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PubMed1977

Breast milk composition in Ethiopian and Swedish mothers. IV. Milk lipases.

The (potential) activities of the two lipases in human milk were determined in breast milk samples collected from Ethiopian and Swedish mothers. The major lipase in human milk is dependent on bile salts for activity and probably participates in intestinal digestion of milk lipids in the newborn. The level of this lipase in the milk did not change with time after parturition, but differed between the groups so that it was higher in the privileged Ethopian mothers than in the nonprivileged Ethiopian mothers, who in turn had a higher level than the Swedish mothers. The other lipase is a serum-stimulated lipase (lipoprotein lipase). The level of this lipase varied between samples from different mothers as well as between different samples from the same mother. It tended to be lower in samples obtained at 4 to 5 days after parturition (Swedish mothers) than in later samples. There were in this case no significant differences between nonprivileged and privileged Ethiopian mothers or between them and Swedish mothers.

Adolescent↗
PubMed1976

Studies on triglyceride lipases from rat adipose tissue.

A new assay procedure for triglyceride lipase [EC 3.1.1.3] was developed in which radioactive triolein was dissolved in ethanol and directly added to the reaction mixture in the absence of serum and albumin. In the rat adipose tissue there appeared to be a triglyceride lipase measurable with this assay in addition to the two previously defined lipases, lipoprotein lipase [EC 3.1.1.34] and hormone-sensitive lipase. The enzyme was active in the absence of serum and was strongly inhibited by albumin. The molecular weight was estimated to be about 42,000. Adenosine 3',5'-monophosphate-dependent protein kinase [EC 2.7.1.27] was unable to activate the enzyme. The three species of lipases mentioned above behaved differently upon chromatography on a Sepharose 4B column, and were distinguishable from each other in their physical and kinetic properties. The physiological roles of the new species of lipase remain to be explored.

Adipose Tissue↗
PubMed1984

Post-heparin hepatic and lipoprotein lipase activities in nephrotic syndrome.

Lipid metabolism was studied in 18 patients with nephrotic syndrome due to various glomerulonephritides. Nephrotic patients had hypercholesterolemia with or without hypertriglyceridemia. The mean serum high-density lipoprotein cholesterol concentration was not significantly reduced in nephrotic patients. Hepatic lipase and lipoprotein lipase activities were measured selectively in post-heparin plasma from all 18 patients using a substrate-specific method. The mean lipoprotein lipase activity in nephrotic patients was markedly reduced while the mean hepatic lipase activity was not significantly different from that of controls. Lipoprotein lipase activities correlated inversely with serum triglyceride concentrations, but positively with in vivo post-heparin fractional clearance rates of Intralipid and with serum high-density lipoprotein concentrations. Nephrotic serum inhibited lipoprotein lipase activity in normal subjects. The percentage inhibition, however, did not correlate with the degree of hypertriglyceridemia. A relatively weak inverse correlation was shown to exist between plasma albumin concentration and hepatic lipase activities.

Adolescent↗
PubMed1980

Lipoprotein lipase of human postheparin plasma and adipose tissue in relation to physical training.

Adipose tissue lipoprotein lipase and postheparin plasma triglyceride lipase activities were measured in 28 men differing in their physical training activity. They were divided into 4 subclasses based on their training intensity. The two most active classes (17 subjects) having regular heavy exercise at least 4 times a week were considered as the actively training group, and the other two (11 subjects) classes not training regularly as the control group. In postheparin plasma, the lipoprotein lipase activities were not different between the two groups, whereas training subjects had significantly (P less than 0.02) lower hepatic lipase activities. Adipose tissue lipoprotein lipase activity was in the training group at about 70% higher level on an average than in the controls (P less than 0.10). A significant positive correlation (r = 0.38, P less than 0.05) was obtained between the adipose tissue lipoprotein lipase activity and the level of physical activity. Our data suggest that even moderate inter-group differences in the physical training activity are reflected as measurable alterations in the adipose tissue lipoprotein lipase activity in man.

