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PubMed1986

Analysis of platelet phospholipids by high performance liquid chromatography. II--Studies on hitherto unknown peak of phospholipid of human platelets.

With our proposed method to analyze platelet phospholipids, utilizing a normal phase high performance liquid chromatography (HPLC), it was able to quantify the amount of major platelet phospholipids (Thromb. Res. 36, 335-344, 1984). A prominent peak of unknown nature (PX) was identified close to the peak of phosphatidylcholine in the HPLC analysis of platelet phospholipids, and the attempts were made to elucidate the nature of PX. By applying several additional authentic phospholipids and those treated by acids on both the HPLC and thin layer chromatography, it was concluded that the major component of PX is 1-lyso phosphatidylethanolamine plasmalogen (PEP), artificially degraded from PEP by the acidic HPLC solvent system. No further degradation of 1-lyso PEP was observed and the absorbance of possibly co-migrated 2-lyso PE in activated platelets was negligible because it was devoid of C-2 double bonds sensitive to the absorbance used in the assay. Therefore, the relative amount of PEP may be detected based on the number of double bonds in platelet PEP. The amount of PEP thus measured was significantly decreased in thrombin-stimulated platelets, suggesting a possible participation of PEP in stimulus-linked platelet reaction.

Blood Platelets↗
PubMed1993

Demonstration that anti-phospholipid auto-antibodies react with both anionic and zwitterionic phospholipids.

The specificity of anti-phospholipid auto-antibodies present in the serum of systemic lupus erythematosus patients towards the phospholipids has been studied by two different methods. The antibodies have been characterized either after affinity purification or by inhibition experiments. Our results clearly demonstrate that anti-phospholipid auto-antibodies recognize all phospholipids, whatever their polar head.

Anions↗
PubMed2006

Anionic phospholipid coatings in capillary electrochromatography. Binding of Ca2+ to phospholipid phosphate group.

Anionic phospholipids phosphatidic acid (PA), phosphatidylglycerol (PG), phosphatidylinositol (PI), and phosphatidylserine (PS) were examined for their effect on 1-palmitoyl-2-oleyl-sn-glycero-3-phosphatidylcholine (POPC)-containing liposomes used as coating material in capillary electrochromatography. Liposome solvent was N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic acid) (HEPES) buffer at pH 7.4 with and without 3 mM of CaCl2. The background electrolyte solution was HEPES buffer at pH 7.4. The net charge, size, and short-term stability of the liposomes were measured with a Zetasizer. Results showed that calcium interacts with all liposomes but most strongly with POPC/PA. The relative migration times, retention factors, and resolution of the model analytes (one cationic, three uncharged ions, and one anionic) were studied. All liposomes successfully coated the silica capillary. Without calcium the strongest interaction and best separation of the analytes were with the POPC/PI and POPC/PS coatings, while interactions with the POPC/PA coating were weak. Calcium enhanced the interactions of the model analytes with all coatings, and the interactions were then strongest with the POPC/PA coating. In the presence of calcium there appears to be a slight reorganization of the coating with increasing number of runs. Our results indicate strong interactions between calcium and the phosphate groups in phospholipids and demonstrate the significant role of the phospholipid polar head group in phospholipid coatings on silica surfaces.

Calcium↗
PubMed1998

Differential influence of rat liver fatty acid binding protein isoforms on phospholipid fatty acid composition: phosphatidic acid biosynthesis and phospholipid fatty acid remodeling.

The ability of two rat liver fatty acid binding protein (L-FABP) isoforms to influence microsomal phosphatidic acid biosynthesis, a key intermediate in glycerolipid formation, and phospholipid fatty acid remodeling was examined in vitro. Isoform I enhanced microsomal incorporation of [1-14C]-oleoyl-CoA into phosphatidic acid 7-fold while isoform II had no effect relative to basal. In contrast, isoform II enhanced microsomal incorporation of [1-14C]-palmitoyl-CoA into phosphatidic acid 4-fold while isoform I had no effect. These results suggest that each L-FABP isoform selectively utilized different acyl-CoAs for glycerol-3-phosphate esterification. Both isoforms stimulated phosphatidic acid formation by increasing glycerol-3-phosphate acyltransferase activity, not by increasing lysophosphatidic acid acyltransferase activity. Furthermore, the effects of L-FABP on phosphatidic acid biosynthesis could not be correlated with protection from acyl-CoA hydrolysis. L-FABP isoforms also influenced phospholipid fatty acid remodeling in a phospholipid-dependent manner. Isoform I preferentially enhanced oleate and palmitate esterification into phosphatidylethanol-amine, while isoform II stimulated esterification into phosphatidylcholine, phosphatidylserine and sphingomyelin. Taken together, these data demonstrated a unique role of each L-FABP isoform in modulating microsomally derived phospholipid fatty acid composition. (c) 1998 Elsevier Science B.V.

