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At least 199 records · Page 11Linked to original sources
PubMed2001

Triglyceride-rich lipoprotein cholesterol exceeds low-density lipoprotein cholesterol in hypertriglyceridemia patients.

The atherogenicity of triglyceride-rich lipoprotein has been revealed. This study was performed to explore the clinical importance of triglyceride-rich lipoprotein by measuring its cholesterol content and comparing it with other lipoprotein fractions. Blood samples were obtained from 103 patients whose fasting plasma triglyceride concentration exceeded 300 mg/dl. The cholesterol monitor using the technique of high-performance liquid chromatography was used for the measurement of their plasma cholesterol concentrations and the determination of cholesterol distribution among lipoprotein fractions. This monitor showed 4 peaks: large-triglyceride-rich lipoprotein, small-triglyceride-rich lipoprotein, low-density lipoprotein, and high-density lipoprotein. Total cholesterol increased with increasing triglyceride. The increment of total cholesterol was nearly equal to that of small-triglyceride-rich lipoprotein cholesterol. Small-triglyceride-rich lipoprotein cholesterol exceeded low-density lipoprotein cholesterol where plasma triglyceride concentration was over 500 mg/dl. In conclusion, triglyceride-rich lipoprotein may be clinically important for hypertriglyceridemic patients as a source of cholesteryl ester in arteriosclerotic plaques, and increased triglyceride-rich lipoprotein cholesterol may be used as a basis for hypertriglyceridemia atherogenicity. Our study suggests that hypertriglyceridemia should be treated to prevent arteriosclerotic disease.

Apolipoproteins E↗
PubMed1997

Antibodies against high-density lipoprotein binding proteins enhance high-density lipoprotein uptake but do not affect cholesterol efflux from rat hepatoma cells.

High-density lipoprotein plays a key role in the reverse cholesterol transport pathway as well as in the delivery of cholesterol to the liver and steroidogenic tissues. Metabolism of high-density lipoprotein is determined by one of its apolipoproteins, apolipoprotein A-I; however, the identity and function of cellular protein which binds high-density lipoprotein remains unclear. The effect of antibodies against rat high-density lipoprotein binding proteins, HB1 and HB2, on high-density lipoprotein metabolism in a rat hepatoma cell line were studied. Cells were preincubated with the antibodies and 125I-labeled high-density lipoprotein binding and uptake as well as cholesterol biosynthesis and cholesterol efflux to human plasma or isolated high-density lipoprotein were studied. Both antibodies reacted specifically with HB1 and HB2 on the ligand and Western blots, but their binding was not blocked by high-density lipoprotein. Both antibodies inhibited 125I-labeled high-density lipoprotein binding to cells by 20-40%, but stimulated 125I-labeled high-density lipoprotein uptake by up to 2.5-fold. The antibodies had no effect on cholesterol efflux or on cholesterol synthesis. It is concluded that high-density lipoprotein binding proteins, HB1 and HB2, may be involved in high-density lipoprotein uptake in the liver rather than in mediating cholesterol efflux.

Animals↗
PubMed1980

Differences in the metabolism of very-low-density lipoproteins by isolated beating-heart cells and the isolated perfused rat heart. Evidence for collagenase-released extracellular lipoprotein lipase.

1. The metabolism of VLD lipoproteins (very-low-density lipoproteins) was studied in intact isolated beating-heart cells and isolated perfused rat heart from starved animals by using [14C]triacylglycerol fatty acid-labelled VLD lipoprotein prepared from rats previously injected with [1-14C]palmitate. 2. 14C-labelled VLD lipoprotein was metabolized by the isolated perfused heart, but was only minimally metabolized by the heart cells unless an exogenous source of lipoprotein lipase was added. 3. Measurements of lipoprotein lipase at pH 7.4 with the natural substrate 14C-labelled VLD lipoprotein indicated that during collagenase perfusion of the heart the enzyme was released into the perfusate, the activity released being proportional to the concentration of collagenase used. Lipoprotein lipase activity in homogenates of hearts that had been perfused with collagenase showed a corresponding loss of activity. 4. At high perfusate concentrations of collagenase, inactivation of the released lipoprotein lipase occurred. 5. Lipoprotein lipase activity was largely undetectable in the homogenate of the isolated heart cells. 6. It is concluded that the lipoprotein lipase responsible for the hydrolysis of VLD lipoprotein triacylglycerol is predominantly located externally to the heart muscle cells and that its release can be facilitated by perfusion of the heart with bacterial collagenase.

