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PubMed1994

Effects of treatment with bezafibrate on lipoprotein lipase activity and mass in patients with hypertriglyceridemia.

The activity and mass of lipoprotein lipase (LPL) in postheparin plasma (PHP) from patients with hypertriglyceridemia coupled with hypertension, impaired glucose tolerance, hyperinsulinemia were investigated in order to clarify the cause of hypertriglyceridemia and the effects of bezafibrate (CAS 41859-67-0), a novel lipid lowering agent. Eight weeks of treatment with bezafibrate (200 mg/d) lowered plasma total cholesterol and triglyceride by 7 and 39%, respectively, and increased plasma high density lipoprotein (HDL) cholesterol by 23% in the patients (n = 15). The LPL activity and mass of PHP in the patients were found to be lower than in the normal controls. The LPL activity and mass of PHP in the patients before treatment with bezafibrate (n = 15) were 2.05 +/- 1.06 mumol/ml/h and 147 +/- 45 ng/ml, respectively, whereas after treatment with 200 mg/d of bezafibrate for 8 weeks, these values were 3.62 +/- 1.30 mumol/ml/h (p < 0.01) and 226 +/- 57 ng/ml (p < 0.05), respectively. The increases of LPL mass were positively correlated with the decrease of triglyceride levels during the same period. These results suggest that the expression of LPL enzyme protein is impaired in patients with hypertriglyceridemia coupled with hypertension, impaired glucose tolerance and hyperinsulinemia, and the impaired expression of LPL recovers during treatment with bezafibrate, resulting in improvement of hypertriglyceridemia.

Adult↗
PubMed2003

Lipoprotein lipase as a therapeutic target for dyslipidemia.

The importance of lipoprotein lipase (LPL) in the regulation of overall lipid metabolism in humans and other animals is well documented. The major goal of this review is to identify and justify features that make LPL an important drug target for lipid management in particular for triglyceride lowering and HDL elevation, and propose strategies to modulate LPL activity.

Animals↗
PubMed1995

Overexpression of human lipoprotein lipase increases hormone-sensitive lipase activity in adipose tissue of mice.

An elevation of lipoprotein lipase (LPL) activity in adipose tissue is considered a possible cause of obesity. However, transgenic mice that overexpress the human LPL gene showed no increase in fat deposition as compared with controls. In the present study, we investigated effects of LPL on fat accumulation. Respiratory quotients and uptake of [3H] triolein by tissues (white and brown adipose tissue, and skeletal muscles) did not differ significantly for transgenic and non-transgenic mice. The mRNA levels of hormone-sensitive lipase (HSL) and HSL activity in adipose tissue during feeding were higher in LPL transgenic mice than in controls. Results suggest that the overexpression of LPL does not induce obesity by enhancing the hydrolysis of triglycerides in adipose tissue.

Adipose Tissue↗
PubMed1984

Folic acid and lipoprotein lipase from aorta and blood plasma of atherosclerotic rats.

The lipoprotein lipase activity is somehow associated with atherosclerosis, and some publications report a protective effect of this enzyme against infiltration of lipids. In this publication, an atherogenic diet was associated with a decrease of this enzyme in aorta and blood plasma of rats. After administration of folic acid, a significant increase of the clearing factor activity was observed.

Animals↗
PubMed1996

Alterations of lipolysis and lipoprotein lipase in chronically nicotine-treated rats.

These studies examined the cellular mechanisms for lower adiposity seen with nicotine ingestion. Rats were infused with nicotine or saline for 1 wk and adipocytes isolated from epididymal fat pads. Nicotine-infused rats gained 37% less weight and had 21% smaller fat pads. Basal lipolysis was 78% higher, whereas the maximal lipolytic response to isoproterenol was blunted in adipocytes from nicotine-infused rats. The antilipolytic actions of adenosine and the levels of serum catecholamines were unaffected by nicotine. The nicotine-induced alteration in lipolysis was not associated with any changes in hormone-sensitive lipase. Nicotine caused a 30% decrease in lipoprotein lipase (LPL) activity, without any changes in LPL mass or mRNA levels, in epididymal fat in the fed state. In contrast, LPL activity, mass, and mRNA levels in heart were increased by nicotine whether animals were fed or fasted. These studies provide evidence for multiple mechanistic events underlying nicotine-induced alterations in weight and suggest that nicotine diverts fat storage away from adipose tissue and toward utilization by muscle.

Adipose Tissue↗
PubMedDate not supplied

[Thermal inactivation of milk lipoprotein lipase].

The kinetics of thermal inactivation of cow's milk lipoprotein lipase (LPL) was studied. LPL inactivation can be described by the first order q equation. Thermodynamic parameters of LPL inactivation were calculated. In the range of physiological temperatures LPL existed as two conformers. The temperature of conformation conversion was 41.5 degrees C. Glycerol increased thermal stability of milk, whereas water dilution of milk, pH shift to the acid or alkaline zone, and glycine addition to milk decreased it. It is suggested that casein micellae stabilize milk LPL.

