein (LDL) series with surface potentials ranging between -4.3 mV and -14.3 mV were used, successive increase and decrease in phospholipid transfer rates were observed along the electronegativity scale. When various plasma HDL subfractions with surface potentials ranging from -10.5 mV to -12.5 mV were separated by anion exchange chromatography, PLTP-mediated phospholipid transfer activity increased progressively with HDL electronegativity until maximal lipid transfer rates were reached for a mean HDL surface potential of -11.6 mV. As the electronegativity of plasma HDL subfractions kept increasing beyond the optimal value, a progressive decrease in PLTP activity was observed. Striking parallelism between cholesteryl ester transfer protein (CETP) and PLTP transfer activity curves obtained with each HDL series were noted, and the optimal HDL surface potential values were remarkably similar, approximating -11.6 mV in all the experiments. With isolated plasma LDL subfractions with surface potentials ranging from -3.5 mV to -5.0 mV, a linear rise in PLTP activity was observed.

In conclusion, data of the present study indicate that, like CETP, the activity of PLTP is influenced by electrostatic interactions with lipoproteins.—Desrumaux, C., A. Athias, D. Masson, P. Gambert, C. Lallemant, and L. Lagrost. Influence of the electrostatic charge of lipoprotein particles on the activity of the human plasma phospholipid transfer protein. J. Lipid Res. 1998. 39: 131–142.

Supplementary key words: CETP, PLTP, surface potential, electronegativity, HDL, LDL

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Settasatian, P. J. Barter, and K.-A. Rye Remodeling of apolipoprotein E-containing spherical reconstituted high density lipoproteins by phospholipid transfer protein J. Lipid Res., January 1, 2008; 49(1): 115 - 126. [Abstract] [Full Text] [PDF]

				M. K. Wu and D. E. Cohen Phosphatidylcholine transfer protein regulates size and hepatic uptake of high-density lipoproteins Am J Physiol Gastrointest Liver Physiol, December 1, 2005; 289(6): G1067 - G1074. [Abstract] [Full Text] [PDF]

				L. Dumont, T. Gautier, J.-P. P. de Barros, H. Laplanche, D. Blache, P. Ducoroy, J. Fruchart, J.-C. Fruchart, P. Gambert, D. Masson, et al. Molecular Mechanism of the Blockade of Plasma Cholesteryl Ester Transfer Protein by Its Physiological Inhibitor Apolipoprotein CI J. Biol. Chem., November 11, 2005; 280(45): 38108 - 38116. [Abstract] [Full Text] [PDF]

				F. Lalanne, C. Motta, Y. Pafumi, D. Lairon, and G. Ponsin Modulation of the phospholipid transfer protein-mediated transfer of phospholipids by diacylglycerols J. Lipid Res., January 1, 2001; 42(1): 142 - 149. [Abstract] [Full Text]

				S. Braschi, T. A-M. Neville, M.-C. Vohl, and D. L. Sparks Apolipoprotein A-I charge and conformation regulate the clearance of reconstituted high density lipoprotein in vivo J. Lipid Res., March 1, 1999; 40(3): 522 - 532. [Abstract] [Full Text]

				C. Desrumaux, C. Labeur, A. Verhee, J. Tavernier, J. Vandekerckhove, M. Rosseneu, and F. Peelman A Hydrophobic Cluster at the Surface of the Human Plasma Phospholipid Transfer Protein Is Critical for Activity on High Density Lipoproteins J. Biol. Chem., February 16, 2001; 276(8): 5908 - 5915. [Abstract] [Full Text] [PDF]