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 ◽  
...  

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.

2004 ◽  
Vol 122 (4) ◽  
pp. 175-177 ◽  
Author(s):  
Eliana Cotta de Faria ◽  
Adriana Celeste Gebrin ◽  
Wilson Nadruz Júnior ◽  
Lucia Nassi Castilho

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.


1992 ◽  
Vol 38 (9) ◽  
pp. 1792-1795 ◽  
Author(s):  
G Carcelain ◽  
F David ◽  
S Lepage ◽  
D Bonnefont-Rousselot ◽  
J Delattre ◽  
...  

Abstract We assessed the distribution of alpha-tocopherol in serum lipoprotein samples after separating the lipoprotein fractions by either sequential ultracentrifugation or selective precipitation with sodium phosphotungstate-magnesium chloride reagent. alpha-Tocopherol concentrations were determined by reversed-phase high-performance liquid chromatography. After ultracentrifugation, we found that in men, low- and very-low-density serum lipoproteins (LDL-VLDL) contained 53.6% of alpha-tocopherol vs 46.4% in high-density lipoproteins (HDL). In women, serum LDL-VLDL contained 45.6% alpha-tocopherol after ultracentrifugation vs 54.4% in HDL. After selective precipitation, the proportions of alpha-tocopherol in men were 56.1% in LDL-VLDL vs 43.9% in HDL, and in women, 45.4% in LDL-VLDL vs 54.6% in HDL. After selective precipitation, alpha-tocopherol recovery from whole lipoprotein fractions was 97% to 100% vs 80% after ultracentrifugation, thus allowing more accurate alpha-tocopherol quantification than after separation by ultracentrifugation.


2002 ◽  
Vol 43 (8) ◽  
pp. 1256-1263 ◽  
Author(s):  
Susan J. Murdoch ◽  
Molly C. Carr ◽  
Hal Kennedy ◽  
John D. Brunzell ◽  
John J. Albers

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.


2015 ◽  
Vol 2015 ◽  
pp. 1-5
Author(s):  
Roy A. Garvin

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.


2000 ◽  
Vol 151 (1) ◽  
pp. 184
Author(s):  
S. Jaari ◽  
M. Jauhiainen ◽  
K.Willems van Dijk ◽  
V.M. Olkkonen ◽  
J. Metso ◽  
...  

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