Acyl Coenzyme A↗
PubMed1986

Interaction of complement proteins C5b-6 and C5b-7 with phospholipid vesicles: effects of phospholipid structural features.

Complement components C5b-6 and C7 assemble to form C5b-7, which then interacts with membranes and commits the membrane attack complex to a target site. This protein-membrane association event was investigated to determine possible structural features that could contribute to a selective membrane attack. This system may also suggest general properties of protein-membrane insertion events. Initial binding of C5b-6 to membranes could potentially determine the site of assembly. However, binding of C5b-6 to membranes required phosphatidylglycerol or phosphatidic acid produced from egg phosphatidylcholine while binding of C5b-6 to phosphatidylcholine, phosphatidylserine, or phosphatidylinositol was undetectable. Binding to phosphatidic acid was irreversible, and the bound C5b-6 could no longer interact with C7. In contrast, C5b-7 interacted with all phospholipids tested. The rate-limiting process was the interaction of C5b-6 and C7, which displayed bimolecular properties and an activation energy of 37 kcal/mol. The C5b-7 complex showed 20-fold selectivity for small unilamellar phospholipid vesicles over large unilamellar vesicles. Vesicles carrying high negative charge densities were selected over neutral vesicles by a factor of about 5. Vesicles formed from phospholipids with short, saturated hydrocarbon side chains (dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine) were about 5-fold less effective than those formed from phospholipids with natural fatty acid distributions. The gel vs. fluid state had little influence on C5b-7 insertion.(ABSTRACT TRUNCATED AT 250 WORDS)

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1997

The anionic phospholipid-mediated membrane interaction of the anti-cancer drug doxorubicin is enhanced by phosphatidylethanolamine compared to other zwitterionic phospholipids.

The interaction of doxorubicin and lipids has been studied using large unilamellar vesicles (LUVET) composed of mixtures of anionic phospholipids and various zwitterionic phospholipids. Dilution of anionic lipids with zwitterionic lipids leads to decreased membrane association of the drug because electrostatic forces are very important in doxorubicin-membrane interaction. However, binding of doxorubicin to LUVET composed of anionic phospholipids combined with phosphatidylethanolamine (PE) is much higher than binding to LUVET made of anionic lipids plus a range of other zwitterionic lipids such as phosphatidylcholine (PC) and the N-methylethanolamine and N, N-dimethylethanolamine derivatives of PE. This preferential interaction is observed with all negatively charged phospholipids tested and is, in the case of phosphatidylserine (PS), confirmed in monolayer experiments. The increase in surface area observed in a monolayer composed of PS and PE (1/3) was 3 times higher than in a monolayer of PS/PC (1/3). The preferential interaction appears not to be due to the ability of PE to adopt inverted nonbilayer structures, but probably involves a combination of the ability of PE to form additional hydrogen bonds and of the intrinsic curvature of a bilayer containing PE because of its small headgroup. Implications of our finding for the in vivo membrane interaction and transport of the drug will be discussed.

Anions↗
PubMed1997

Effects of maturation on the phospholipid and phospholipid fatty acid compositions in primary rat cortical astrocyte cell cultures.

