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PubMed1975

Release of lipoprotein lipase from fat cells in vitro.

Release of lipoprotein lipase from rat fat cells incubated at 20 degrees in medium with albumin, but without glucose proceeded at a constant rate for 30 min. The initial rate of release was increased when serum was present in the medium. Maximal stimulation (100-300%) was produced with 3.8% serum. The maximal increment in release caused by serum was always greater than that produced by heparin and when both were added release was greater than it was with either one alone. The active component(s) of serum, nondialyzable and stable for 30 min at 56 degrees C, was present in sera from humans and rats in the fed or fasted state. Glucose plus insulin (but neither alone) enhanced the rate of lipase release in the presence of serum but not in its absence. The half-life of the lipase in basal medium of 20 degrees C was 90 min. Heparin decreased this to about 50 min and serum markedly prolonged it whether or not heparin was present. Lipoprotein lipase activity in cells and fractions thereof was assayed in extracts of acetone powders. After centrifugation of fat cell homogenates at 600 times g for 15 min, only 50-60% of the activity was recovered in the supernatant. After centrifugation at 100 000 times g for 60 min, the supernatant contained about 10% of the total activity and the sediment 40%. In some experiments, most of the rest was recovered in the floating fat fraction. Total lipoprotein lipase activity of cells plus medium increased steadily during incubation of fat cells for 1h at 30 degrees C. The major increment occurred in the cells and activity in the medium was always less than 15% of the total. Our observations are consistent with the view that activation may be an important determinant of fat cell lipoprotein lipase activity as well as an integral part of the release process.

Adipose Tissue↗
PubMed1983

Influence of nutritional state on lipoprotein lipase activities in the hypothyroid rat.

We have investigated the effects of nutritional state on the lipoprotein lipase activities of the experimentally hypothyroid rat. Both short-term effects (i.e., those of a 24 h fast with and without re-feeding) and long-term effects (due to decreased food intake in hypothyroidism) have been studied. The hypothyroid rats had significantly higher lipoprotein lipase activities of adipose tissue and heart muscle. The effect of hypothyroidism on adipose tissue lipoprotein lipase activities was modified by the nutritional state. In rats studied after 24 h fasting, the hypothyroid group had significantly higher lipoprotein lipase activities than weight-matched, age-matched and pair-fed (i.e., semi-starved) control groups. In rats studied in the re-fed state, the effects of hypothyroidism as such were less evident, since the pair-fed group also demonstrated significantly higher enzyme activities than did the other control groups. We have also studied the lipoprotein lipase activities of different enzyme preparations from adipose tissue. The effects of hypothyroidism were most clearly reflected in an increase of heparin-elutable enzyme activity from adipose tissue, whereas adipocyte lipoprotein lipase activity and the lipoprotein lipase secretion rate from adipocytes were affected to a lesser extent. We conclude that alterations in food intake strongly influence the lipoprotein lipase activities in the hypothyroidism. Our data also imply that the increased lipoprotein lipase activity in the hypothyroid state is due to a decreased degradation of the enzyme, both intra- and extracellularly.

Adipose Tissue↗
PubMedDate not supplied

Uptake and degradation of human chylomicrons by macrophages in culture. Role of lipoprotein lipase.

Because macrophages secrete lipoprotein lipase (LPL), we sought to determine if LPL activity would influence the metabolism of chylomicrons by macrophages. In initial studies, we showed that normal chylomicrons were a substrate for the macrophage's LPL activity. Uptake of normal chylomicrons occurred in a saturable fashion and was effectively competed for by human chylomicrons, very low density lipoproteins (VLDL), and rabbit beta-VLDL, but not by acetyl-low density lipoprotein (LDL), and only modestly by native LDL. When apoprotein C-II-deficient chylomicrons were incubated with macrophages, no hydrolysis of triglyceride occurred, yet saturable uptake of chylomicron protein and lipid occurred, demonstrating that LPL activity is not a prerequisite for saturable uptake. However, addition of apo C-II led to marked hydrolysis and enhanced uptake of protein and lipid moieties. When albumin was present in the medium, there was approximately equal enhancement of cellular content of triglyceride and cholesteryl ester, despite the fact that chylomicrons are triglyceride-rich. This was due to uptake of a triglyceride-depleted particle produced by LPL, as well as a preferential re-release of triglyceride. These studies suggest potential pathways by which triglyceride-rich lipoproteins could contribute to accumulation of cholesteryl esters in macrophages, even while only small amounts of triglyceride accumulate.

Cells, Cultured↗
PubMed1994

Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis.

