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PubMed1986

Lipoprotein lipase in guinea pig tissues: molecular size and rates of synthesis.

Lipoprotein lipase was immunoprecipitated from guinea pig tissues which had been pulse labeled with [35S]methionine. The apparent size of the product (on SDS gels) was 55 kDa in all tissues studied. Lipoprotein lipase released by heparin from adipocytes and from perfused hearts had the same apparent size. No significant amounts of immunoreactive protein with smaller size were found on immunoblotting of tissue homogenates, or in preparations partially purified by heparin-Sepharose chromatography. Lipoprotein lipase accounted for only a small proportion of total protein synthesis. The highest value was in adipose tissue (0.3-0.8%). In lactating mammary gland lipoprotein lipase accounted for about 0.1%, a figure similar to that previously estimated for the proportion of lipoprotein lipase protein in milk. This suggests that lipoprotein lipase is secreted into milk as efficiently as other milk proteins are, in contrast to the previous opinion that the enzyme appears in milk because small amounts leak out from tissue sites. Relative synthesis of lipoprotein lipase was the same in adipocytes from fed or fasted animals, whereas relative synthesis of several other proteins changed dramatically. This indicates that some proteins in guinea pig adipose tissue are under transcriptional control in response to feeding-fasting, but that lipoprotein lipase is not.

Adipose Tissue↗
PubMed1995

In vitro and in vivo analysis of murine lipoprotein lipase gene promoter: tissue-specific expression.

Lipoprotein lipase, an enzyme of central importance to lipid metabolism, is most abundant in adipose tissues, cardiac and skeletal muscle, and portions of the brain. The current work examined the murine lipoprotein lipase promoter using transient transfection, gel-retention analyses, and transgenic mice. Maximum expression of the luciferase reporter gene in transfected cells was observed with -101 bp of the promoter. Nuclear extracts from tissues expressing lipoprotein lipase contained DNA binding proteins that recognize the CCAAT box (-64 bp) and an octamer motif (-46 bp); this combination of factors was absent in nonexpressing tissues. Transgenic mice from three of five founders prepared with -1,824-bp promoter constructs expressed the luciferase reporter gene at highest levels in brown adipose tissue and brain. These findings suggest that the -1,824-bp promoter region contains sequence elements responsible for the tissue-specific transcription of lipoprotein lipase in vivo.

Animals↗
PubMed1986

Characterization of rat adipose tissue lipoprotein lipase using a monospecific antibody.

An antibody to a highly pure enzyme preparation was developed to facilitate detailed studies of rat adipose tissue lipoprotein lipase regulation. Lipoprotein lipase was purified by heparin-Sepharose affinity chromatography followed by preparative isoelectric focusing. The enzyme migrated as a single broad band on SDS disc gel and two-dimensional gel electrophoresis with an apparent molecular mass of 67 000 and 62 000 Da, respectively. The amino acid composition of the purified rat enzyme was virtually identical to that of bovine milk. A major protein component with no lipase activity co-eluted with the enzyme from the affinity column, but was separated by the isoelectric focusing step. The molecular mass was slightly lower (58 000 Da) but the amino acid composition of this protein was similar to that of the enzyme. An antibody raised against the purified rat enzyme was highly potent and was effective in inhibiting rat heart lipoprotein lipase, but not the salt-resistant hepatic lipase. Analysis of crude acetone-ether adipose tissue preparation on SDS slab polyacrylamide gel coupled to Western blotting revealed five protein bands = (62 000, 56 000, 41 700, 22 500, 20 000 Da). Similarly, following affinity purification by immunoadsorption, the purified antibody reacted with five equivalent protein bands. Fluorescent concanavalin A binding data indicated that the 56 kDa band is a glycosylated form of lipoprotein lipase. Pretreatment of adipose tissue with proteinase inhibitors revealed that the lower molecular mass proteins (41 700 and 20 000 Da) were degradation products of lipoprotein lipase, and the 22 500 Da band could be accounted for by non-specific binding.

Adipose Tissue↗
PubMed1980

Cigarettes smoking and adipose tissue lipoprotein lipase.

