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PubMed1983

The relationship between the basal lipolytic and lipoprotein lipase activities in human adipose tissue.

The basal rate of lipolysis and basal lipoprotein lipase activity were determined in vitro in subcutaneous adipose tissue obtained from eight healthy non-obese subjects, ten obese subjects before and during one week's starvation, nine untreated non-insulin dependent diabetics and seven treated non-insulin dependent diabetics whose disease had been under metabolic control for at least three months. There was a negative correlation between the rate of lipolysis and activity of lipoprotein lipase in untreated diabetes mellitus and during starvation (r from -0.87 to -0.81). Under these two conditions the rate of lipolysis is increased and the lipoprotein lipase activity is decreased. There was no correlation between lipolysis and lipoprotein lipase in non-obese subjects, non-starving obese subjects and treated diabetic patients (r from 0.11 to 0.36). Thus, during starvation and in untreated diabetes, there is a strong reciprocal relationship between basal lipolytic activity and basal lipoprotein lipase activity in human adipose tissue which is not found under normal conditions or in obesity and well-controlled diabetes. It is concluded that a negative connection between lipolysis and lipoprotein lipase in human adipose tissue may be of physiological importance for the regulation of the energy balance in conditions such as untreated non-insulin dependent diabetes and starvation where adipose tissue lipids are the major source of energy.

Adipose Tissue↗
PubMed1983

Hepatic lipase stimulates the uptake of high density lipoprotein cholesterol by hepatoma cells.

The objective of this study was to determine whether high density lipoproteins (HDL) that have been treated with hepatic lipase have an enhanced ability to deliver cholesterol to cells. Human HDL was incubated with rat hepatic lipase, reisolated, and subjected to compositional analysis. Approximately 28% of the HDL phosphatidylcholine was hydrolyzed by the hepatic lipase but no change was detected in the cholesterol or apoprotein content of the HDL compared to HDL incubated with heat-inactivated hepatic lipase. Cultured rat hepatoma cells exposed to hepatic lipase-modified HDL showed an increased uptake of HDL free cholesterol relative to cells exposed to control HDL. This increased delivery of HDL free cholesterol was demonstrated by both isotopic and mass determinations and it contributed to a 1.6-fold increase in total cellular cholesterol content relative to cells treated with control HDL. The free cholesterol delivered by the HDL is functionally available to the cell as evidenced by the conversion of radiolabeled free cholesterol to cholesteryl ester. The stimulation of free cholesterol delivery was dose-dependent up to a level of 100 micrograms of HDL free cholesterol/ml of extracellular medium, and was directly related to the extent of phosphatidylcholine hydrolysis. The enhanced cellular accumulation of HDL free cholesterol observed with hepatic lipase appears to be due to the phospholipase activity of this enzyme, since similar results were obtained with HDL that had been modified by snake venom phospholipase A2.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1983

Purification and characterization of rat lingual lipase.

Lingual lipase was highly purified from serous glands of rat tongue. Protein containing lipolytic activity was precipitated with 30-60% saturated ammonium sulfate from the 100,000 X g supernatant of a homogenate of the glands, resuspended in buffered solution, treated and precipitated with acetone at -20 degrees C, and redissolved in buffered solution at pH 5.4. This protein was further purified by hydrophobic chromatography on ethyl agarose; it was eluted with a micellar solution of sodium taurodeoxycholate, oleic acid, and monooleoylglycerol at pH 6.3. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed this fraction consisted of one major protein band, with Mr = 51,000, and several minor bands. A similar value for Mr of protein with lipolytic activity was obtained when acetone-precipitated protein was subjected to gel filtration on Sephadex G-200 indicating that 51,000 is the Mr of an active form of lingual lipase. Lingual lipase purified from rat tongue had a specific activity of 230 units/mg of protein (unit = micromoles of fatty acid formed/min at 37 degrees C). Purified lingual lipase hydrolyzed immediately long chain triacylglycerol to diacylglycerol and fatty acid in medium containing 17 mM sodium taurodeoxycholate and 3.3 mM CaCl2 at pH 5.4. It then hydrolyzed diacylglycerol, and later monoacylglycerol, but at rates 1:6 and 1:20, respectively, of that for triacylglycerol. The activity of lingual lipase in the presence of sodium taurodeoxycholate and CaCl2 was decreased only 33% when pH of the incubation medium was increased to 6.5. This indicates that lingual lipase, which is known to be active in stomach, could act in the small intestines.