Adipose Tissue↗
PubMedDate not supplied

Plasma lipoproteins in familial hepatic lipase deficiency.

We have studied the lipoproteins, apolipoproteins, and postheparin lipase activities in an extended pedigree with familial hepatic lipase deficiency. A deficiency of hepatic lipase was found in three of five brothers and in one of their children. Triglyceride enrichment of low density and high density lipoproteins was identified as the constitutive phenotype. beta-very low density lipoprotein was observed in hepatic lipase-deficient subjects, but it was absent when the plasma triglyceride concentration was less than 1 mM/l. The hepatic lipase-deficient subjects had normal or elevated low density lipoprotein cholesterol and high density lipoprotein cholesterol concentrations. Hyperprebetalipoproteinemia, hyperbetalipoproteinemia, and hyperalphalipoproteinemia were observed in both affected and unaffected family members. Compared with the unaffected family members, the hepatic lipase-deficient subjects had no significant differences in very low density lipoprotein cholesterol, very low density lipoprotein triglyceride, or low density lipoprotein cholesterol. These observations are consistent with the presence of additional genes causing hyperlipidemia in this family, independent of the deficiency of hepatic lipase.

Apolipoproteins↗
PubMed1987

Regulation of bovine adipose tissue metabolism during lactation. 3. Adaptations of hormone-sensitive and lipoprotein lipases.

Activity of lipases in adipose tissue during pregnancy and lactation was investigated in Holstein cows producing 5950 to 10,000 kg milk per 305 d. Activity of cytoplasmic lipoprotein lipase per gram of tissue was 97, 78, 140, 162, 179, and 235% of 30 d prepartum at -15, 15, 30, 60, 180, and 349 d about calving in yr 1. In yr 2, lipoprotein lipase per gram was 100, 259, 838, 791, and 430% of -30 d at -15, 30, 60, 120, and 180 d. Adaptations in activity per milligram cytoplasm protein were similar to those per gram tissue. Hormone-sensitive lipase per milligram protein was 161, 251, 114, 126, and 252% of -30 d when measured at 30, 60, 120, 180, and 240 d postpartum. Activity per gram of tissue responded similarly to the lactation state. Lipoprotein lipase is thus not a large contributor to the peripartum bovine adipose adaptation but is important in reattainment of body composition in mid and late lactation. Hormone-sensitive lipase is also increased during peak and midlactation. The pattern of elevated activity of these oppositely directed lipases reflects the dichotomous forces of milk fat production and body fat recovery acting on adipose tissue of lactating heifers.

Adipose Tissue↗
PubMed2000

PLTP activity in premenopausal women. Relationship with lipoprotein lipase, HDL, LDL, body fat, and insulin resistance.

Plasma phospholipid transfer protein (PLTP) is thought to play a major role in the facilitated transfer of phospholipids between lipoproteins and in the modulation of high density lipoprotein (HDL) particle size and composition. However, little has been reported concerning the relationships of PLTP with plasma lipoprotein parameters, lipolytic enzymes, body fat distribution, insulin, and glucose in normolipidemic individuals, particularly females. In the present study, 50 normolipidemic healthy premenopausal females were investigated. The relationships between the plasma PLTP activity and selected variables were assessed. PLTP activity was significantly and positively correlated with low density lipoprotein (LDL) cholesterol (r(s) = 0.53), apoB (r(s) = 0.44), glucose (r(s) = 0.40), HDL cholesterol (r(s) = 0.38), HDL(3) cholesterol (r(s) = 0.37), lipoprotein lipase activity (r(s) = 0.36), insulin (r(s) = 0.33), subcutaneous abdominal fat (r(s) = 0.36), intra-abdominal fat (r(s) = 0.29), and body mass index (r(s) = 0.29). HDL(2) cholesterol, triglyceride, and hepatic lipase were not significantly related to PLTP activity. As HDL(2) can be decreased by hepatic lipase and hepatic lipase is increased in obesity with increasing intra-abdominal fat, the participants were divided into sub-groups of non-obese (n = 35) and obese (n = 15) individuals and the correlation of PLTP with HDL(2) cholesterol was re-examined. In the non-obese subjects, HDL(2) cholesterol was found to be significantly and positively related to PLTP activity (r(s) = 0.44). Adjustment of the HDL(2) values for the effect of hepatic lipase activity resulted in a significant positive correlation between PLTP and HDL(2) (r(s) = 0.41), indicating that the strength of the relationship between PLTP activity and HDL(2) can be reduced by the opposing effect of hepatic lipase on HDL(2) concentrations. We conclude that PLTP-facilitated lipid transfer activity is related to HDL and LDL metabolism, as well as lipoprotein lipase activity, adiposity, and insulin resistance.