Animals↗
PubMed2002

Hormone-sensitive lipase deficiency in mice changes the plasma lipid profile by affecting the tissue-specific expression pattern of lipoprotein lipase in adipose tissue and muscle.

Hormone-sensitive lipase (HSL) is believed to play an important role in the mobilization of fatty acids from triglycerides (TG), diglycerides, and cholesteryl esters in various tissues. Because HSL-mediated lipolysis of TG in adipose tissue (AT) directly feeds non-esterified fatty acids (NEFA) into the vascular system, the enzyme is expected to affect many metabolic processes including the metabolism of plasma lipids and lipoproteins. In the present study we examined these metabolic changes in induced mutant mouse lines that lack HSL expression (HSL-ko mice). During fasting, when HSL is normally strongly induced in AT, HSL-ko animals exhibited markedly decreased plasma concentrations of NEFA (-40%) and TG (-63%), whereas total cholesterol and HDL cholesterol levels were increased (+34%). Except for the increased HDL cholesterol concentrations, these differences were not observed in fed animals, in which HSL activity is generally low. Decreased plasma TG levels in fasted HSL-ko mice were mainly caused by decreased hepatic very low density lipid lipoprotein (VLDL) synthesis as a result of decreased NEFA transport from the periphery to the liver. Reduced NEFA transport was also indicated by a depletion of hepatic TG stores (-90%) and strongly decreased ketone body concentrations in plasma (-80%). Decreased plasma NEFA and TG levels in fasted HSL-ko mice were associated with increased fractional catabolic rates of VLDL-TG and an induction of the tissue-specific lipoprotein lipase (LPL) activity in cardiac muscle, skeletal muscle, and white AT. In brown AT, LPL activity was decreased. Both increased VLDL fractional catabolic rates and increased LPL activity in muscle were unable to provide the heart with sufficient NEFA, which led to decreased tissue TG levels in cardiac muscle. Our results demonstrate that HSL deficiency markedly affects the metabolism of TG-rich lipoproteins by the coordinate down-regulation of VLDL synthesis and up-regulation of LPL in muscle and white adipose tissue. These changes result in an "anti-atherogenic" lipoprotein profile.

Adipose Tissue↗
PubMed1986

Lipoprotein lipase secretion from isolated rat fat cells of different size.

Lipoprotein lipase(LPL) release from isolated small fat cells from young rats and large fat cells from older, fatter rats was compared during in vitro incubation at 30 degrees C. Although large fat cells had nearly three times higher cellular LPL activity, they secreted similar amounts of LPL activity into the incubation medium under both basal conditions (Krebs Ringer bicarbonate buffer containing 4% albumin and 6mM glucose) and after stimulation of LPL release by 5% human serum, or serum plus 1 U/ml heparin. These data suggest that previous observations of an altered tissue distribution of LPL in adipose tissue containing large fat cells can be at least in part explained by an alteration at the level of LPL secretion.

Adipose Tissue↗
PubMed1978

Post-translational regulation of lipoprotein lipase activity in adipose tissue.

Changes in adipose-tissue lipoprotein lipase activity that are independent of protein synthesis were investigated in an incubation system in vitro. Under appropriate conditions at 25 degrees C a progressive increase in the enzyme activity occurs that is energy-dependent. Part of the enzyme is rapidly inactivated when the tissue is incubated with adrenaline or adrenaline plus theophylline. The mechanism of this inactivation appears to be distinct from, and to follow, the activation of the enzyme. A hypothesis is presented to account for the results in terms of an activation of the enzyme during obligatory post-translational processing and a catecholamine-regulated inactivation of the enzyme as an alternative to secretion from the adipocyte.

Adipose Tissue↗
PubMed1986

Existence of lipoprotein lipase in rat brain microvessels.

To clarify the possibility that brain microvessels could utilize very low density lipoprotein (VLDL)-triglyceride, the hydrolysis of [14C] triolein in VLDL by rat brain microvessels was examined. The rat brain microvessels were prepared under microscopy. In the homogenate, triolein hydrolyzing activity was observed only in the presence of apolipoprotein C-II. That activity was diminished by the addition of 1 M NaCl. [14C] triolein incorporated in VLDL was hydrolyzed time- dependently. These results suggested that there exists lipoprotein lipase in brain microvessels and the brain can utilize VLDL triglyceride as a source of fatty acids.

Animals↗
PubMed1979

The effect of short-term starvation on the lipoprotein lipase activity of adipose tissue and cardiac muscle during postnatal development of the rat.