Animals↗
PubMed1983

Studies on the detergent inhibition of pancreatic lipase activity.

Pancreatic lipase requires colipase, a protein cofactor, to counteract the in vitro inhibition by bile salt. Lipase activity is inhibited by nonsteroidic detergents regardless of their charge and structure. Detergent-inhibited lipase is reactivated by colipase but in all cases activation is limited to a narrow range of detergent concentration. Complementary studies on the bile salt and detergent effect on lipase activity and on interfacial tension at the substrate-water interface show that inhibition is not related to the interfacial surface tension. It is hypothesized that absorption of amphiphilic compounds to the substrate surface modifies the distribution of the enzyme between the lipid surface and the aqueous phase. The activity of detergent-inhibited lipase is fully restored by adding bile salt to the reaction system. Bile salt might play a critical role during in vivo lipolysis by desorbing surface-active substances from the lipid-water interface thus allowing lipase and colipase to interact with substrate.

Animals↗
PubMed1983

Cytochemical localization of lipases during spore germination from Bryum capillare.

In the oil containing spores of Bryum capillare, lipid breakdown occurs within three days after sowing. The periods of activity of acid, neutral and alkaline lipases are coincident. They start at the first day after sowing the spores. After 3 days of germination, when storage fats forming large globules are mobilised no lipase activity could be detected any longer in the glyoxysomes. Acid lipase is preferentially located in spherosomal membrane but is also present at the glyoxysomal membrane. Alkaline lipase is specifically located in the glyoxysomes and mitochondria. A cooperation presumably exists between acid and alkaline lipases in the hydrolysis of monoglycerides at the glyoxysomal level. Neutral lipase activity is localized at the spherosomal membrane, in the endoplasmic reticulum and in dictyosomes. It is absent from glyoxysomes.

Histocytochemistry↗
PubMed1983

Metabolic abnormalities in multiple symmetric lipomatosis: elevated lipoprotein lipase activity in adipose tissue with hyperalphalipoproteinemia.

Lipoprotein lipase activity in lipomatous tissue, post-heparin lipoprotein lipase activity in plasma, and the composition and concentration of serum lipoproteins were studied in 15 patients with Multiple Symmetric Lipomatosis (MSL). Extremely elevated lipoprotein lipase activity in adipose tissue was found in MSL patients. Total and hepatic post-heparin plasma lipolytic activity was normal, while a moderate but statistically significant increase of extrahepatic lipolytic activity was present. An abnormal composition of serum lipoproteins, characterized by a significant increase in high density lipoproteins, namely HDL2 subfraction, and apoprotein A-I, was demonstrated. A concomitant decrease in and abnormal composition of low density lipoproteins were found. This lipoprotein pattern is consistent with a newly recognized type of hyperalphalipoproteinemia. Significant correlations were found between serum HDL2 cholesterol values and lipoprotein lipase activity in adipose tissue (as well as between serum VLDL-triglyceride and HDL2 cholesterol values). These observations confirm the role of adipose tissue lipoprotein lipase in triglyceride-rich lipoprotein catabolism. The elevated levels of lipoprotein lipase activity in adipose tissue, in addition to a previously demonstrated decrease in adrenergic-stimulated lipid mobilization, could account for both the abnormal fat accumulation in lipomatous fat cell and for hyperalphalipoproteinemia in MSL patients. The occurrence of MSL in two brothers suggests an inherited enzymatic defect, indicating MSL as a "triglyceride storage disease in adipose tissue".

Adipose Tissue↗
PubMedDate not supplied

[Isolation and characterization of intracellular lipase from Serratia marcescens 345].