Adipose Tissue↗
PubMed1992

Why is there sequence similarity between insect yolk proteins and vertebrate lipases?

The major proteins stored in the yolk of developing oocytes are thought to provide a nutritional store for utilization during embryogenesis. They seem to fall into two major families of proteins. The first are called vitellogenins and are found in frog, chicken, nematode, fish, and some insects such as the boll weevil. The other group are called yolk proteins and are found in dipteran insects such as fruitfly, housefly, fleshfly, and blue-bottles. Both groups are the major proteins found in the oocyte and are female-specific proteins endocytosed from the serum or hemolymph. The yolk protein group were found to have sequence similarity to the triacylglycerol lipases and lipoprotein lipases of vertebrates, including rat, pig, and human. The yolk proteins do not have lipase activity, but the sequences conserved between yolk proteins and lipases surround the active site where there are interactions with lipids. The likely reason for the presence of this domain in the yolk proteins is to bind a steroid hormone in a storage form conjugated to lipids. This permits the storage of the hormone in an inactive form until the yolk proteins are degraded, when it can be released from its conjugate to induce developmental decisions in embryogenesis. They may also transport lipids into the oocyte for use in embryogenesis. Whilst the vitellogenin family of proteins do not share this homology with the lipases they do have similarity to the human serum protein, apolipoprotein B, which also has a role in binding lipids. These findings are discussed in relation to the evolution and functions of lipases, apolipoproteins, vitellogenins, and yolk proteins. Experiments aimed at isolating genes encoding lipases in insects and at further elucidating the function of the yolk proteins are suggested.

Amino Acid Sequence↗
PubMed1990

Relationship between lipase and esterase.

There are at least two sites on the lipase which are concerned with catalysis: the catalytic site and the hydrophobic recognition site (lipid-binding site). The recognition site may be destroyed by mild proteolytic digestion, but the catalytic site may not be changed by this treatment. Mild treatment with trypsin caused change in the catalytic properties of hepatic triglyceride lipase; the water-insoluble ester-hydrolyzing activity of hepatic triglyceride lipase decreased, whereas the water-soluble ester-hydrolyzing activity did not change. After proteolytic digestion, hepatic triglyceride lipase resembles esterase since it hydrolyzes the water-soluble substrate better than the water-insoluble substrate. Conversely, esterase was converted to lipase by treatment with phospholipid. Cardiolipin in a concentration-dependent fashion enhanced triolein-hydrolysis of human serum carboxylesterase and this effect was associated with a dose-dependent decrease in water-soluble tributyrin hydrolysis. Based on these results, we propose the hypothesis that lipase and esterase have similar catalytic sites and that addition of a hydrophobic recognition site to esterase causes conversion of esterase to lipase (Fig. 9).

Animals↗
PubMed1986

Effect of the combined lipase deficiency mutation (cld/cld) on ultrastructure of tissues in mice. Diaphragm, heart, brown adipose tissue, lung, and liver.