When male rats of between 6 and 13 days of age were starved for 6 h the lipoprotein lipase activity of the epididymal and subcutaneous white adipose tissue did not decline as it did in adults and in animals aged 14-30 days. The lipoprotein lipase activity in the hearts of animals from 6 days of age increased in response to starvation as it did in adults. The relationship of these changes to changes in circulating hormone levels during development was considered.

Adipose Tissue↗
PubMed1989

Interaction of lipoprotein lipase with heparin.

The hydrolysis of triglyceride-rich plasma lipoproteins is initiated by lipoprotein lipase (LPL) located at the luminal surface of endothelial cells. We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate. We and others recently isolated LPL cDNAs from various animals. The deduced amino acid sequence from cDNA sequence is highly conserved among animal species. The structural analysis revealed two regions rich in basic amino acid residues at the carboxyl-terminal region that may interact with the anionic heparin-like molecules. Amino acid residues 292 to 300 of bovine LPL are extremely similar to the reported heparin binding sites on apolipoproteins B-100 (amino acid residues 3359-3367) and E (amino acid residues 142-150).

Amino Acid Sequence↗
PubMed1992

Effect of cyclosporin on plasma lipoprotein lipase activity in rats.

The effects of cyclosporin on plasma lipoproteins and lipoprotein lipase (LPL) activity were studied in rats treated with different doses of the drug for periods ranging between 7 and 30 days. The treatment with cyclosporin resulted in an increase in plasma triglycerides and non-HDL-cholesterol, and a dose and time-dependent decrease of LPL activity and HDL-cholesterol, mainly because of a fall in the HDL2-cholesterol subfraction. The decrease of LPL activity was positively correlated (p < 0.01) with plasma HDL-cholesterol and HDL2-cholesterol and negatively with plasma triglycerides and non-HDL-cholesterol (p < 0.01). Our results indicate that the decrease in plasma LPL activity may be responsible for the increase in plasma triglycerides and the decrease in plasma HDL-cholesterol found in rats under cyclosporin treatment.

Animals↗
PubMed2001

Severe hypercholesterolemia in a double heterozygote for lipoprotein lipase deficiency (LPL(Arita)) and apolipoprotein epsilon4: a report of a family with LPL(Arita).

Although heterozygous lipoprotein lipase (LPL) deficiency is not rare, only part of the phenotypes may have been reported in Japan. Here we describe a Japanese family with LPL(Arita), the most common mutation linked to familial LPL deficiency in Japan, and show for the first time a heterozygote for the mutation who had marked hypercholesterolemia due to increased low-density lipoprotein (LDL) cholesterol. The proband's mother, one of the heterozygotes for LPL(Arita) in the family, had both severe hypercholesterolemia (total cholesterol 306 mg/dl) with an especially increase in LDL-cholesterol and mild hypertriglyceridemia (180 mg/dl). She had normal LDL receptor activity and did not show clear evidence of possible causes of secondary hyperlipidemia. In addition to being heterozygous for LPL deficiency, she was also heterozygous for apo epsilon4. Because the epsilon4 allele is known to be associated with higher LDL-cholesterol, heterozygous apo epsilon4 may be one of causes of her LDL-cholesterol elevation. The other three heterozygotes for LPL(Arita) were moderate drinkers, and all of them had both remarkable hypertriglyceridemia and mild hypercholesterolemia due to increased very-low-density lipoproteins (VLDL). The results suggest that heterozygotes for LPL(Arita) can exhibit various phenotypes of hyperlipidemia, that is, hypertrigliceridemia and/or hypercholesterolemia due to not only increased VLDL but also increased LDL. The phenotypes appear to depend on some other genetic and environmental factors.

Adult↗
PubMed1987

Diet composition and lipoprotein lipase (EC 3.1.1.34) activity in human obesity.

1. Adipose tissue lipoprotein lipase (EC 3.1.1.34; AT-LPL), a rate-limiting enzyme in triglyceride storage in adipose tissue, is hormonally regulated and may be important in the maintenance of obesity. 2. In twelve obese women, AT-LPL activity was measured before weight loss, during weight loss and after 1 and 2 weeks of weight maintenance on either a high-carbohydrate or a high-protein diet. 3. When related to tissue weight, AT-LPL activity during the 2 weeks of weight maintenance was higher than the initial AT-LPL activity; there was no difference when activity was expressed per cell. 4. Changes in AT-LPL activity were not affected by diet composition. AT-LPL activity correlated with insulin levels and a change in insulin sensitivity of AT-LPL was observed after weight loss.

Adipose Tissue↗
PubMed1996

The relation of plasma triglyceride, apolipoprotein B, and high-density lipoprotein cholesterol to postheparin lipoprotein lipase activity is dependent on apolipoprotien E polymorphism.