Lipase was extracted from cells of Serratia marcescens 345 treated with 0.8% Na cholate for 30 min at 37 degrees C. The mixture was then centrifuged and lipase was isolated from the supernatant. The preparation was purified by ammonium sulfate protein precipitation and subsequent dialysis, ultrafiltration of the protein solution through the membrane filter UAM-200 and gel filtration through Sephadex G-200. The effect of metal ions, inhibitors and bile salts as well as temperature and pH on the resultant lipase activity was studied. The substrate specificity of the enzyme was examined. The temperature optimum for the lipase activity was 45 degrees C and pH optimum 6.0--6.3. The enzyme was activated only by Mg2+ at a concentration of 1.10(-4)M in the reaction mixture. Lipase was inhibited by Ni2+, Zn2+, Fe2+ and particularly Cu2+ and Hg2+. Out of the inhibitors tested the strongest were EDTA, o-phenanthrolin and alpha,alpha-dipyridil. Lipolysis was activated by bile salts at a concentration over 0.5%. Intracellular lipase from S. marcescens 345 was able to hydrolyze glycerol esters containing both unsaturated fatty acids (vegetable oils) and saturated fatty acids with a short and a long carbon chain.

Bile Acids and Salts↗
PubMed1982

Effect of apolipoproteins on the hepatic lipase-catalyzed hydrolysis of human plasma high density lipoprotein2-triacylglycerols.

The effect of apolipoproteins on the hepatic lipase-catalyzed hydrolysis of high density lipoprotein (HDL) triacylglycerols was studied in an in vitro system consisting of purified human post-heparin hepatic lipase, HDL2 and albumin. The apparent values of the Michaelis constant (Km) and maximal velocity (Vmax) for the hepatic lipase-catalyzed hydrolysis of HDL2-triacylglycerols were 0.18 mM and 86 nmol free fatty acids released/mg hepatic lipase per min, respectively. The addition of purified human plasma apolipoprotein A-I, A-II, E, C-I or C-III2 (containing 2 mol of sialic acid) to HDL2 caused inhibition of hepatic lipase activity. At a 1:1 weight ratio of added apolipoprotein to HDL2-protein, inhibition was 50% for apolipoprotein E and over 75% for the other apolipoproteins tested. Inhibition of enzyme activity occurred with both the unfractionated HDL2 and the HDL which were reisolated by ultracentrifugation. The major alteration in the composition of the reisolated HDL was an increase in the protein to phospholipid ratio. Based on these results, we speculate on the possible role of the apolipoproteins in the metabolism of HDL2 by hepatic lipase.

Apolipoproteins↗
PubMed1982

Porcine pancreatic lipase. The disulfide bridges and the sulfhydryl groups.

Following complete sequence analysis of the 449 amino acids in porcine pancreatic lipase [J. De Caro et al. (1981) Biochim. Biophys. Acta, 671, 129-138], the position of the six disulfide bridges and of the two free thiols of the protein was investigated using a variety of techniques. Three bridges (Cys-4--Cys-10, Cys-237--Cys-261 and Cys-433--Cys-449) were easily identified in the peptic digest of lipase at pH 2.0. In the latter digest, two other bridges (Cys-285--Cys-296 and Cys-299--Cys-304) were also identified by means of the cystine peptide constituted by two peptide segments: Ala281-Gly-Phe-Pro-Cys-Asp-Ser287 and Thr292-Ala-Asn-Lys-Cys-Phe-Pro-Cys-Pro-Ser-Glu-Gly-Cys-Pro-Gln-Met307. A disulfide bridge, formed by Cys-285 and one of the three half-cystines of the other segment, connected the two peptide moieties. A second disulfide bridge linked the two remaining half-cystines. It was not possible to split any peptide bond between Cys-296 and Cys-304 with proteolytic enzymes. The determination of the pairing of the four half-cystines was resolved as follows. Bond Lys-295--Cys-296 was cleaved with trypsin. A single cycle of Edman degradation was then performed on the peptide compound, thus freeing, in particular, Cys-296 of the peptide bond (296-297). Cys-296 only retained its S-S connection with the half-cystine partner. At the completion of the above operations, the two peptide segments (282-287) and (297-307) could be separated. Consequently it was concluded that Cys-285 is linked to Cys-296. Therefore Cys-299 and Cys-304 are paired. The most reactive SHI group of the enzyme was localized on Cys-181 by condensation of the native protein with radioactive N-ethylmaleimide. The alkylation of the SHII group required previous denaturation of the molecule at alkaline pH. The results obtained for the characterization of the SHII group suggested the existence of two isomeric forms, the SHII being either on Cys-101 or Cys-103 and the bridge alternately between Cys-90--Cys-103 or Cys-90--Cys-101. It is not yet known whether these two forms pre-exist in native lipase or result from an exchange reaction. The bridge Cys-90--Cys-101 was characterized in a thermolytic digest of a cyanogen bromide fragment (CN II) of the protein. However, another bridge involving Cys-181 was also found in the digest. This bridge is considered as being an artefact. It is possible that considering the treatments undergone by the large peptide (CN II), the SH groups of lipase were oxidized and transformed in an S-S bridge. The disulfide bridges of lipase form relatively small loops along the main chain. This arrangement is consistent with a high flexibility of the molecule. As reported earlier [R. Verger et. al. (1971) Biochim. Biophys. Acta. 242, 580-592], the SHI group is not essential for lipase activity. The role of the SHII group should be more precisely investigated.