Phospholipid and phospholipid fatty acid compositional changes were studied in rat cortical astrocytes during dibutyryl cyclic adenosine monophosphate (dBcAMP, 0.25 mM) treatment starting after 14 days in culture (DIC). After 15 DIC, ethanolamine- and choline glycerophospholipid levels were increased 1.2- and 1.3-fold, respectively in treated compared to control cells. However, after 21 and 28 DIC, these levels were not significantly different between groups. Both groups had an increase in phosphatidylserine levels with increasing time in culture. Similarly, ethanolamine plasmalogen levels were transiently elevated after 21 DIC, but returned to previous levels after 28 DIC. The phospholipid fatty acid compositions for the acid stable and labile ethanolamine- and choline glycerophospholipids indicated that in dBcAMP treated cells, 20:4 n-6 and 22:6 n-3 proportions were elevated with increasing time in culture relative to control cells. As 20:4 n-6 proportions increased, there was a concomitant decrease in 20:3 n-9 proportions, suggesting an up regulation of n-6 series elongation and desaturation. In contrast, in control cells, the 20:4 n-6 proportions decreased with a corresponding increase in the 20:3 n-9 proportions. Thus, in treated cells, the cellular phospholipid fatty acid composition was dramatically different than control cells, suggesting that dBcAMP treatment may act to increase fatty acid elongation and desaturation.

Animals↗
PubMed1974

The phospholipid-dependence of uridine diphosphate glucuronyltransferase. Effect of protein deficiency on the phospholipid composition and enzyme activity of rat liver microsomal fraction.

After force-feeding a protein-free diet to male rats for 5-7 days a substantial (2.4-fold) increase in the specific activity of the liver microsomal enzyme UDP-glucuronyltransferase (EC 2.4.1.17) was observed. A similar activation of the enzyme occurred when rats were fed on a low-protein (5%, w/w, casein) diet for 60 days. Although both the short- and long-term protein-deficient diets decreased the contents of microsomal protein and phospholipid in liver tissue they did not significantly alter the ratio of these major membrane components. Protein deficiency profoundly altered the phospholipid composition of microsomal membranes. The most striking difference in microsomal phospholipid composition between control and protein-deficient rats was their content of lysophosphatides. Whereas microsomal membranes from protein-deficient rats contained significant proportions of lysophosphatidylcholine and lysophosphatidylethanolamine very little or no lysophosphatides were detected in control preparations. Pretreatment of microsomal fractions from normal rats with phospholipase A markedly increased their UDP-glucuronyltransferase activity as did their pretreatment with lysophosphatidylcholine. It is concluded that the quantities of lysophosphatides present in microsomal membranes from protein-deficient rats were sufficient to have caused the increased UDP-glucuronyltransferase activities of these preparations. Evidence is presented suggesting that these changes in microsomal phospholipid composition and UDP-glucuronyltransferase activity caused by protein deficiency reflect changes that occur in vivo. The possible physiological significance of these findings is discussed.

Acute Disease↗
PubMed1977

The phospholipid-dependence of uridine diphosphate glucuronyltransferase. Phospholipid depletion and re-activation of guinea-pig liver microsomal enzyme.

More than 80% of the phospholipid component of guinea-pig liver microsomal membranes (prepared with 154mM-KCl) was removed by treatment with phospholipase A followed by extraction of the lysophosphatides and fatty acids produced with albumin. Delipidation strongly inactivated the highly active UDP-glucuronyltransferase of these preparations and activity was restored by mixtures of phosphatidylcholine and lysophosphatidylchlone. However, small quantities of lysophosphatides were still associated with the delipidated fractions after extraction with albumin and might have influenced the inactivation and re-activation observed. To eliminate these uncertainties, microsomal proteins and phospholipids were separated by gel filtration on Sephadex G-150 in the presence of cholate. This technique also strongly inactivated the enzyme but did not generate membrane-active phospholipid degradation products. High transferase activity was again restored to the delipidated protein by choline glycerophosphatides. These results confirm the view that the fully active form of microsomal UDP-glucuronyltransferase is phospholipid-dependent.

Animals↗
PubMed1999

gamma-cyclodextrins greatly enhance translocation of hydrophobic fluorescent phospholipids from vesicles to cells in culture. Importance of molecular hydrophobicity in phospholipid trafficking studies.