Animals↗
PubMed2000

Effects of normalization of GH hypersecretion on lipoprotein(a) and other lipoprotein serum levels in acromegaly.

BACKGROUND & AIMS: Lipoprotein(a) has been recognized as an important risk factor for cardiovascular disease. Lipoprotein(a) has been found to be elevated in sera of acromegalic patients, possibly contributing to the increased incidence of coronary heart disease found in these patients. In the present study we sought to determine the effects of GH hormonal status on lipoprotein(a) and other lipid parameters, including lipoprotein lipase (LPL) activity. DESIGN: Cross-sectional study. PATIENTS: Twenty acromegalic patients, with either active (n = 12) or controlled (n = 8) acromegaly, were studied. Twenty-nine healthy subjects served as control group for serum lipid measurements. MEASUREMENTS: Serum GH, IGF-1, IGF binding protein-3 (IGFBP-3) and insulin levels were measured in patients. Insulin resistance was measured by the homeostatic model assessment (HOMA). Plasma total cholesterol, triglycerides, HDL-lipids, apolipoproteins A-I and B, lipoprotein(a) and lipoprotein lipase activity were also measured. RESULTS: The highest lipoprotein(a) levels were observed in patients with active acromegaly, followed by patients with controlled acromegaly, whose lipoprotein(a) concentrations were still significantly higher than those of the control group (means +/- SEM: active acromegaly, 0.67+/-0.13 g/l; controlled acromegaly, 0.41+/-0.12 g/l; controls 0.17+/-0.02 g/l; P<0.05). There were no differences in other lipid and lipoprotein values among the groups. In patients, significant correlations were observed between lipoprotein(a) and basal GH levels (r = 0.56, P<0.02), mean GH levels (r = 0.48, P<0.05) and with insulin resistance estimated by HOMA (r = 0.62, P<0.01). No correlations were found between lipoprotein(a) and IGF-1 or IGFBP-3 levels. CONCLUSIONS: Our present results demonstrate that both active acromegalic patients and those with controlled disease have elevated serum lipoprotein(a) concentrations. The findings might suggest that the present biochemical criteria for cure of acromegaly are not strict enough to result in the normalization of all the undesirable metabolic changes found in this disease, and also that significant cardiovascular risk may persist despite successful treatment of acromegaly.

Acromegaly↗
PubMed1991

Characterization of lipoprotein secreted by cultured eel hepatocytes and its comparison with serum lipoproteins.

The lipoprotein secreted by cultured eel hepatocytes was fractionated by density gradient ultracentrifugation and compared with eel serum lipoproteins. Eel hepatocytes were cultured for 7 to 10 days as a monolayer in Williams' medium E containing 5% fetal bovine serum and 0.16 microM insulin on a dish precoated with fibronectin of horse serum. The only lipoprotein secreted by eel hepatocytes was a very-low-density lipoprotein like one which consisted of 69% triglyceride, 15% phospholipid, 4% cholesterol, and 12% protein. On the other hand, very-low-density lipoprotein and high density lipoprotein were found in eel serum, in which high density lipoprotein was a main lipoprotein. The secreted lipoprotein contained apo B and apo A as the main protein components. Furthermore, the lipoprotein contained proapo A-I in addition to apo A-I, which was proved by comparing the amino acid composition of both proteins. In our discussion, we noted that the lipoprotein secreted by eel hepatocytes was a good material for the study of high-density lipoprotein formation.

Amino Acids↗
PubMed1996

Binding of lipoprotein lipase to apolipoprotein B-containing lipoproteins.

The binding of lipoprotein lipase (LPL) to different lipoproteins and to a lipid emulsion was studied. After incubating the same amount of 125I-labelled LPL with VLDL, LDL or a lipid emulsion containing no apolipoproteins, we separated the free enzyme from the lipoprotein-bound LPL by gel filtration and by lipoprotein precipitation with phosphotungstic acid. By the former method we observed that all these types of lipid particles bound LPL indicating that the lipid moiety accounts for the LPL-lipoprotein interaction. This binding of LPL to lipoproteins was disrupted by high salt concentrations. When balanced by the apolipoprotein B content, it was observed that a significantly higher amount of 125I-labelled LPL co-eluted with VLDL than with LDL in gel permeation. The Kd values for binding of LPL to lipoproteins were estimated by use of lipoprotein precipitation. The obtained Kd values, both in the absence and in the presence of human lipoprotein deficient serum, were lower for VLDL than for LDL indicating a higher affinity of LPL for VLDL than for LDL. We finally compared binding capacity of LPL to VLDL subfractions with different apo E content. For this, we used apo E-poor (VLDL-B) and apo E-rich (VLDL-D) subfractions separated by heparin-Sepharose chromatography. We found that 125I-labelled LPL co-eluted to a similar extent with both subfractions on gel filtration, and the estimated Kd values from lipoprotein precipitation were not statistically different. Taken together, our results indicate that the lipid moiety, probably the phospholipids, accounts for the LPL-lipoprotein interaction; differences in size, the presence of C apolipoproteins or the conformation of apo B may be responsible for the higher affinity of LPL for VLDL than for LDL herein observed.