Lipoprotein lipase and hepatic lipase activities are very low in tissues of mice born with genetic combined lipase deficiency (cld/cld). Consequently, if allowed to suckle, the mice develop severe hyperlipemia and die within 3 days. The ultrastructure of capillaries and parenchymal cells in tissues that normally contain lipoprotein lipase and hepatic lipase was studied in tissues from cld/cld and unaffected mice 6 to 24 hours of age. Capillaries in tissues from suckled cld/cld mice were packed with numerous abnormally shaped chylomicrons. There was close contact between surfaces of chylomicrons and the luminal plasma membrane of endothelium. Chylomicrons were sometimes found between endothelial cells and in the subendothelial space in heart, lung, and liver, and in the lumen of lung alveoli. In contrast, capillaries of suckled unaffected mice contained very few chylomicrons, and the subendothelial spaces and lung alveoli were free of chylomicrons. Myocytes of diaphragm and heart from suckled cld/cld mice did not contain lipid droplets, whereas brown adipocytes contained a few small droplets. Parenchymal cells in diaphragm, heart, brown adipose tissue, and lung from suckled unaffected mice contained numerous large lipid droplets. Hepatocytes of suckled cld/cld mice contained small irregularly shaped lipoprotein particles (100 A) in endoplasmic reticulum and Golgi, numerous large lysosomes containing small lipoprotein particles, lipid spheres and lamellar structures, and no intracellular lipid droplets, whereas hepatocytes of suckled unaffected mice contained larger lipoprotein particles (400 A), large lipid droplets, and very few lysosomes. Triacylglycerol of chylomicrons from cld/cld mice was readily hydrolyzed by bovine lipoprotein lipase in vitro, and this effect was not augmented by heat-inactivated serum, indicating that the chylomicrons contained adequate amounts of apoprotein C-II. Thus, the large amount of chylomicrons in capillaries and small amount of lipid droplets in cells of suckled cld/cld mice reflect the very low level of lipoprotein lipase activity in these animals. The findings in hepatocytes indicate that lipoprotein metabolism in liver is markedly disturbed in cld/cld mice.

Adipose Tissue, Brown↗
PubMed1985

Triacylglycerol lipase activities of cultured rat L6 myoblasts.

The utilization of exogenous triacylglycerol by fusing and non-fusing rat L6 myoblasts grown in culture was investigated. Although small quantities of triacylglycerol were accumulated by both cell lines during an incubation of 2 h, no evidence could be found for the presence of lipoprotein lipase, either in the cells or released into the medium. Cell homogenate studies confirmed the absence of lipoprotein lipase but revealed the presence of an acid lipase having a pH optimum at 4.6. Acid lipase activity was mainly associated with a 15 000 g pellet and was capable of hydrolysing triolein at maximum velocity in the millimolar range. Unlike lipoprotein lipase, acid lipase was strongly inhibited by serum and preliminary investigations suggest that the inhibitory component of serum is located amongst the higher density lipoproteins. It is likely that the acid lipase is of lysosomal origin and is responsible for the hydrolysis of internalized triacylglycerol for subsequent utilization by the cell.

Acid Phosphatase↗
PubMed1984

Two methods compared for measuring lipase activity in plasma after heparin administration.

We compared two methods for the direct selective measurement of hepatic lipase and lipoprotein lipase activities in human plasma after intravenous administration of heparin. Except for the emulsifier (gum arabic vs lecithin), the two assay media for hepatic lipase are essentially similar. Results for hepatic lipase by these two assays correlate well (r = 0.99). The assays for lipoprotein lipase in the two procedures differ in the way that hepatic lipase activity is eliminated (immunological inhibition vs a specific substrate emulsion), and also with regard to the emulsifier. The substrate emulsion stabilized by gum arabic (immunological assay) consistently yielded about three times higher enzymic activity than the specific substrate stabilized by lecithin. Experiments in which purified enzymes were used demonstrated that this systematic difference can be accounted for by the different emulsifiers. The satisfactory correlation (r = 0.92) between the two lipoprotein lipase assays, however, demonstrates that they measure the same enzymic activity.

Adult↗
PubMed1984

Properties of acyl-coenzyme A:1-acylglycerophosphate acyltransferase and lipases in porcine erythrocyte membranes.

