Interfacial and Lipid Transfer Properties of Human Phospholipid Transfer Protein:  Implications for the Transfer Mechanism of Phospholipids†

Biochemistry ◽  
2007 ◽  
Vol 46 (5) ◽  
pp. 1312-1319 ◽  
Author(s):  
Niko L. Setälä ◽  
Juha M. Holopainen ◽  
Jari Metso ◽  
Susanne K. Wiedmer ◽  
Gebrenegus Yohannes ◽  
...  
2007 ◽  
Vol 149 ◽  
pp. S88-S89
Author(s):  
Niko Setälä ◽  
Jari Metso ◽  
Susanne Wiedmer ◽  
Gebrenegus Yohannes ◽  
Paavo Kinnunen ◽  
...  

2016 ◽  
Vol 291 (46) ◽  
pp. 24280-24292 ◽  
Author(s):  
Ross J. Hill ◽  
Alessa Ringel ◽  
Ellen Knuepfer ◽  
Robert W. Moon ◽  
Michael J. Blackman ◽  
...  

2015 ◽  
Vol 117 (suppl_1) ◽  
Author(s):  
Meng Zhang

Human phospholipid transfer protein (PLTP) mediates the transfer of lipids among atheroprotective high-density lipoproteins (HDL) and atherogenic low-density lipoproteins (LDL) by an unknown mechanism. Delineating this mechanism would be an important step toward the understanding and regulation of PLTP for treating cardiovascular diseases, hypoalphalipoproteinemia and hyperalphalipoproteinemia. Using electron microscopy, negative-staining, and single-particle image processing, we discovered that PLTP penetrates each class of HDL, LDL and liposome independently, and also bridges a ternary complex with one of its distal end-domains penetrating into HDL and another distal domain interacting with LDL. These new insights into PLTP interaction with lipoproteins and liposomes provide a molecular basis for analyzing PLTP-dependent lipid transfer between lipoprotein particles.


2001 ◽  
Vol 360 (2) ◽  
pp. 379-385 ◽  
Author(s):  
Jessica LIE ◽  
Rini de CROM ◽  
Matti JAUHIAINEN ◽  
Teus van GENT ◽  
Rien van HAPEREN ◽  
...  

High-density lipoproteins (HDLs) are considered anti-atherogenic because they mediate peripheral cell cholesterol transport to the liver for excretion and degradation. An important step in this reverse cholesterol-transport pathway is the uptake of cellular cholesterol by a specific subclass of small, lipid-poor apolipoprotein A-I particles designated preβ-HDL. The two lipid-transfer proteins present in human plasma, cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP), have both been implicated in the formation of preβ-HDL. In order to investigate the relative contribution of each of these proteins, we used transgenic mouse models. Comparisons were made between human CETP transgenic mice (huCETPtg), human PLTP transgenic mice (huPLTPtg) and mice transgenic for both lipid-transfer proteins (huCETPtg/huPLTPtg). These animals showed elevated plasma levels of CETP activity, PLTP activity or both activities, respectively. We evaluated the generation of preβ-HDL in mouse plasma by immunoblotting and crossed immuno-electrophoresis. Generation of preβ-HDL was equal in huCETPtg and wild-type mice. In contrast, in huPLTPtg and huCETPtg/huPLTPtg mice, preβ-HDL generation was 3-fold higher than in plasma from either wild-type or huCETPtg mice. Our findings demonstrate that, of the two plasma lipid-transfer proteins, PLTP rather than CETP is responsible for the generation of preβ-HDL. These data support the hypothesis of a role for PLTP in the initial stage of reverse cholesterol transport.


2011 ◽  
Vol 39 (4) ◽  
pp. 984-988 ◽  
Author(s):  
Thomas Gautier ◽  
Laurent Lagrost

Plasma PLTP (phospholipid-transfer protein) is a member of the lipid transfer/LBP [LPS (lipopolysaccharide)-binding protein] family, which constitutes a superfamily of genes together with the short and long PLUNC (palate, lung and nasal epithelium clone) proteins. Although PLTP was studied initially for its involvement in the metabolism of HDL (high-density lipoproteins) and reverse cholesterol transport (i.e. the metabolic pathway through which cholesterol excess can be transported from peripheral tissues back to the liver for excretion in the bile), it displays a number of additional biological properties. In particular, PLTP can modulate the lipoprotein association and metabolism of LPS that are major components of Gram-negative bacteria. The delayed association of LPS with lipoproteins in PLTP-deficient mice results in a prolonged residence time, in a higher toxicity of LPS aggregates and in a significant increase in LPS-induced mortality as compared with wild-type mice. It suggests that PLTP may play a pivotal role in inflammation and innate immunity through its ability to accelerate the ‘reverse LPS transport’ pathway.


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