Apolipoproteins B↗
PubMed1996

Alpha-tocopherol as a reductant for Cu(II) in human lipoproteins. Triggering role in the initiation of lipoprotein oxidation.

Initiation of lipid peroxidation by Cu(II) requires reduction of Cu(II) to Cu(I) as a first step. It is unclear, however, whether this reaction occurs in the course of lipoprotein oxidation. It is also unknown which reductant, if any, can drive the reduction of Cu(II) in this case. We found that Cu(II) was rapidly reduced to Cu(I) by all major human lipoproteins (high, low, and very low density lipoproteins (HDL, LDL, and VLDL), and chylomicrons). Cu(II)-reducing activity was associated with a lipid moiety of the lipoproteins. The rates of Cu(II) reduction by different lipoproteins were similar when the lipoproteins were adjusted to similar alpha-tocopherol concentrations. Enriching lipoproteins with alpha-tocopherol considerably increased the rate of CU(II) reduction. CU(II) reduction by alpha-tocopherol-deficient LDL isolated from a patient with familial inherited vitamin E deficiency was found to occur much slower in comparison with LDL isolated from a donor with a normal plasma level of alpha-tocopherol. Initial rate of CU(II) reduction by alpha-tocopherol-deficient LDL was found to be zero. Enriching LDL with ubiquinol-10 to concentrations close to those of alpha-tocopherol did not influence the reaction rate. When LDL was treated with ebselen to eliminate preformed lipid hydroperoxides, the reaction rate was also not changed significantly. CU(II) reduction was accompanied by a consumption of lipoprotein alpha-tocopherol and accumulation of conjugated dienes in the samples. Increasing alpha-tocopherol content in lipoproteins slightly decreased the rate of conjugated diene accumulation in LDL and HDL and considerably increased it in VLDL. The results suggest that alpha-tocopherol plays a triggering role in the lipoprotein oxidation by CU(II), providing its initial step as follows: alpha TocH + CU(II) --> alpha Toc. + Cu(I) + H+. This reaction appears to diminish or totally eliminate the antioxidative activity of alpha-tocopherol in the course of lipoprotein oxidation.

Adult↗
PubMed1997

Autoantibodies to oxidized low density lipoprotein: the relationship to low density lipoprotein fatty acid composition in diabetes.

Autoantibodies to oxidized low density lipoprotein have been shown to be an independent predictor of the progression of carotid atherosclerosis. This study examines the relationship between low density lipoprotein fatty acid composition and autoantibodies to both malondialdehyde-modified and copper-oxidized low density lipoprotein in non-diabetic patients with (n = 17), and without (n = 18), definite evidence of previous myocardial infarction. The third group were non-insulin-dependent diabetic patients with no evidence of atherosclerosis (n = 15) and the fourth group were patients with non-insulin-dependent diabetes (n = 17) who had definite evidence of previous myocardial infarction. Fatty acids were measured by gas-liquid chromatography. Antibodies to malondialdehyde-modified low density lipoprotein and copper-oxidized low density lipoprotein were determined by an ELISA method. Autoantibodies to copper-oxidized low density lipoprotein were significantly higher in the non-diabetic patients with heart disease when compared to any other group (p < 0.05). Autoantibodies to malondialdehyde-modified low density lipoprotein were significantly higher in the non-diabetic subjects with heart disease and in both diabetic groups compared to non-diabetic subjects without coronary heart disease (p < 0.05). Linoleic acid (%) in low density lipoprotein did not differ between groups groups but arachidonic acid (%) was significantly lower in both diabetic and non-diabetic patients with coronary heart disease (p < 0.05). The diabetic patients with low antibodies had 39.6 +/- 2.2% polyunsaturated fatty acids in their low density lipoprotein while diabetic patients with high antibodies had 46.7 +/- 1.2% polyunsaturates in their low density lipoprotein (p < 0.01). This study confirms the association between antibodies to oxidized low density lipoprotein and coronary heart disease and shows raised low density lipoprotein antibody levels in diabetic patients with and without demonstrable atherosclerosis. In the diabetic patients, those with high antibody levels had high polyunsaturated fatty acid levels in their LDL suggesting a possible role for dietary intervention.