Acyl-CoA:1-acylglycerophosphate acyltransferase activity was found in porcine erythrocyte membranes. However, the membrane preparations did not catalyze the acylation of either 2-acylglycerophosphate or 2-acylglycerophosphocholine. The 1-acylglycerophosphate acyltransferase and the known acyl-CoA:1-acylglycerophosphocholine acyltransferase systems differ in their specificities for acyl-CoAs and in their stabilities to detergents. Diacylglycerol lipase and monoacylglycerol lipase activities were also detected in porcine erythrocytes. These two activities appear to be catalyzed by different enzymes inasmuch as diacylglycerol lipase but not monoacylglycerol lipase was completely inhibited by divalent cations. The diacylglycerol lipase was relatively specific for the 1-position yielding 2-acylglycerol. The monoacylglycerol lipase hydrolyzed 1-acylglycerol and 2-acylglycerol at comparable rates. Phosphatidic acid was dephosphorylated to form 1,2-diacylglycerol but the acyl groups of phosphatidate were not hydrolyzed significantly by the erythrocyte membranes. Thus, the origin of 1-acylglycerophosphate, a substrate for the newly described enzyme, acyl-CoA:1-acylglycerophosphate acyltransferase, in mature erythrocyte could not be ascribed to action of diacylglycerol lipase, glycerophosphate acyltransferase, or phosphatidate-specific phospholipase A. 1-Acylglycerophosphate may be supplied extracellularly or the 1-acylglycerophosphate acyltransferase activity in erythrocytes may be a remnant of de novo phosphatidate synthesizing system of reticulocytes.

1-Acylglycerol-3-Phosphate O-Acyltransferase↗
PubMed2001

Improved enantioselectivity of a lipase by rational protein engineering.

A model based on two different binding modes for alcohol enantiomers in the active site of a lipase allowed rational redesign of its enantioselectivity. 1-Halo-2-octanols were poorly resolved by Candida antarctica lipase B. Interactions between the substrates and the lipase were investigated with molecular modeling. Unfavorable interactions were found between the halogen moiety of the fast-reacting S enantiomer and a region situated at the bottom of the active site (stereoselectivity pocket). The lipase was virtually mutated in this region and energy contour maps of some variants displayed better interactions for the target substrates. Four selected variants of the lipase were produced and kinetic resolution experiments were undertaken with these mutants. Single point mutations gave rise to one variant with doubled enantioselectivity as well as one variant with annihilated enantioselectivity towards the target halohydrins. An increased volume of the stereoselectivity pocket caused a decrease in enantioselectivity, while changes in electrostatic potential increased enantioselectivity. The enantioselectivity of these new lipase variants towards other types of alcohols was also investigated. The changes in enantioselectivity caused by the mutations were well in agreement with the proposed model concerning the chiral recognition of alcohol enantiomers by this lipase.

Binding Sites↗
PubMed2006

Adipokinetic hormone-induced mobilization of fat body triglyceride stores in Manduca sexta: role of TG-lipase and lipid droplets.

Triglycerides (TG) stores build up in the insect fat body as lipid droplets at times of excess of food. The mobilization of fat body triglyceride (TG) is stimulated by adipokinetic hormones (AKH). The action of AKH involves a rapid activation of cAMP-dependent protein kinase (PKA). Recent in vitro studies have shown that PKA phosphorylates and activates the TG-lipase substrate, the lipid droplets. Conversely, purified TG-lipase from Manduca sexta fat body is phosphorylated by PKA in vitro but is not activated. This study was directed to learn whether or not AKH promotes a change in the state of phosphorylation of the lipase in vivo, and what are the relative contributions of cytosol and lipid droplets to the overall increase of lipolysis triggered by AKH. TG-lipase activity of fat body cytosols isolated from control and AKH-treated insects was determined against the native substrate, in vivo [3H]-TG radiolabeled lipid droplets, obtained from control and AKH-treated insects. The lipase activity of the system composed of AKH-cytosol and AKH-lipid droplets (11.1 +/- 2.1 nmol TG/min-mg) was 3.1-fold higher than that determined with control cytosol and lipid droplets (3.6 +/- 0.5 nmol TG/min-mg). Evaluation of the role of AKH-induced changes in the lipid droplets on lipolysis showed that changes in the lipid droplets are responsible for 70% of the lipolytic response to AKH. The remaining 30% appears to be due to AKH-dependent changes in the cytosol. However, the phosphorylation level of the TG-lipase was unchanged by AKH, indicating that phosphorylation of the TG-lipase plays no role in the activation of lipolysis induced by AKH.

