Abstract 127: Structure and Function Relationship of Phospholipid Transfer Protein in Lipid Transfer Activity Revealed by Electron Microscopy

2015 ◽  
Vol 117 (suppl_1) ◽  
Author(s):  
Meng Zhang
Keyword(s):  
Electron Microscopy ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Function Relationship ◽  
Structure And Function Relationship ◽  
And Function ◽  
Relationship Of

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.

Evaluation of phospholipid transfer protein and cholesteryl ester transfer protein as contributors to the generation of preβ-high-density lipoproteins

2001 ◽  
Vol 360 (2) ◽  
pp. 379-385 ◽  
Author(s):  
Jessica LIE ◽  
Rini de CROM ◽  
Matti JAUHIAINEN ◽  
Teus van GENT ◽  
Rien van HAPEREN ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Reverse Cholesterol Transport ◽  
High Density Lipoproteins ◽  
Cholesterol Transport ◽  
Phospholipid Transfer Protein ◽  
Lipid Transfer ◽  
Wild Type ◽  
Lipid Transfer Proteins ◽  
Transfer Protein ◽  
Phospholipid Transfer

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.

Plasma PLTP (phospholipid-transfer protein): an emerging role in ‘reverse lipopolysaccharide transport’ and innate immunity

2011 ◽  
Vol 39 (4) ◽  
pp. 984-988 ◽  
Author(s):  
Thomas Gautier ◽  
Laurent Lagrost
Keyword(s):  
Innate Immunity ◽  
Biological Properties ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Lipid Transfer ◽  
Transport Pathway ◽  
Peripheral Tissues ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Lipoprotein Association

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.

scholarly journals Selective and independent associations of phospholipid transfer protein and hepatic lipase with the LDL subfraction distribution

2002 ◽  
Vol 43 (8) ◽  
pp. 1256-1263 ◽  
Author(s):  
Susan J. Murdoch ◽  
Molly C. Carr ◽  
Hal Kennedy ◽  
John D. Brunzell ◽  
John J. Albers
Keyword(s):  
Hepatic Lipase ◽  
Premenopausal Women ◽  
Plasma Lipoproteins ◽  
Cholesterol Concentration ◽  
Phospholipid Transfer Protein ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Pltp Activity ◽  
Hdl Metabolism ◽  
Relationship Of

Phospholipid transfer protein (PLTP), hepatic lipase (HL), and lipoprotein lipase (LPL) have all been reported to be intricately involved in HDL metabolism but the effect of PLTP on the apolipoprotein B-containing lipoproteins relative to that of HL and LPL has not been established. Due to our previous observation of a positive correlation of PLTP activity with plasma apoB and LDL cholesterol, the relationship of PLTP with the LDL subfractions was investigated and compared with that of HL and LPL. Plasma lipoproteins from 50 premenopausal women were fractionated by density gradient ultracentrifugation. Correlations were calculated between the cholesterol concentration of each fraction and plasma PLTP, HL, and LPL activity. Plasma PLTP activity was highly, positively, and selectively correlated with the cholesterol concentration of the buoyant LDL/dense IDL fractions, yet demonstrated a complete absence of an association with the dense LDL fractions. In contrast, HL was positively correlated with the dense LDL fractions but showed no association with buoyant LDL. LPL was also positively correlated with several buoyant LDL fractions; however, the correlations were weaker than those of PLTP. PLTP and LPL were positively correlated and HL was negatively correlated with HDL fractions.The results suggest that PLTP and HL may be important and independent determinants of the LDL subpopulation density distributions.

scholarly journals Elevated Phospholipid Transfer Protein in Subjects with Multiple Sclerosis

2015 ◽  
Vol 2015 ◽  
pp. 1-5
Author(s):  
Roy A. Garvin
Keyword(s):  
Multiple Sclerosis ◽  
Structural Changes ◽  
Protein A ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Lipid Uptake ◽  
Myelin Lipid ◽  
Transfer Protein ◽  
Transfer Activity ◽  
Phospholipid Transfer

An anomaly in the plasma proteins of patients with multiple sclerosis detectable on SDS-PAGE has been reported. The molecular weight of the anomaly was the same as the phospholipid transfer protein. A metabolic protein was involved in lipid homeostasis and remodeling of the high density lipoproteins. We have identified the anomaly as the phospholipid transfer protein by western blot using antiphospholipid transfer antibodies. Activity assays showed that the phospholipid transfer activity was elevated in fasted plasma samples from subjects with MS compared to controls. Sequence analysis of the gene encoding the phospholipid transfer protein did not identify any mutations in the genetic structure, suggesting that the increase in activity was not due to structural changes in the protein, but may be due to one of the other proteins with which it forms active complexes. Altered phospholipid transfer activity is important because it could be implicated in the decreased lipid uptake and abnormal myelin lipids observed in multiple sclerosis. It has been shown that alteration in myelin lipid content is an epitope for autoimmunity. Therefore, lipid changes due to a defect in phospholipid transfer and/or uptake could potentially influence the course of the disease. Further research is needed to elucidate the role of the phospholipid transfer protein in subjects with multiple sclerosis.

Structure and Function Relationship of Murine Insulin-like Peptide 5 (INSL5): Free C-Terminus Is Essential for RXFP4 Receptor Binding and Activation

Biochemistry ◽  
2011 ◽  
Vol 50 (39) ◽  
pp. 8352-8361 ◽  
Author(s):  
Alessia Belgi ◽  
Mohammed A. Hossain ◽  
Fazel Shabanpoor ◽  
Linda Chan ◽  
Suode Zhang ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Structure And Function ◽  
C Terminus ◽  
Function Relationship ◽  
Structure And Function Relationship ◽  
And Function ◽  
Relationship Of
Sign in / Sign up

Export Citation Format

Share Document