Postheparin plasma (PH)-lipoprotein lipase (LPL) activity has been reported to be a significant correlate of plasma triglyceride and high-density lipoprotein cholesterol (HDL-C) levels. However, some studies have failed to observe these associations. In this regard, apolipoprotein (apo) E polymorphism may play an important role, since the apo E2 isoform has unfavorable effects on the catabolism of triglyceride-rich lipoprotein particles. We have thus examined the relationships between PH-LPL activity and plasma lipoprotein-lipid levels within groups of men classified on the basis of apo E phenotypes, to verify whether apo E polymorphism could alter these associations. In men carrying the apo E2 isoform (n = 12), PH-LPL activity showed a strong negative correlation with plasma triglyceride (r = -.72, P < .01), very-low-density lipoprotein (VLDL) triglyceride ([VLDL-TG] r = -.83, P < .001), and VLDL cholesterol ([VLDL-C] r = -.57, P < .05) levels and a positive correlation with plasma HDL-C (r = .87, P < .001) and HDL2-C (r=.90, P < .001) concentrations. These correlations were also noted for plasma apo B levels (r = -.65, P < .05), VLDL-apo B concentrations (r= -.76, P < .01), and the HDL-C to cholesterol ratio (r = .85, P < .001). In contrast, none of these associations were found in men carrying the apo E4 isoform (n = 11). In men homozygous for the apo E3 isoform (n = 29), PH-LPL activity was only significantly correlated with plasma HDL2-C levels (r = .46, P < .01). Results of the present study indicate that PH-LPL activity is related to plasma triglyceride, VLDL-TG, VLDL-C, VLDL-apo B, apo B, and HDL-C levels and the HDL-C to cholesterol ratio in men carrying the apo E2 isoform, but not in men homozygous for the apo E3 isoform or among apo E4 carriers. Thus, apo E polymorphism appears to modulate the effect of variation in PH-LPL activity on the plasma lipoprotein profile.

Adult↗
PubMed1995

The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes.

The very low density lipoprotein (VLDL) receptor binds apolipoprotein E-rich lipoproteins as well as the 39-kDa receptor-associated protein (RAP). Ligand blotting experiments using RAP and immunoblotting experiments using an anti-VLDL receptor IgG detected the VLDL receptor in detergent extracts of human aortic endothelial cells, human umbilical vein endothelial cells, and human aortic smooth muscle cells. To gain insight into the role of the VLDL receptor in the vascular endothelium, its ligand binding properties were further characterized. In vitro binding experiments documented that lipoprotein lipase (LpL), a key enzyme in lipoprotein catabolism, binds with high affinity to purified VLDL receptor. In addition, urokinase complexed with plasminogen activator-inhibitor type I (uPA.PAI-1) also bound to the purified VLDL receptor with high affinity. To assess the capacity of the VLDL receptor to mediate the cellular internalization of ligands, an adenoviral vector was used to introduce the VLDL receptor gene into a murine embryonic fibroblast cell line deficient in the VLDL receptor and the LDL receptor-related protein, another endocytic receptor known to bind LpL and uPA.PAI-1 complexes. Infected fibroblasts that express the VLDL receptor mediate the cellular internalization of 125I-labeled LpL and uPA.PAI-1 complexes, leading to their degradation. Non-infected fibroblasts or fibroblasts infected with the lacZ gene did not internalize these ligands. These studies confirm that the VLDL receptor binds to and mediates the catabolism of LpL and uPA.PAI-1 complexes. Thus, the VLDL receptor may play a unique role on the vascular endothelium in lipoprotein catabolism by regulating levels of LpL and in the regulation of fibrinolysis by facilitating the removal of urokinase complexed with its inhibitor.

Adenoviruses, Human↗
PubMed1978

The influence of dietary fat and meal frequency on lipoprotein lipase and hormone-sensitive lipase in rat adipose tissue.

Activities of NaCl-inactivated lipoprotein lipase (LPL) and protamine-resistant hormone-sensitive lipase (HSL) in adipose tissue, accumulation of carcass fat, and serum triglycerides (TG) were determined in meal-fed (MF) and ad libitum-fed (AD) rats. At each feeding frequency, diets provided total fat as 15 or 30% of calories and polyunsaturated fatty acids (PUFA) as 2.5 or 11% of calories. The average energy intake of MF rats was 67% that of AD rats. Total weight gained by MF rats was only 60% that of the AD rats. Significantly greater activities of LPL, HSL, and LPL:HSL in adipose of MF rats suggested a greater capacity for fat accumulation which was not realized at the limited energy intake. In AD rats, the percentage of body fat was significantly correlated with LPL:HSL and with serum TG, suggesting that the relative enzyme activities and fat deposition may be influenced by the concentration of circulating TG. Mean body fat of rats receiving the 30% fat diet was significantly greater than that of rats fed 15% fat. Both serum TG and adipose LPL activity were significantly reduced when the diet contained high levels of PUFA.

Adipose Tissue↗