scholarly journals Plasma phospholipid transfer protein enhances transfer and exchange of phospholipids between very low density lipoproteins and high density lipoproteins during lipolysis.

1985 ◽  
Vol 26 (7) ◽  
pp. 842-851
Author(s):  
A R Tall ◽  
S Krumholz ◽  
T Olivecrona ◽  
R J Deckelbaum
Keyword(s):  
Plasma Phospholipid ◽  
Low Density Lipoproteins ◽  
High Density ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Transfer Protein ◽  
Phospholipid Transfer

scholarly journals Phospholipid transfer protein activity in two cholestatic patients

2004 ◽  
Vol 122 (4) ◽  
pp. 175-177 ◽  
Author(s):  
Eliana Cotta de Faria ◽  
Adriana Celeste Gebrin ◽  
Wilson Nadruz Júnior ◽  
Lucia Nassi Castilho
Keyword(s):  
Density Lipoprotein ◽  
Plasma Phospholipid ◽  
Low Density Lipoproteins ◽  
High Density ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Low Density ◽  
Protein Activity ◽  
Transfer Protein ◽  
Phospholipid Transfer

CONTEXT: Plasma phospholipid transfer protein mediates the transfer of phospholipids from triglyceride-rich lipoproteins, very low density lipoproteins and low density lipoproteins to high density lipoproteins, a process that is also efficient between high density lipoprotein particles. It promotes a net movement of phospholipids, thereby generating small lipid-poor apolipoprotein AI that contains particles and subfractions that are good acceptors for cell cholesterol efflux. CASE REPORT: We measured the activity of plasma phospholipid transfer protein in two cholestatic patients, assuming that changes in activity would occur in serum that was positive for lipoprotein X. Both patients presented severe hypercholesterolemia, high levels of low density lipoprotein cholesterol and, in one case, low levels of high density lipoprotein cholesterol and high levels of phospholipid serum. The phospholipid transfer activity was close to the lower limit of the reference interval. To our knowledge, this is the first time such results have been presented. We propose that phospholipid transfer protein activity becomes reduced under cholestasis conditions because of changes in the chemical composition of high density lipoproteins, such as an increase in phospholipids content. Also, lipoprotein X, which is rich in phospholipids, could compete with high density lipoproteins as a substrate for phospholipid transfer protein.

Plasma phospholipid transfer protein and the anti-atherogenic potential of high density lipoproteins

2000 ◽  
Vol 151 (1) ◽  
pp. 182
Author(s):  
A. Van Tol ◽  
P.S. Vermeulen ◽  
M. Jauhiainen ◽  
R. Van Haperen ◽  
T. Van Gent ◽  
...  
Keyword(s):  
Plasma Phospholipid ◽  
High Density ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Transfer Protein ◽  
Phospholipid Transfer

scholarly journals Lipopolysaccharide Is Transferred from High-Density to Low-Density Lipoproteins by Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein

2005 ◽  
Vol 73 (4) ◽  
pp. 2321-2326 ◽  
Author(s):  
J. H. M. Levels ◽  
J. A. Marquart ◽  
P. R. Abraham ◽  
A. E. van den Ende ◽  
H. O. F. Molhuizen ◽  
...  
Keyword(s):  
Acute Phase ◽  
Binding Protein ◽  
Low Density Lipoproteins ◽  
High Density ◽  
Phospholipid Transfer Protein ◽  
Low Density ◽  
Lipoprotein Subclasses ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Dose Dependent

ABSTRACT Lipopolysaccharide (LPS), the major outer membrane component of gram-negative bacteria, is a potent endotoxin that triggers cytokine-mediated systemic inflammatory responses in the host. Plasma lipoproteins are capable of LPS sequestration, thereby attenuating the host response to infection, but ensuing dyslipidemia severely compromises this host defense mechanism. We have recently reported that Escherichia coli J5 and Re595 LPS chemotypes that contain relatively short O-antigen polysaccharide side chains are efficiently redistributed from high-density lipoproteins (HDL) to other lipoprotein subclasses in normal human whole blood (ex vivo). In this study, we examined the role of the acute-phase proteins LPS-binding protein (LBP) and phospholipid transfer protein (PLTP) in this process. By the use of isolated HDL containing fluorescent J5 LPS, the redistribution of endotoxin among the major lipoprotein subclasses in a model system was determined by gel permeation chromatography. The kinetics of LPS and lipid particle interactions were determined by using Biacore analysis. LBP and PLTP were found to transfer LPS from HDL predominantly to low-density lipoproteins (LDL), in a time- and dose-dependent manner, to induce remodeling of HDL into two subpopulations as a consequence of the LPS transfer and to enhance the steady-state association of LDL with HDL in a dose-dependent fashion. The presence of LPS on HDL further enhanced LBP-dependent interactions of LDL with HDL and increased the stability of the HDL-LDL complexes. We postulate that HDL remodeling induced by LBP- and PLTP-mediated LPS transfer may contribute to the plasma lipoprotein dyslipidemia characteristic of the acute-phase response to infection.