Animals↗
PubMedDate not supplied

Study on immunocapture-chemiluminescence assay of lipase activity in a biological sample.

A new approach for the determination of lipase (triacylglycerol lipase, EC.3.1.1.3) activity in a biological sample was investigated by combining an immunocapture technique with a chemiluminescence (CL) assay method in order to eliminate interference with CL detection. The proposed method consists of an immunocapture step to trap lipase and a subsequent step for CL detection of the activity of the captured lipase. The CL detection is based on the luminol-hydrogen peroxide (H(2)O(2))-horseradish peroxidase (HRP) reaction and utilizes a proenhancer substrate [a lauric acid ester of 2-(4-hydroxyphenyl)-4,5-diphenylimidazole (HDI)] which liberates an active enhancer, HDI, by enzymatic hydrolysis. A polyclonal antibody prepared with porcine pancreas lipase was used for the immunocapture. The proposed immunocapture-CL method effectively eliminated the interference with the CL reaction from biological components and enabled the determination of spiked porcine pancreas lipase activity in serum samples in the range 0.41-1.1 U(HDI) (1 U(HDI) corresponds to the amount which liberates 1 pmol HDI/min at 37 degrees C from the substrate). The method was further applied to the assay of the activity for human pancreas lipase in serum and the results showed good correlation (r = 0.871) with those by the conventional colorimetric method.

Colorimetry↗
PubMed2005

A supported liquid membrane encapsulating a surfactant-lipase complex for the selective separation of organic acids.

We have developed a novel, lipase-facilitated, supported liquid membrane (SLM) for the selective separation of organic acids by encapsulating a surfactant-lipase complex in the liquid membrane phase. This system exhibited a high transport efficiency for 3-phenoxypropionic acid and enabled the selective separation of organic acids due to the different solubilities of the acids in the organic phase and the variable substrate specificity of the surfactant-lipase complex in the liquid membrane phase. We found that various parameters, such as the amount of surfactant-lipase complex in the SLM, the lipase concentration in the receiving phase, and the ethanol concentration in the feed phase, affected the transport behavior of organic acids. The optimum conditions were 5 g L(-1) of the surfactant-CRL complex in the SLM (CRL=lipase from Candida rugosa), 8 g L(-1) of PPL in the receiving phase (PPL=lipase from porcine pancreas), and an ethanol concentration of 50 vol %. Furthermore, we achieved high enantioselective transport of (S)-ibuprofen attributable to the enantioselectivity of the surfactant-CRL complex.

Carboxylic Acids↗
PubMed2006

Increased enantioselectivity and remarkable acceleration of lipase-catalyzed transesterification by using an imidazolium PEG-alkyl sulfate ionic liquid.

Several types of imidazolium salt ionic liquids were prepared derived from poly(oxyethylene)alkyl sulfate and used as an additive or coating material for lipase-catalyzed transesterification in an organic solvent. A remarkably increased enantioselectivity was obtained when the salt was added at 3-10 mol % versus substrate in the Burkholderia cepacia lipase (lipase PS-C)-catalyzed transesterification of 1-phenylethanol by using vinyl acetate in diisopropyl ether or a hexane solvent system. In particular, a remarkable acceleration was accomplished by the ionic liquid coating with lipase PS in an iPr(2)O solvent system while maintaining excellent enantioselectivity; it reached approximately 500- to 1000-fold acceleration for some substrates with excellent enantioselectivity. A similar acceleration was also observed for IL 1-coated Candida rugosa lipase. MALDI-TOF mass spectrometry experiments of the ionic-liquid-coated lipase PS suggest that ionic liquid binds with lipase protein.

Candida↗