Amino Acid Sequence↗
PubMed1982

Lipoprotein lipase activity in turkey aorta.

Lipoprotein lipase activity was measured in heparin extracts of aortic intima and adventitia from normal and cholesterol-fed turkeys. This lipolytic activity showed typical characteristics of lipoprotein lipase i.e., requirement of serum for activity and a 92% inhibition by protamine sulfate. The highest lipoprotein lipase activity was found in the adventitia of the abdominal aorta. Lipoprotein lipase activity was greater in the intima of the thoracic aorta than in the intima of the abdominal aorta. This higher activity of thoracic intima was not correlated with development of fibrous plaques which were found only in abdominal aorta. Cholesterol-feeding resulted in plasma very low density lipoproteins enriched in cholesterol-ester but had no effect on the level of lipoprotein lipase activity of aortic intima. Cholesterol-feeding, although altering lipoprotein composition, did not increase aortic intima lipoprotein lipase activity.

Animals↗
PubMed1981

Preparation of thioester substrates and development of continuous spectrophotometric assays for phospholipase A1 and monoacylglycerol lipase.

Current assays of phospholipase A1 (EC 3.1.1.32) and monoacylglycerol lipase (EC 3.1.1.23) activities in tissues are discontinuous, laborious, and expensive. Some spectrophotometric substrates were synthesized to alleviate this problem. Thioester analogs of phosphatidylcholine and phosphatidylethanolamine. rac-1,2-S,O-didecanoyl-3-phosphocholine-1-mercapto-2,3-propanediol and rac-1,2-S,O-didecanoyl-3-phosphoethanolamine-1-mercapto-2,3-propanediol, were synthesized from the diacylglycerol analog, rac-1,2-S,O--didecanoyl-1-mercapto-2,3-propanediol. The latter was prepared from triacylmercaptoglycerol by lipolysis and separation by chromatography on silica gel. Monoacylglycerol thioester analogs, 1-S-hexadecanoyl-1-mercapto-2,3-propanediol and 1-S-decanoyl-1-mercapto-2,3-propanediol, were synthesized by selective acylation of mercaptoglycerol. All of the substrates were hydrolyzed by Rhizopus delemar lipase to release sulfhydryl groups reactive towards 4,4'-dithiobispyridine. The hydrolysis could be followed continuously in a spectrophotomer with 0.1 absorbance unit corresponding to 5 nmol product. The structure and isomeric purity of the phospholipid analogs were verified by their behavior on thin-layer chromatography, elemental analyses, infrared spectra, and by the specificity of the colorimetric reaction with lipolytic enzymes. Whereas phospholipase A1 activity hydrolyzed both phospholipid analogs to release the theoretical amount of free thiol, neither phospolipases C nor A2 promoted thio release. The pH optimum, heat stability, and Ca2+ ion dependency were determined for the hydrolysis of each substrate by R. delemar lipase. The results indicate that the phospholipase A1 and monoacylglycerol lipase activities in R. delemar lipase are due to separate enzymes, and that these enzyme specific assays will be of general utility for enzyme characterization and purification studies. These substrates are useful for sensitive, convenient, and specific spectrophotometric assays for phospholipase A1 and monoacylglycerol lipase over the pH range 3 to 8.

Calcium↗
PubMed1980

[New results about the role of lipase, colipase and bile acids in the fat digestion (author's transl)].