Adipose-tissue lipoprotein-lipase activity was measured in otherwise healthy smokers and compared with that of a nonsmoking control population. Adipose-tissue lipoprotein-lipase activity was significantly higher (P < 0.001) in smokers (5.4 +/- 2.6 mU/10(6) cells) than in controls (1.9 +/- 0.7 mU/10(6) cells) of similar weight.

Adipose Tissue↗
PubMed1999

Functional variants in the lipoprotein lipase gene and risk cardiovascular disease.

The current report is a quantitative review of the relationship between lipoprotein lipase gene variants and cardiovascular disease based on published population-based studies. Sixteen studies, representing 17,630 individuals, report allelic distribution for lipoprotein lipase gene variants among patients and control individuals. Patient outcomes included clinical cardiovascular disease events, documented coronary disease based on angiography, or intimal media thickening by B-mode ultrasonography. Mantel-Haenszel stratified analysis was used to compute a summary odds ratio and 95% confidence intervals for the association between rare allele in the lipoprotein lipase gene and disease status. Because of potential differing effects associated with different lipoprotein lipase variants, each lipoprotein lipase mutant allele was considered separately. The lipoprotein lipase D9N/-93G to T allele has a summary odds ratio of 2.03 (95% confidence interval 1.30-3.18), indicating a twofold increase in risk of coronary disease for carriers with this allelic variant. The summary odds ratio for the relationship of the rare lipoprotein lipase G188E variant with cardiovascular disease is 5.25 (95% confidence interval 1.54-24.29). The lipoprotein lipase N291S allele is associated with a marginal increase in cardiovascular disease (summary odds ratio 1.25, 95% confidence interval 0.99-1.60, P = 0.07). However, there is stronger evidence for a positive association in certain populations. The summary odds ratio for lipoprotein lipase S447X allele is 0.81 (95% confidence interval 0.65-1.0), which indicates a cardioprotective effect of this lipoprotein lipase gene variant. Thus, lipoprotein lipase gene variants are associated with differential susceptibility to cardiovascular disease.

Alleles↗
PubMed2002

Endothelial-derived lipoprotein lipase is bound to postprandial triglyceride-rich lipoproteins and mediates their hepatic clearance in vivo.

Lipoprotein lipase (LPL) is the key enzyme in the intravascular hydrolysis of triglyceride-rich lipoproteins (TRL). Furthermore, it has been shown that inactive LPL can mediate cellular binding and uptake of TRL in vitro. This study investigated whether LPL is bound to postprandial human TRL in vivo, and whether it plays a role in the hepatic clearance of these particles independent of its catalytic activity. LPL was found to bind to postprandial TRL in preheparin plasma of healthy young men. To study the effect of inactive LPL on particle uptake, TRL isolated from patients with inactive LPL (LPL or apoC-II mutations) were used before and after heparin administration. These model particles allow one to study the bridging effect of LPL independent of its enzymatic activity. Organ uptake studies with these particles in mice revealed that inactive LPL increases the hepatic clearance of TRL significantly while uptake into other organs remains largely unaffected. Further evidence that endothelial-derived LPL directs TRL to the liver in vivo was gained with transgenic mice that express inactive LPL exclusively in muscle, revealing greater hepatic uptake than in wild-type mice. In conclusion, these data demonstrate for the first time that LPL is a structural component of postprandial TRL which facilitates hepatic TRL clearance from the circulation independent of its catalytic function.

Adult↗
PubMed1986

Dibutyryl cyclic AMP decreases the rate of lipoprotein lipase synthesis in cultured adipocytes.