Short-chain, fluorescent derivatives are commonly used to investigate intracellular phospholipid trafficking. However, their use can yield misleading results because they, unlike the native species, can rapidly distribute between organelles due to their low hydrophobicity. On the other hand, hydrophobic derivatives are very difficult to introduce to cells and thus have hardly been used. Here we show that carboxyethylated gamma-cyclodextrin (CE-gamma-CD) greatly enhances transfer of a variety of hydrophobic fluorescent phospholipid derivatives from vesicles to cultured cells. Several lines of evidence indicate that CE-gamma-CD enhances transfer of lipid molecules by increasing their effective concentration in the aqueous phase, rather than by inducing membrane fusion or hemifusion. Incubation with CE-gamma-CD and donor lipid vesicles does not extract cholesterol or phospholipids from the cells or compromise plasma membrane intactness or long term cell viability. Using CE-gamma-CD-mediated transfer, we introduced hydrophobic pyrene-labeled phosphatidylserine to the plasma membrane of fibroblast cells and followed their distribution with time. In contrast to what has been previously observed for other, less hydrophobic species, transport of this lipid to the Golgi apparatus or mitochondria was not detected. Rather, much of this fluorescent PS remained in the plasma membrane or was incorporated to various endocytotic compartments. These findings indicate that the native, typically hydrophobic phosphatidylserine molecules efflux only very slowly via the cytoplasm to intracellular organelles. This helps to explain how cells can maintain a very high concentration of phosphatidylserine in the inner leaflet of their plasma membrane. Furthermore, the present results underline the importance of using hydrophobic analogues when studying intracellular trafficking of many phospholipid classes.

Animals↗
PubMed1994

Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes in phospholipid biosynthesis: ethanolamine-dependent effects on steady-state membrane phospholipid composition in Saccharomyces cerevisiae.

It has been established that yeast membrane phospholipid content is responsive to the inositol and choline content of the growth medium. Alterations in the levels of transcription of phospholipid biosynthetic enzymes contribute significantly to this response. We now describe conditions under which ethanolamine can exert significant influence on yeast membrane phospholipid composition. We demonstrate that mutations which block a defined subset of the reactions required for the biosynthesis of phosphatidylcholine (PC) via the CDP-choline pathway cause ethanolamine-dependent effects on the steady-state levels of bulk PC in yeast membranes. Such an ethanolamine-dependent reduction in bulk membrane PC content was observed for both choline kinase (cki) and choline phosphotransferase (cpt1) mutants, but it was not observed for mutants defective in cholinephosphate cytidylyltransferase, the enzyme that catalyzes the penultimate reaction of the CDP-choline pathway for PC biosynthesis. Moreover, the ethanolamine effect observed for cki and cpt1 mutants was independent of the choline content of the growth medium. Finally, we found that haploid yeast strains defective in the activity of both the choline and ethanolamine phosphotransferases experienced an ethanolamine-insensitive reduction in steady-state PC content, an effect which was not observed in strains defective in either one of these activities alone. The collective data indicate that specific enzymes of the CDP-ethanolamine pathway for phosphatidylethanolamine biosynthesis, while able to contribute to PC synthesis when yeast cells are grown under conditions of ethanolamine deprivation, do not do so when yeast cells are presented with this phospholipid headgroup precursor.

Carrier Proteins↗
PubMed1994

Effect of methylene chain length in phospholipid moiety on blood compatibility of phospholipid polymers.

To investigate the effects of the methylene chain length between the phospholipid polar group and the backbone on blood compatibility of a phospholipid polymer, copolymers of omega-methacryloyloxyalkyl phosphorylcholine (MAPC) with n-butyl methacrylate (BMA) were synthesized. The methylene chains were ethylene (n = 2), tetramethylene (n = 4), and hexamethylene (n = 6). Every MAPC copolymer with an MAPC mole fraction in the range of 0.1-0.3 was soluble in ethanol but only swelled in water, and the equilibrium water fraction of the water-swollen MAPC copolymer membrane decreased with the length of the methylene chain. When a rabbit platelet-rich plasma was applied on the MAPC copolymer surface with an 0.1 MAPC mol fraction for 180 min, the number of adhered platelets depended on the length of the methylene chain in the MAPC moiety of the copolymer. The amount of phospholipid adsorbed on the MAPC copolymer from human plasma was larger than that on hydrophobic poly(BMA) and increased with the length of the methylene chain in the MAPC moiety. That is, the reduction of platelet adhesion corresponded to the increase in the amount of phospholipid adsorbed on the MAPC copolymer.

Adsorption↗
PubMed1996

Increased prebeta-high density lipoprotein, apolipoprotein AI, and phospholipid in mice expressing the human phospholipid transfer protein and human apolipoprotein AI transgenes.