scholarly journals A Molecular and Biochemical Study for Cholesteryl Ester Transfer Protein (CETP) Taq1B in Iraqi Patients with Hyperlipidemia

2019 ◽  
Vol 16 (3(Suppl.)) ◽  
pp. 0747
Author(s):  
Alkhafajy Et al.
Keyword(s):  
Cholesteryl Ester ◽  
Total Cholesterol ◽  
Cholesteryl Ester Transfer Protein ◽  
Serum Lipid ◽  
Low Density Lipoproteins ◽  
High Density ◽  
High Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Transfer Protein

Cholesteryl ester transfer protein gene contains some single nucleotide polymorphisms, which have been associated with serum high-density lipoprotein concentration and other lipoproteins. This study is done for determining of cholesteryl ester transfer protein polymorphism and evaluate its effect on serum lipid profile concentrations in some hyperlipidemic patients compared with healthy subjects in Salah Al-din governorate-Iraq. Blood samples were taken from (90) patients suffering from hyperlipidemia, and (70) samples that were apparently healthy controls.  Serum lipid concentrations were measured by enzymatic assays. The polymorphism was genotyped using polymerase chain reaction restriction fragment length polymorphism analysis.  The results showed that there was a significant decrease (P<0.05) in the frequency B2 allele, and B1B2, B2B2 genotype, and a significant increase (P<0.05) in the frequency B1 allele, and B1B1 genotype between patients and controls groups. There was a non-significant decrease in the levels of high density lipoproteins, total cholesterol, low density lipoproteins, and very low density lipoproteins levels, and non-significant increase in levels of triglycerides in individuals with the B1B1 genotype than in the B1B2 and B2B2 genotype. However, high density lipoproteins showed a significant decrease (P<0.001) between individuals with the B1B1 genotype and B2B2 genotype. Also, there was a non-significant difference in the levels of high density lipoproteins, total cholesterol, low density lipoproteins, and very low density lipoproteins levels, in individuals with the B1B2 genotype when compared with that of the B2B2 genotype.

scholarly journals Human plasma phospholipid transfer protein accelerates exchange/transfer of α-tocopherol between lipoproteins and cells

1995 ◽  
Vol 305 (2) ◽  
pp. 659-667 ◽  
Author(s):  
G M Kostner ◽  
K Oettl ◽  
M Jauhiainen ◽  
C Ehnholm ◽  
H Esterbauer ◽  
...  
Keyword(s):  
Serum Lipoprotein ◽  
Alpha Tocopherol ◽  
Plasma Lipoproteins ◽  
High Density Lipoproteins ◽  
Phospholipid Transfer Protein ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Transfer Protein ◽  
Transfer Processes ◽  
Phospholipid Transfer

alpha-Tocopherol (alpha-T), an important anti-oxidant of plasma lipoproteins and cell membranes, is secreted from liver together with very-low-density lipoproteins into the blood stream. Other serum lipoprotein classes gain alpha-T by exchange and transfer processes. We show here that the lipoprotein-free d > 1.22 g/ml fraction of human or pig serum increases the exchange rate of alpha-T by a factor of 2-4 as compared with spontaneous exchange/transfer. The alpha-T exchange/transfer (alpha-TET) activity was purified by multiple-step column chromatography. It gave a single band in PAGE with an apparent molecular mass of 75 kDa, and was found to be identical with the phospholipid transfer protein (PLTP). PLTP catalysed alpha-T exchange between different lipoprotein classes, as well as the transfer of alpha-T from artificial liposomes to high-density lipoproteins. The alpha-TET activity measured with a newly developed assay in ten healthy people was 2.45 +/- 0.88 nmol.ml-1.h-1.alpha-TET activity was negatively correlated with plasma low-density lipoprotein-cholesterol (r = -0.75; P < 0.01). It is concluded that human PLTP catalyses exchange/transfer processes of alpha-T between lipid compartments. This factor may be of relevance in atherogenesis and tumour initiation and growth.

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