Aged↗
PubMed2002

Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals.

Lipoproteins are present in a wide variety of bacteria and are anchored to membranes through lipids attached to the N-terminal cysteine. The Lol system of Escherichia coli mediates the membrane-specific localization of lipoproteins. Aspartate at position 2 functions as a Lol avoidance signal and causes the retention of lipoproteins in the inner membrane, whereas lipoproteins having residues other than aspartate at position 2 are released from the inner membrane and localized to the outer membrane by the Lol system. Phospholipid:apolipoprotein transacylase, Lnt, catalyzes the last step of lipoprotein modification, converting apolipoprotein into mature lipoprotein. To reveal the importance of this aminoacylation for the Lol-dependent membrane localization, apolipoproteins were prepared by inhibiting lipoprotein maturation. Lnt was also purified and used to convert apolipoprotein into mature lipoprotein in vitro. The release of these lipoproteins was examined in proteoliposomes. We show here that the aminoacylation is essential for the Lol-dependent release of lipoproteins from membranes. Furthermore, lipoproteins with aspartate at position 2 were found to be aminoacylated both in vivo and in vitro, indicating that the lipoprotein-sorting signal does not affect lipid modification.

ATP-Binding Cassette Transporters↗
PubMed1981

Isolation and partial characterization of the lipoprotein families A and A-I from high-density lipoproteins of human serum.

Procedures for the isolation of two lipoprotein fractions from plasma high-density lipoproteins (HDL), characterized by apolipoprotein A-I and apolipoprotein A-I together with apolipoprotein A-II, have been elaborated. Apolipoprotein A-I was identified as the protein moiety of one of these fractions (lipoprotein A-I) with polyacrylamide gel electrophoresis (at basic and acidic pH, as well as in the presence of sodium dodecyl sulphate), immuno-double-diffusion, and amino acid analysis. Apolipoproteins A-I and A-II were identified as the protein moiety of the other fraction (lipoprotein A) with polyacrylamide gel electrophoresis (basic and acidic pH) and immuno-double-diffusion. Lipoprotein A-I consisted of spherical particles with a diameter similar to that of HDL as judged from negative strains in the transmission electron microscope. The diameter was estimated to be 8.7 nm from gel chromatography. Lipoprotein A-I migrated in the HDL position on crossed immunoelectrophoresis. On iso-electric focusing lipoprotein A-I appeared as multiple bands in the pH range 5.05-5.55. Lipoprotein A-I had the density of an HDL-2 fraction (rho: 1.063-1.105). Lipoprotein A consisted of spherical particles with a diameter similar to that of HDL, as judged from negative strains in the transmission electron microscope. The diameter was estimated to be 7.9 nm from gel chromatography. The molar ratio between the A-I and A-II polypeptides was estimated to 1.3:1 with electroimmunoassay and calculations from the amino acid compositions. Lipoprotein A migrated in the position of HDL on crossed immuno-electrophoresis. On iso-electric focusing lipoprotein A appeared as one major and two minor bands in the pH range 5.10-5.30. Lipoprotein A had the hydrated density of an HDL-2 fraction.

Adult↗
PubMed1982

Hepatic Golgi lipoproteins: precursors to plasma lipoproteins in hypercholesterolemic rats.

Two classes of nascent lipoproteins can be isolated from Golgi apparatus-rich fractions of liver from hypercholesterolemic rats. Golgi very low density lipoproteins (VLDL, d less than 1.006 g/ml) are enriched in cholesteryl esters and are similar in many respects to hypercholesterolemic plasma B-VLDL. Golgi low density lipoproteins (LDL, d 1.006-1.05 g/ml) are cholesteryl ester-rich beta-migrating lipoproteins similar to hypercholesterolemic plasma LDL. To determine if this latter lipoprotein is a precursor to plasma LDL, control and hypercholesterolemic rats were injected with Triton WR 1339 (400 mg/kg) to block intravascular lipoprotein catabolism, followed in 30 min with 100 microCi [3H]leucine. At time intervals up to 3 hours after [3H]leucine injection, rats were killed, and plasma lipoproteins and, in some experiments, Golgi lipoproteins were isolated. Three hours after radioisotope injection, 52% of the total lipoprotein radioactivity was found in the plasma VLDL of hypercholesterolemic rats compared to 82% in chow-fed control rats. Twenty-four percent of the total lipoprotein radioactivity appeared in the plasma IDL fraction in hypercholesterolemic rats, while only 3% was found in the same fraction in control rats. After Triton, the time course of specific activities of the Golgi and plasma lipoproteins was consistent with Golgi VLDL and LDL being precursors to plasma VLDL and IDL, respectively. The time course of specific activities of the tetramethylurea-insoluble proteins of plasma and Golgi lipoproteins provided additional evidence in support of this relationship. Furthermore the composition of plasma VLDL and IDL after Triton injection resembled their hepatic Golgi counterparts. We conclude that the liver of the hypercholesterolemic rat synthesizes, assembles, and secretes a cholesteryl ester-enriched VLDL and a cholesteryl ester-rich, beta-migrating LDL. The former is a precursor to plasma VLDL while the latter is a precursor to plasma IDL.