Pancreatic lipase B and a minor specific lipase A are involved in the digestion of fats. The lipolysis is a heterogeneous catalysis. Lipases, colipase(s), bile acids, bile lipids and calcium ions play a role in the lipolysis. Colipase(s) makes it possible for lipase to adsorb to the substrate in presence of bile acids activating the adsorption of lipase and protecting the lipase at the interfaces.

Bile Acids and Salts↗
PubMed1981

Binding of lipoprotein lipase to endothelial cells in culture.

Equilibrium-binding data of highly purified avian lipoprotein lipase to cultured bovine endothelial cells demonstrate the presence of a class of high affinity sites. Analysis of the binding function by weighted least squares technique yielded an association constant of K = 0.7 X 10(7) M-1 and a maximum binding capacity of 1.6 micrograms/1.9 X 10(6) cells. Lipoprotein lipase was monitored both by its catalytic activity and a sensitive radioimmunoassay which permitted the accurate measurement of nanogram quantities of enzyme protein. Specific activity of the bound enzyme was similar to that of the initial purified enzyme. Lipoprotein lipase binding to endothelial cells was inhibited 80% by preincubating cells in 0.1% trypsin for 3 min at 37 degrees C, 92% by 0.01% pronase, and 91% by 0.008% proteinase K. Heparin was most efficient in releasing lipoprotein lipase from endothelial cells. Fifty per cent of the enzyme appeared in the medium at a concentration of 3 micrograms/ml of heparin. At the same concentration of heparan sulfate, 20% of the enzyme was released. Hyaluronic acid and chondroitin sulfate were not effective in stimulating enzyme release. Preincubating endothelial cells with purified human platelet endoglucuronidase for 1 h at 37 degrees C led to a 90% reduction in lipoprotein lipase binding. Endoglucuronidase was purified 20,000-fold as compared to the initial platelet lysate by a 5-step purification method. The extent of inhibition of binding was shown to be dependent on concentration of endoglucuronidase in the preincubation medium. The specificity of platelet endoglucuronidase and the demonstration that the preparation utilized contained no detectable protease activity is further evidence that lipoprotein lipase is bound to endothelial cell heparan sulfate or heparan sulfate-like molecules.

Animals↗
PubMed1981

Measurement of serum lipase activity with the oxygen electrode.

We describe the measurement of lipase (triacylglycerol lipase; EC 3.1.1.3) in serum by continuous monitoring of relative rates of oxygen consumption with a polarographic oxygen electrode. The reactions described by Proelss and Wright (Clin. Chem. 23: 522-531, 1977) are used: trilinolein, with lipase catalysis, yields linoleic acid, which reacts with oxygen in the presence of lipoxygenase. Lipase activity is measured by comparing the zero order reaction rate of the specimen with that obtained with linoleic acid standards. Results for lipase (y) correlated well with those by the copper-soap method of Myrtle and Zell (x) (Clin. Chem. 21: 1469-1473, 1975); y = 0.33x - 11; r = 0.98; n = 34. Results are unaffected by specimen dilution, and the standard curve is linear to 520 U/L. Day-to-day precision (CV) is 10.4% for normal activities, 6.1% for above-normal activities. We believe the method offers a precise, practical approach to lipase analysis.

Blood Chemical Analysis↗
PubMed1995

The lipase to amylase ratio in acute pancreatitis.

OBJECTIVES: The ratio of serum lipase to serum amylase has been proposed to distinguish acute episodes of alcoholic from nonalcoholic pancreatitis. We evaluated the efficacy of this test in a community hospital setting. METHODS: Charts of all patients discharged with a diagnosis of acute pancreatitis over 19 months were retrospectively reviewed. Patients were excluded if their creatinine was greater than 3.0 mg/dl, if the amylase and lipase were not measured within 72 h of the onset of symptoms, or if the cause of pancreatitis was not known by the time of discharge. RESULTS: Of the 56 patients, 31 had alcoholic pancreatitis. The lipase to amylase ratio did not differ significantly between patients with alcoholic and nonalcoholic pancreatitis. Median amylase and lipase were significantly higher in nonalcoholic pancreatitis; however, the wide ranges of both meant that neither amylase nor lipase accurately determined the cause of pancreatitis. CONCLUSION: The lipase to amylase ratio does not appear to be sufficiently sensitive or specific to distinguish alcoholic from nonalcoholic acute pancreatitis.