The regulation of avian lipoprotein lipase by dibutyryl cyclic AMP in cultured adipocytes was studied with quantitative and specific methods for the measurements of enzyme catalytic activity, enzyme protein mass, and immunoadsorption of labeled enzyme. Incubation of adipocytes in 0.5 mM dibutyryl cyclic AMP plus 0.5 mM theophylline results in a time-dependent decrease in cell lipoprotein lipase catalytic activity. The activity is decreased by 70% in 4 h and over 90% by 12 h. The decrease in cellular catalytic activity is due to a decrease in both enzyme content and enzyme catalytic efficiency. 4 h after exposure of adipocytes to cAMP, enzyme protein was decreased from 3.58 +/- 0.5 to 1.92 +/- 0.1 ng/dish and specific activity from 15.1 +/- 2.1 to 8.4 +/- 1.1 nmol/ng. In the presence of 0.5 mM theophylline, the dibutyryl cyclic AMP-mediated decrease in lipoprotein lipase activity was half-maximal at less than 25 microM dibutyryl cyclic AMP. The rate of lipoprotein lipase synthesis was estimated by measuring the incorporation of L-[35S]methionine into enzyme protein during 30 min. A method for the quantitative immunoadsorption of lipoprotein lipase from cell lysates was developed. Utilizing this immunoadsorption technique, the rate of incorporation of L-[35S]methionine into lipoprotein lipase was 0.0026 +/- 0.002%, when expressed as a percentage of that incorporated into total trichloroacetic acid-precipitable counts. By 2 h after exposure of adipocytes to 0.5 mM dibutyryl cAMP, the relative synthesis rate had already decreased to 64 +/- 4% of the control rate. After 16 h the synthesis rate was 43.2 +/- 13.8% of the control rate. The observed decreased synthesis rate could account for most of the decreased cellular enzyme content and diminished enzyme secretion rate.

Adipose Tissue↗
PubMed1994

Characterization of a fluorometric method for lipoprotein lipase.

A fluorometric assay for determining lipoprotein lipase (LPL) activity is described. Dibutyrilfluorescine (DBF) was used as substrate for the enzyme and the fluoresceine liberated by enzymatic hydrolysis of the substrate was measured. Extracts of acetone powder from adipose tissue as an enzyme source showed characteristics of lipoprotein lipase activity, i.e., inhibition by NaCl and optimum activity in alkaline pH. There was close agreement in LPL activity when the same sample was measured simultaneously using either dibutyrilfluorescine or tri[9,10(3)H]oleylglycerol as substrate. The extent of inhibition of lipoprotein lipase by NaCl was similar with both methods. The fluorometric method detected changes in LPL activity in heart and adipose tissue related to the nutritional status of the animal with the same specificity and sensitivity than did the radioactive method. The fluorometric method is as sensitive, less expensive and less time consuming than the radioactive method.

Animals↗
PubMed1983

Lipoprotein lipase of sheep and rat adipose tissues.

Lipoprotein lipase preparations were obtained by aqueous extraction of various tissues from sheep and rats. Preparations having high activity towards serum-activated triolein emulsions were obtained from actively growing sheep, provided that the tissue was maintained at 37 degrees C throughout the extraction procedure. Activity of lipoprotein lipase from sheep adipose tissue, like that from the rat, was dependent upon the presence of serum in the reaction mixture, and was optimal at pH 8-9. Inhibition of sheep adipose tissue preparations by protamine sulfate (1 mg/ml) and 0.6 M NaCl was similar to that found for rat adipose tissue preparations. The affinity of the lipoprotein lipase preparation for the activated substrate from sheep and rat adipose tissue was, however, markedly different; sheep preparations being activated at much lower substrate concentrations (Km 0.43 mM) than rat preparations (Km greater than 5 mM). These findings, confirmed with acetone-ether preparations of lipoprotein lipase, indicate that the enzyme from sheep adipose tissue has a greater potential to remove triacylglycerol from the plasma. This could result in a greater deposition of fat in the tissue.

Adipose Tissue↗
PubMed1999

The effect of insulin sensitizer, troglitazone, on lipoprotein lipase mass in preheparin serum.

Lipoprotein lipase mass exists in preheparin serum, even though the activity is scarcely found. The implication of this is unclear. We studied the effect of an insulin sensitizer, troglitazone, on this preheparin serum lipoprotein lipase mass (preheparin LPL mass) in non-insulin-dependent diabetes mellitus (NIDDM) patients as well as on serum lipid levels and low density lipoproteins (LDL) particle size. Thirty-one NIDDM patients with poor control were administered troglitazone 400 mg/day. Hemoglobin A1c had significantly decreased (13%, P < 0.001) 2 months later. Preheparin LPL mass had gradually increased and a 69% increase (P<0.01) was observed 4 months later. Triglyceride significantly decreased (23%, P < 0.01) and high density lipoprotein-cholesterol increased (10%, P < 0.01), whereas total cholesterol and LDL levels did not change 4 months later. The size of LDL increased significantly (P < 0.01). These results were consistent with the idea that preheparin LPL mass might be relating to the insulin sensitivity enhanced by troglitazone, as well as LDL particle size.