Lipoprotein lipase and pancreatic lipase have about 30% sequence identity, suggesting a similar tertiary fold. Three-dimensional models of lipoprotein lipase were constructed, based upon two recently determined x-ray crystal structures of pancreatic lipase, in which the active site was in an open and closed conformation, respectively. These models allow us to propose a few hypotheses on the structural determinants of lipoprotein lipase which are responsible for heparin binding, dimer formation, and phospholipase activity. The folding of the protein assembles a number of positive charge clusters at the back of the molecule, opposite the active site. These clusters probably form the heparin binding site, as confirmed by recent site-directed mutagenesis experiments. The active sites of lipoprotein lipase and pancreatic lipase look very similar, except for the lid (a surface loop covering the catalytic serine in the inactive state). A different open (active) conformation of the lid in both enzymes may be responsible for their differing substrate specificities. Predictions of the nature of the lipoprotein lipase dimer remain elusive, although our model enabled us to propose a few possibilities.

Amino Acid Sequence↗
PubMed1993

Different hydrolytic efficiencies of adipose tissue lipoprotein lipase on very-low-density lipoprotein subfractions separated by heparin-Sepharose chromatography.

Human very-low-density lipoproteins (VLDL) were subfractionated by heparin-Sepharose chromatography into an unbound (A) and three bound (B, C and D) populations at increasing ionic strengths. Subfractions were characterized regarding their chemical composition and efficiency of triacylglycerol hydrolysis by rat adipose tissue LPL. The triacylglycerol content decreased, whereas the cholesterol and protein contents increased from subfractions A and B to subfraction D. VLDL-D showed the highest apo E/apo C ratio, though all the subfractions contained appreciable apo E. Appearance of VLDL-A resulted from exceeding the binding capacity of the column, since practically all its particles eluted at positions of bound VLDL under re-chromatography. Subfractions B, C and D stimulated LPL activity on emulsified tri[14C]oleoylglycerol to a similar extent, indicating that their apo C-II content was equally effective activating LPL. Incubation of tri[14C]oleoylglycerol labeled VLDL subfractions with fat pad pieces in the presence or absence of heparin resulted in greater hydrolysis and fatty acid uptake for VLDL-B and -C than for VLDL-D, a pattern observed over a wide range of LPL activities in the media. We conclude: (1) any VLDL particle can interact with heparin, which is consistent with the presence of apo E in all the subfractions, and (2) triacylglycerols in apo E-rich VLDL are less efficiently hydrolyzed by LPL than those in apo E-poor particles. We propose that richness in apo E impairs LPL action upon VLDL and decreases the rate of delivery of fatty acids to peripheral tissues.

Adipose Tissue↗
PubMedDate not supplied

[Activity of postheparin lipoprotein lipase in rabbit blood plasma].

Activity of lipoprotein lipase was studied in rabbit blood plasma after administration of heparin at a dose 50 un/kg into animals. NaCl was added to incubation mixture at final concentration 1 M to differentiate the enzyme from liver triglyceride lipase. The salt inhibited strongly (sometimes completely) the lipolytic activity in rabbit postheparin blood plasma. These data suggest predominance of lipoprotein lipase, sensitive to NaCl, in total lipolytic activity of rabbit postheparin blood plasma. Only slight alterations in the value of total lipolytic activity and in activity, depending on lipoprotein lipase, were observed in rabbits maintained at high cholesterol diet. Under these conditions distinct increase in activity of triglyceride lipase, stable to NaCl , was not found.

Animals↗
PubMed1993

Lipoprotein lipase in human plasma is mainly inactive and associated with cholesterol-rich lipoproteins.

This study was designed to further ascertain the presence in plasma of lipoprotein lipase (LPL) bound to circulating lipoproteins. Lipoprotein lipase mass and activity values in preheparin plasma from 20 volunteers were 69.8 +/- 6.6 ng.ml-1 and 1.54 +/- 0.15 mU.ml-1, respectively, and no significant correlation between mass and activity was observed. Fifteen min after heparin injection, LPL mass had increased to 536 +/- 60 ng.ml-1 and LPL activity to 261 +/- 34 mU.ml-1 and a highly significant correlation between the increments in mass and activity was observed. The released material had a specific activity of 0.57 +/- 0.03 mU.ng-1. The LPL mass in preheparin plasma eluted early from heparin-Sepharose, in the position expected for inactive LPL monomers. Western blot analysis showed that the eluted material had the size expected for the LPL subunit (55 kDa). The increment of mass and activity after heparin eluted later from heparin-Sepharose, in the position expected for active LPL dimers. It is concluded that preheparin plasma contains substantial amounts of inactive LPL protein, and that heparin releases mainly active LPL into circulation. On gel filtration LPL activity and mass in postheparin plasma eluted mainly in the positions of LDL and HDL. Electron microscopy of immunostained fractions showed reaction for LPL and apolipoprotein B, or apolipoprotein A-I, on the same particles. LPL mass in preheparin plasma eluted in a similar pattern, associated with LDL and HDL. In postprandial plasma substantial amounts of LPL protein eluted with the triglyceride-rich lipoproteins. When 125I-labeled bovine LPL was added to plasma or to ultracentrifugally isolated lipoproteins and then analyzed by gradient gel electrophoresis, the labeled lipase moved with the lipoproteins. The presence of substantial amounts of inactive LPL protein associated with lipoproteins in plasma may have important implications for the metabolism of the particles in view of recent reports on avid binding of LPL-lipoprotein complexes to cell surfaces and receptors.