Acute Disease↗
PubMed1994

Role of hepatic lipase in the uptake and processing of chylomicron remnants in rat liver.

The participation of hepatic lipase in the initial uptake and processing of chylomicron remnants was studied in the isolated, perfused rat liver. Hepatic lipase activity was either reduced by preperfusion of livers with heparin or inhibited with specific rat hepatic lipase antibodies. [3H]palmitate-labeled chylomicron remnants were recirculated through control and treated livers for 15 min; the livers were then flushed, homogenized, and endosome-rich fractions were isolated. Depletion of hepatic lipase activity by both methods reduced the uptake of chylomicron remnants and hydrolysis of their component triglycerides by perfused rat livers, but at the same time significantly increased the rate of endocytosis of those chylomicron remnants taken up. We conclude that hepatic lipase facilitates, but is not essential for, the initial uptake of chylomicron remnants by rat liver. Furthermore, endocytosis of chylomicron remnants does not require binding to hepatic lipase or the associated hydrolysis of remnant lipids.

Animals↗
PubMed1975

[Lipase activity in the calf serum under different types of feeding].

The development of lipase activity in serum (S-lipase activity) was studied in two groups of the calves of the Bohemian Red-Pied breed in the post-natal period up to the age of nine weeks from birth. From the eighth day of age, the two groups differed from each other in their lactic nutrition. Group A calves were given whole milk (obtained at primary production) and group B calves were fed the Laktosan mixture instead of milk. The different type of nutrition did not influence the character of the development of S-lipase activity with increasing age. A difference was found between the two groups as to the level of the activity of the enzyme under study. In the whole-milk group the average S-lipase activity values were higher than in the group fed Laktosan in a larger part of the test period. Some differences were statistically significant. It is assumed that lipase activity in blood is a reflection of the external secretion of pancreas changing according to the structure of food taken in. The activity of S-lipase was determined by the method according to Cherry and Crandall (Seligson, 1964); the average minimum value was 0.025 +/- 0.0017 u. in group A and 0.017 +/- 0.0081 u. in group B, and the average maximum value was 0.370 +/- 0.100 u. and 0.286 +/- 0.0766 u., respectively.

Animal Feed↗
PubMed1996

Studies on the inhibition of pancreatic and carboxylester lipases by protamine.

The basic protein protamine strongly inhibited hydrolysis of triolein emulsified with soybean phosphatidylcholine (PC) by pancreatic and carboxylester lipases; 10 micrograms/ml protamine, about 1000 times lower than the concentration of bovine serum albumin for the same effect, inhibited triolein hydrolysis completely. This inhibition was not affected by the incubation pH or bile salt concentration. Two other basic proteins, histone and purothionin, also inhibited hydrolysis of triolein emulsified with soybean PC, but they did not inhibit triolein hydrolysis by gastric lipase. When gum arabic was used as an emulsifier instead of soybean PC, these basic proteins did not affect triolein hydrolysis by pancreatic or carboxylester lipases. The effects of protamine on triolein hydrolysis by pancreatic and carboxylester lipases was studied using various phospholipids as emulsifiers. Protamine (10 micrograms/ml) did not inhibit hydrolysis of triolein emulsified with dicaproyl PC (DCPC), phosphatidic acid (PA), or phosphatidylserine (PS) by pancreatic and carboxylester lipases. Conversely, protamine at high concentrations slightly stimulated hydrolysis of triolein emulsified with DCPC or PA. Hydrolysis of triolein-phosphatidylethanolamine (PE) emulsion was inhibited slightly by protamine. The profiles of protamine inhibition of triolein-phosphatidyl-N,N-dimethyl ethanolamine (PDME) and triolein-phosphatidyl-N-monomethyl ethanolamine (PMME) emulsions were intermediate between those of PC and PE emulsions. These results suggest that the phospholipid species, especially choline moieties and fatty acid chain length, affect the lipase inhibitory activity of protamine profoundly. In vivo, oral administration of protamine to rats reduced and delayed the peak plasma triacylglycerol concentration, but neither bovine serum albumin nor an amino acid mixture with an amino acid composition identical to protamine affected plasma triacylglycerol levels.

Animals↗