Human plasma phospholipid transfer protein (PLTP) circulates bound to high density lipoprotein (HDL) and mediates both net transfer and exchange of phospholipids between different lipoproteins. However, its overall function in lipoprotein metabolism is unknown. To assess the effects of increased plasma levels of PLTP, human PLTP transgenic mice were established using the human PLTP gene driven by its natural promoter. One line of PLTP transgenic mice with moderate expression of PLTP mRNA and protein was obtained. The order of human PLTP mRNA expression in tissues was: liver, kidney, brain, small intestine > lung > spleen > heart, adipose tissue. Western blotting using a human PLTP monoclonal antibody revealed authentic human PLTP (Mr 80 kD) in plasma. Plasma PLTP activity was increased by 29% in PLTP transgenic mice. However, plasma lipoprotein analysis, comparing PLTP transgenic mice to control littermates, revealed no significant changes in the plasma lipoprotein lipids or apolipoproteins. Since previous studies have shown that human cholesteryl ester transfer protein and lecithin:cholesterol acyltransferase only function optimally in human apoAI transgenic mice, the human PLTP transgenic mice were cross-bred with human apoAI transgenic mice. In the human apoAI transgenic background, PLTP expression resulted in increased PLTP activity (47%), HDL phospholipid (26%), cholesteryl ester (24%), free cholesterol (37%), and apoAI (22%). There was a major increase of apoAI in prebeta-HDL (56%) and a small increase in alpha-HDL (14%). The size distribution of HDL particles within alpha- and prebeta-migrating species was not changed. The results suggest that PLTP increases the influx of phospholipid and secondarily cholesterol into HDL, leading to an increase in potentially antiatherogenic prebeta-HDL particles.

Animals↗
PubMed1986

Effect of surfactant substitution on lung effluent phospholipids in respiratory distress syndrome: evaluation of surfactant phospholipid turnover, pool size, and the relationship to severity of respiratory failure.

The turnover and pool size of surfactant has been studied in animals, but there is little similar information in humans. In the present investigation lung effluent phospholipids were studied in 29 small preterm infants with severe RDS. Thirteen were treated with mechanical ventilation, and 16 additionally received natural human surfactant. The first dose (60 mg surfactant/kg body wt) was given between 2 and 10 h of age, and the surfactant was given again if there was an insufficient response. Together 260 aspirates, recovered during routine suctioning of the airways, were analyzed for phospholipids. Phosphatidylglycerol, present only in exogenous surfactant, was used as a specific marker to estimate the apparent pool size and the half-life of surfactant phospholipid. In addition, the saturated phosphatidylcholine/sphingomyelin ratios were correlated with the ventilatory index (mean airway pressure X fractional inspiratory oxygen/arterial oxygen tension). There was a linear correlation between the ventilatory index and the saturated phosphatidylcholine/sphingomyelin (r approximately -0.70) but no consistent correlation between the ventilatory index and the amount of phospholipids in the aspirate. The saturated phosphatidylcholine/sphingomyelin ratio increased during the surfactant-induced remission of respiratory failure, decreased during the recovery. The control infants tended to have lower saturated phosphatidylcholine/sphingomyelin ratios during the first week than the surfactant-treated infants.(ABSTRACT TRUNCATED AT 250 WORDS)

Half-Life↗
PubMed1975

Determinants of the formation and activity of factor V-phospholipid complexes. I. Influence of phospholipid structure.