Adult↗
PubMed1977

Antibodies to lipoprotein lipase. Application to perfused heart.

An antibody was prepared against purified rat heart lipoprotein lipase. 1. This antibody showed marked species specificity. It inhibited almost totally the lipoprotein lipase activity from all rat tissues examined (i.e., heart, adipose, postheparin plasma, and mammary gland), while having no effect on the activity of lipoprotein lipase partially purified from rabbit, guinea pig and bovine heart and from bovine milk. The antibody also had no effect on the hepatic lipase activity of rat postheparin plasma. 2. After antibody to rat heart lipoprotein lipase was recirculated for 5 min through isolated rat hearts, little or no lipoprotein lipase activity could be detected in the perfusate during 0-20 s of a subsequent non-recirculating perfusion with buffer containing 1 unit heparin/ml. 3. Following recirculation of antibody to lipoprotein lipase for 10 min and a non-recirculating perfusion with buffer for 2 min, the hearts no longer oxidized any significant amounts of 14C-labelled palmitate chylomicron triacylglycerol fatty acid to 14CO2 during a 15-min perfusion. The data give compelling evidence that the functional fraction of lipoprotein lipase in hearts is at the endothelial cell surface accessible to lipoprotein lipase antibody.

Animals↗
PubMed1978

The effect of nutritional state on the lipoprotein lipase activity of isolated fat cells.

The lipoprotein lipase activity of rat epididymal adipose tissue falls on starvation and increases on refeeding. Studies with fat cells isolated from this tissue have shown that increases in the activity of the enzyme occur under appropriate incubation conditions in vitro. The present study compares the responses of cells isolated from the adipose tissue of fed and 48-h starved rats. Fat cells from rats starved for 48 h display a lower initial lipoprotein lipase activity than cells from fed rats. When cells from rats in both nutritional states are incubated in a suitable medium at 25 degrees C, there is a progressive increase in the medium lipoprotein lipase activity. The absolute increase in the total activity of the incubation system during incubations of cells from 48-h starved rats is significantly less than during incubations of cells from fed rats. However, when expressed as a percentage of the initial cell activity, the rises in total activity are similar in the two nutritional states. Cycloheximide has no significant effect on the increase in activity of lipoprotein lipase that occurs with cells from 48-h starved rats. However, it does partially block the increase in activity seen with cells from fed rats and in a manner similar to that previously reported for cells from 24-h starved rats. The significance of the results is discussed in relation to previous studies with both intact adipose tissue and isolated fat cells.

Adipose Tissue↗
PubMed1993

Lipoprotein lipase in developing rat tissues: differences between Wistar and Sprague-Dawley rats.

Lipoprotein lipase in animal tissues is known to be affected by fasting, but contradictory results have been published concerning this effect in particular tissues. For example, we reported that lipoprotein lipase activity expressed in the liver of neonatal rats was either increased or not affected by fasting. To evaluate the influence of the rat strain used as experimental animal model, we studied differences between Wistar and Sprague-Dawley rats in the development and in the effect of fasting on lipoprotein lipase and hepatic lipase activities in tissues of neonatal rats. Beside some minor differences in the development of lipoprotein lipase in some tissues like brown adipose tissue and lungs, we found quite remarkable differences between both strains in the development of lipoprotein lipase and hepatic lipase activities in the liver. In 1-day-old neonates, differences between both strains were also observed in the effect of fasting on lipoprotein lipase activity both in liver and lungs. In the liver of Wistar pups lipoprotein lipase activity was increased by fasting by 350%, but only by 50% in the liver of Sprague-Dawley pups. In contrast, in the lungs of Wistar pups lipoprotein lipase activity was increased by fasting by 280%, but by 580% in lungs of Sprague-Dawley rats. Therefore, our results indicate that quantitative differences exist between Wistar and Sprague-Dawley rats in the regulation of lipoprotein lipase.

Adipose Tissue, Brown↗
PubMed1987

High-cholesterol diet-induced lipoproteins stimulate lipoprotein lipase secretion in cultured rat alveolar macrophages.