Apolipoproteins↗
PubMed1987

Human genes involved in lipolysis of plasma lipoproteins: mapping of loci for lipoprotein lipase to 8p22 and hepatic lipase to 15q21.

We have used cDNA probes for lipoprotein lipase and hepatic lipase to determine the chromosomal and subchromosomal locations of the human genes for these lipolytic enzymes. Southern blot analysis of genomic DNA from 17 independent mouse-human somatic cell hybrids demonstrated the presence of the gene for human lipoprotein lipase on chromosome 8, whereas the gene for hepatic lipase was on chromosome 15. Regional mapping of the genes by in situ hybridization to human chromosomes indicated that the lipoprotein lipase gene (LPL) resides in the p22 region of chromosome 8, while hepatic lipase gene (HL) resides in the q21 region of chromosome 15. We previously reported, on the basis of nucleotide and amino acid homologies, that these genes are members of a gene family of lipases, and, thus, the present findings indicate that the members of this family are dispersed. The results are also of significance with respect to disorders involving deficiencies of the enzymes. In particular, they suggest that certain rare combined deficiencies of both enzymes do not involve mutations of the structural loci.

Animals↗
PubMed1999

Physical activity modulates the effect of a lipoprotein lipase mutation (D9N) on plasma lipids and lipoproteins.

We investigated interactions between a mutation (D9N) in the lipoprotein lipase (LPL) gene and physical activity, as well as other lifestyle factors, on lipid traits in a population-based sample of Dutch men and women (n = 379). We used questionnaire information to classify physical activity, alcohol consumption, and smoking habits, while overweight was defined as a body mass index (BMI) > 25 kg/m2. Non-fasting blood samples were used for the determination of lipid traits and the D9N genotype. Fifteen subjects (4%) carried the mutation. They presented with higher levels of total cholesterol, apolipoprotein (apo) B and triglycerides compared to non-carriers. While no interactions with overweight, alcohol consumption, and smoking were found, a strong interaction between the D9N mutation and physical activity became apparent. Physically inactive D9N carriers (n = 5) had considerably higher total cholesterol (+2 mmol/l, p < or = 0.0001) and apo B levels (+63 mg/dl, p < or = 0.0001) compared to non-carriers of this mutation, whereas their high-density lipoprotein (HDL)-cholesterol concentrations were lower (-0.22 mmol/l, p < 0.05). This was not the case for physically active D9N carriers (n = 10). In conclusion, a common variant of the LPL gene (D9N) adversely affects plasma lipid and lipoprotein profiles. However, the unfavorable consequences may be counteracted by physical activity.

Adult↗
PubMed1986

Primary lipoprotein lipase deficiency.

The enzyme lipoprotein lipase plays a central role in the processing of energy in the form of calorically dense triglyceride. Classical LPL deficiency usually presents in childhood with the multiple manifestations related to chylomicronemia. Many patients with genetic variations have been noted who differ in one of many ways from the classical patients. With the development of techniques to measure enzyme mass and to study gene expression, the molecular defects in each of these families should become evident.

Adipose Tissue↗
PubMed1989

The effect of dietary fish oil on muscle and adipose tissue lipoprotein lipase.

The activity of lipoprotein lipase (LPL) in the adipose tissue and skeletal muscle of rats fed glucose- or fructose-based diets containing fish oil, corn oil or tallow was examined. In addition, heart LPL activity was measured in rats fed a glucose-based diet containing either corn oil or fish oil. Adipose tissue LPL activity was unaffected by dietary fat. In both heart and skeletal muscle, LPL activity was higher in rats fed the fish oil diet. These results suggest that increased removal of triglyceride by muscle may contribute to the blood triglyceride lowering effect of dietary fish oil.

Adipose Tissue↗