Previous studies showed that factor V consists of multiple oligomeric forms including a minor component (form L) which contained lipid and was eluted in the excluded volume of a Sepharose 4B column. In the present and following study the hypothesis that factor V is a lipid requiring protein rather than a lipoprotein has been tested. Modification of a previous purification procedure resulted in the separation of factor V from lipoprotein. The lipid extracted from this lipoprotein was qualitatively similar to that previously isolated from form L. Removal of this lipoprotein by sucrose density gradient ultracentrifugation resulted in the isolation of factor V of high specific activity which contained no detectable phospholipid and less than 0.2% cholesterol. No component was excluded from Sepharose 4B after gel filtration of this purified preparation. It is concluded that factor V is not a lipoprotein, but rather a protein which requires lipid for its coagulant properties. To define this requirement further the ability of factor V-phospholipid complexes to accelerate the conversion of prothrombin to thrombin by factor Xa in the presence of calcium was tested. The rate of thrombin formation was highly dependent on the phospholipid employed with each active phospholipid exhibiting a characteristic optimal concentration. At 250 muM, the order of activity was phosphatidyl ethanolamine greater than phosphatidyl inositol greater than cardiolipin greater than phosphatidyl choline. Phosphatidyl serine was inert at all concentrations employed. No single fatty acid was consistently present in active lipid preparations, nor was a specific fatty acid absent from those which had no clotting activity. In comparing different lipid classes, a direct relationship between the overall degree of unsaturation and activity was not observed. However, bovine phosphatidyl inositol, which is highly unsaturated, is active, while plant phosphatidyl inositol, which contains only trace amounts of unsaturated fatty acids, were inert. At lipid concentrations below 300 muM, saturated phosphatidyl ethanolamine produced by hydrogenation of bovine phosphatidyl ethanolamine was less active than an equal concentration of the native lipid. In mixtures containing both lipids, artificially saturated phosphatidyl ethanolamine potentiated the activity of the native compound.

Animals↗
PubMed1986

Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture.

The interaction of nonepithelial intermediate filament (IF) proteins with vesicles produced from total Ehrlich ascites tumor cell lipids results in the formation of complexes which in sucrose density gradient centrifugation attain positions distinctly different from those of the original reactants. In KBr density gradient equilibrium centrifugation, the IF protein-lipid adducts accumulate as thin proteolipid films on top of the KBr gradients, whereas in the absence of lipids the proteins remain distributed within the density gradients. Similar results were obtained with vesicles derived from individual phospholipids and a mixture thereof. The affinity of IF proteins for negatively charged phospholipids is greater than that for vesicles derived from uncharged phospholipids. Limited digestion of IF proteins with various proteinases demonstrated that for optimal association of the reactants IF proteins must carry an intact N terminus and that the isolated N-terminal polypeptide itself shows strong reactivity with lipid vesicles. Arginine-phosphate interactions between the N terminus and phospholipids seem to be partly responsible for this association. However, as shown by hydrophobic interaction chromatography on phenyl- and octyl-Sepharose 4B, IF proteins and their proteolytic derivatives also appear to have high affinities for aromatic and aliphatic substructures of biologically important molecules. The results are discussed in terms of a possible functional role of IF protein-lipid interactions in the association of nonepithelial intermediate filaments with intracellular membrane systems.

Animals↗
PubMed1986

[Effect of hydrocortisone on the phospholipid composition and activity of various enzymes of phospholipid metabolism in the nuclear membranes of the rat liver].

It was shown that hydrocortisone injections markedly increase the total content of liver nuclear membrane phospholipids, the greatest increase being observed in the phosphatidyl choline level. It was found also that nuclear membranes contain phospholipid metabolism enzymes. The hormone-induced increase in the phospholipid content is accompanied by a marked decrease of the activity of phospholipase A2 (5.3 times against control), phospholipase C (9.3 times) and acyl-CoA: lysophosphatidylcholine transferase (2.5 times). The results obtained are suggestive of appreciable metabolic changes in nuclear membrane phospholipids caused by hydrocortisone which, in turn, may be due to hormonal activation of the genome.

Acetyl-CoA C-Acyltransferase↗
PubMed1983

[Practical value of the selective precipitation of LDL, LDL-phospholipids and the molar ratio of cholesterol to LDL-phospholipids in lecithin-cholesterol-acyltransferase deficiency].

There is a high morbidity from hepato-biliary disease in France. These diseases are often accompanied by a reduction in serum lecithin-cholesterol-acyl-transferase activity, which is difficult and costly to diagnose in the laboratory. Thanks to a simple and inexpensive method of selective precipitation of light lipoproteins, we have been able to establish the practical value of the determination of the LDL-phospholipids and the molar cholesterol ratio on the phospholipids in the LDL (MCPR) in familial or secondary deficiencies of Lecithin-Cholesterol-Acyl-Transferase. These conditions are characterized by a high proportion of serum phospholipids transported by the LDL (more than 60%) and by the marked reduction in the cholesterol ratio of the phospholipids in the LDL. The authors propose a classification for the commonest causes of lecithin-cholesterol-acyl-transferase deficiency.

Cholesterol↗