We have previously shown that cultured rat alveolar macrophages synthesize and secrete lipoprotein lipase into the medium. The purpose of the present experiments is to examine whether cholesterol-enriched lipoproteins from cholesterol-fed animals have any effects on the lipoprotein lipase secretion and the lipid accumulation in macrophages. Macrophages incubated with the VLDL obtained from rats fed a normal diet secreted 2-fold higher amounts of lipoprotein lipase than those without lipoproteins. Intermediate-, low- and very-low-density lipoproteins from rats fed a high-cholesterol diet also enhanced the lipoprotein lipase secretion. Normal high- and low-density lipoproteins, and high-density lipoproteins from hypercholesterolemic animals did not cause any increase in the lipoprotein lipase secretion. The lipoproteins which stimulated the lipoprotein lipase secretion caused intracellular accumulation of both triacylglycerol and cholesterol. It is speculated that macrophages residing in the environment rich in lipoproteins, especially hypercholesterolemic lipoproteins, take them up and accumulate lipids intracellularly, and that this process links with the lipoprotein lipase secretion. The secreted lipoprotein lipase could facilitate, by degrading lipoproteins, the uptake of lipoprotein lipase-modified lipoproteins. Probably such a series of events is of importance in the foam cell formation of macrophages.

Animals↗
PubMed1989

Lipoprotein lipase activity in neonatal-rat liver cell types.

The lipoprotein lipase activity in the liver of neonatal (1 day old) rats was about 3 times that in the liver of adult rats. Perfusion of the neonatal liver with collagenase decreased the tissue-associated activity by 77%. When neonatal-rat liver cells were dispersed, hepatocyte-enriched (fraction I) and haemopoietic-cell-enriched (fraction II) populations were obtained. The lipoprotein lipase activity in fraction I was 7 times that in fraction II. On the basis of those activities and the proportion of both cell types in either fraction, it was estimated that hepatocytes contained most, if not all, the lipoprotein lipase activity detected in collagenase-perfused neonatal-rat livers. From those calculations it was also concluded that haemopoietic cells did not contain lipoprotein lipase activity. When the hepatocyte-enriched cell population was incubated at 25 degrees C for up to 3 h, a slow but progressive release of enzyme activity to the incubation medium was found. However, the total activity (cells + medium) did not significantly change through the incubation period. Cycloheximide produced a time-dependent decrease in the cell-associated activity. Heparin increased the amount of lipoprotein lipase activity released to the medium. Because the cell-associated activity was unchanged, heparin also produced a time-dependent increase in the total activity. In those cells incubated with heparin, cycloheximide did not affect the initial release of lipoprotein lipase activity to the medium, but blocked further release. The cell-associated activity was also decreased by the presence of cycloheximide in those cells. It is concluded that neonatal-rat hepatocytes synthesize active lipoprotein lipase.

Animals↗
PubMed1994

Effect of protamine on lipoprotein lipase and hepatic lipase in rats.

The polycation protamine impedes the catabolism of triglyceride-rich lipoproteins and this has been suggested to be due to intravascular inactivation of lipoprotein lipase. We have made intravenous injections of protamine to rats and found that both lipoprotein lipase and hepatic lipase activities were released to plasma. The effect of protamine was more short-lived than that obtained by injection of heparin. The release of hepatic lipase by protamine was as effective as the release by heparin, while the amount of lipoprotein lipase released by protamine was only about one-tenth of that released by heparin. This was not due to inactivation of lipoprotein lipase, since injection of an excess of heparin 10 min after injection of protamine released as much lipoprotein lipase activity to plasma as in controls. The results in vivo differed from those obtained in model experiments in vitro. Protamine was able to almost quantitatively release both lipoprotein lipase and hepatic lipase from columns of heparin-agarose. The displacement was dependent on the total amount of protamine that had passed over the column, indicating that it was due to occupation by protamine of all available binding sites. Our results in vivo showed that the binding sites for lipoprotein lipase were not blocked as efficiently as those for hepatic lipase, indicating that the binding structures were not identical. It was concluded that the impaired turnover of lipoproteins by protamine probably was due to prevention of binding of the lipoproteins to endothelial cell surfaces rather than to impaired lipase function.

Animals↗