Animals↗
PubMed1985

Induction of macrophage growth by the lipid moiety of lipoprotein and its augmentation by denaturation of the lipoproteins.

Lipoprotein (d less than 1.21) isolated from mouse tumor ascitic fluid or mouse-serum induced growth of peritoneal macrophages in vitro. Lipoprotein fractions that stimulated macrophage growth were the chylomicron, very-low-density lipoprotein (VLDL), and low-density lipoprotein (LDL), whereas the high-density lipoprotein (HDL) fraction did not. Lipids extracted from total lipoprotein also showed significant macrophage-growth-stimulating activity and lost this activity when hydrolyzed. The macrophage-growth-stimulating activity of the lipoprotein (d less than 1.21) was increased about ten times by heat treatment of the lipoprotein (100 degrees C, 30 min). The HDL fraction that had no activity in the native form also showed activity after heat treatment. Lipoprotein-depleted ascitic fluid and simple proteins such as bovine serum albumin (BSA) had no activity even after heat treatment. These results show that the lipid moiety of lipoproteins caused proliferation of macrophages and that denatured lipoproteins were more effective than native ones.

Animals↗
PubMed1982

Hydrolysis of plasma triacylglycerol-rich lipoproteins from immature and laying hens (Gallus domesticus) by lipoprotein lipase in vitro.

Very-low-density (VLD) lipoproteins and portomicrons were isolated from the plasma of immature and laying hens and their size, lipid composition and susceptibility to hydrolysis by lipoprotein lipase were compared. In agreement with other studies, VLD lipoproteins from laying hens were found to be smaller and have a different lipid composition than VLD lipoproteins from immature hens. Portomicrons from immature and laying hens had mean diameters of about 150 nm and similar lipid compositions. Hydrolysis of VLD lipoproteins from immature hens, and portomicrons from immature and laying hens, proceeded rapidly until at least 40% of the substrate had been used. In contrast only 1--15% of laying-hen VLD-lipoprotein triacylglycerol was readily hydrolysis occurred slowly. The limited susceptibility of laying-hen VLD lipoproteins appeared to be due to their low content of lipoprotein lipase activator apoprotein, which occurred despite an abundance of activator in the high-density lipoproteins of laying-hen plasma. The results provide further evidence that the liver of the laying hen synthesizes specialized lipoproteins. Their limited susceptibility to hydrolysis by lipoprotein lipase is probably a major factor in ensuring transport of lipid to yolk rather than to other tissues. The form of transport of dietary lipid, however, is similar in immature and laying hens.

Age Factors↗
PubMed1986

The effects of oral agent or insulin treatments on the plasma lipoproteins and the plasma lipoprotein lipase activator in diabetic patients.

The structure and the metabolism of plasma lipoproteins are altered in diabetes mellitus. Insulin or oral agent treatments affect the lipoprotein metabolism in addition to improving hyperglycemia. However, it is not clear whether the alterations seen in lipoproteins during treatment are related to the degree of diabetic control or to the mode of diabetic treatment. The effects of insulin or oral agent treatments on the plasma lipoproteins and lipoprotein lipase activator were compared in a strictly defined non-obese, non-insulin dependent diabetic patient. Both treatment groups had similar plasma triglyceride, total cholesterol, low and high density lipoprotein cholesterol, and lipoprotein lipase activator levels. Lipoprotein lipase activator contents of the very low density lipoproteins correlated positively with their triglyceride (r = 0.803 in insulin, r = 0.828 in oral agent treated patients) and protein (r = 0.713 in insulin, r = 0.862 in oral agent treated patients) contents. The findings of this study indicated that plasma lipid levels, very low density lipoprotein compositions, and lipoprotein lipase activator contents were not significantly different in non-obese, non-insulin dependent diabetic patients treated with either oral hypoglycemic agents or insulin.

Administration, Oral↗