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At least 163 records · Page 9Linked to original sources
PubMed1981

High density lipoprotein subfractions in relation to lipoprotein lipase activity of tissues in man--evidence for reciprocal regulation of HDL2 and HDL3 levels by lipoprotein lipase.

High density lipoprotein subfractions HDL2 and HDL3 were separated from plasma of 22 normolipidemic healthy human subjects and analyzed for cholesterol, triglyceride, phospholipid and protein. In the same subjects the heparin-releasable lipoprotein lipase activity was assayed from biopsies of adipose tissue and skeletal muscle. A significant inverse correlation was found between the plasma concentrations of HDL2 and HDL3 (4= -0.55, p less than 0.01). The HDL2 cholesterol and HDL2 phospholipid levels were negatively correlated with HDL3 protein levels. The total HDL2 and HDL2 cholesterol, phospholipid and protein concentrations were all positively correlated with lipoprotein lipase activity of both adipose tissue and skeletal muscle. In contrast, the corresponding HDL3 values did not show any correlation with adipose tissue lipoprotein lipase but the HDL3 cholesterol, triglyceride and protein levels were inversely correlated with skeletal muscle lipoprotein lipase activity. The results suggest that plasma HDL2 and HDL3 concentrations are reciprocally regulated by the activity of lipoprotein lipase. THe data are compatible with a concept proposing conversion of HDL3 to HDL2 through assimilation of cholesterol, phospholipids and apoproteins from triglyceride-rich lipoproteins during their degradation by lipoprotein lipase. Particularly the concentration of the HDL2 is closely related to the rat of intravascular lipolysis.

Adipose Tissue↗
PubMed1985

Role of acid lipase in cholesteryl ester accumulation during atherogenesis. Correlation of enzyme activity with acid lipase-containing macrophages in rabbit and human lesions.

Purified acid lipase was previously shown to hydrolyze the artificial substrate, alpha-naphthyl palmitate, as well as triglycerides and cholesteryl esters and to form cholesteryl esters. To determine to what extent these activities are associated with acid lipase-containing cells in atherosclerotic plaques, we examined rabbit aortas at different stages of experimental lesion induction and human atherosclerotic arteries. Assays of cholesteryl ester formation, and alpha-naphthyl palmitate and cholesteryl ester hydrolysis were performed on homogenates of lesions and the hydrolysis of the artificial fatty acid ester was used as a histochemical marker to identify acid lipase positive foam cells in sections of the same lesions. The volume of lesions occupied by cells stained for acid lipase correlated strongly with the enzyme activities of the arterial homogenates. These results suggest that acid lipase-containing cells may mediate the accumulation of cholesteryl ester during atherogenesis. Since acid lipase activity marks macrophages, these methods may be useful for relating macrophage distribution and function to lesion progression, regression, and complication.

Animals↗
PubMed1984

Regulation of steroidogenesis in rat adrenal gland: identification of the bifunctional, hormone-sensitive cholesterol esterase--triacylglycerol lipase enzyme protein and its discrimination from hormone-insensitive lipases.

The activities of hormone-sensitive cholesterol esterase and hormone-sensitive triacylglycerol lipase from rat adrenal glands were enhanced about 2-fold by means of ether stress and showed parallel elution profiles on a Sepharose CL-6B column. Both enzymatic activities were inhibited to a similar extent by DFP after separation from hormone-insensitive lipase on heparin-Sepharose. Fractions from the gel filtration column containing the two hormone-sensitive enzymes showed incorporation of tritium-labelled DFP into only one polypeptide of Mr 84 000. From these results we conclude that both hormone-sensitive activities reside on one polypeptide of Mr 84 000, thus providing further support to the concept that the different hormone-sensitive acylester hydrolase activities in steroid-secreting tissues as well as in adipose tissue are performed by the same bifunctional enzyme. In addition to the hormone-sensitive enzyme, rat adrenals contained high amounts of neutral triacylglycerol lipase activity which was not affected by stress. The latter enzyme was resistant to high salt concentrations, was less susceptible to inhibition by DFP, but could be inhibited completely by the addition of antibodies raised against rat liver lipase, thus most probably representing the adrenal liver lipase-like triacylglycerol lipase.

Adrenal Glands↗
PubMed2006

Scorpion digestive lipase: a member of a new invertebrate's lipase group presenting novel characteristics.

Unlike classical digestive lipases, the scorpion digestive lipase (SDL) has a strong basic character. The SDL activity's optimal pH, when using tributyrin or olive oil as substrate, was 9.0. Added to that, the estimated isoelectric point of the native SDL using the electrofocusing technique, was found to be higher than 9.6. To our knowledge, this is the first report of an animal digestive lipase having such a basic character. When olive oil was used as substrate, SDL was shown to be insensitive to the presence of amphiphilic proteins such as bovine serum albumin (BSA). Furthermore, the hydrolysis was found to be specifically dependent on the presence of Ca(2+) ions, since no significant SDL activity was detected in the presence of ions chelator such as EDTA. Nevertheless, the SDL does not require Ca(2+) to trigger the hydrolysis of tributyrin emulsion. Interestingly Zn(2+) and Cu(2+) ions act as strong inhibitors of SDL activity when using tributyrin as substrate. An internal chymotryptic cleavage of SDL generated two fragments of 28 and 25 kDa having the same N-terminal sequence. This sequence of 19 residues does not share any homology with known animal and microbial lipases. Polyclonal antibodies directed against SDL (pAbs anti-SDL) failed to recognise ostrich pancreatic and dog gastric lipases (OPL and rDGL). Moreover, both pAbs anti-OPL and anti-rDGL failed to immunoreact with SDL. These immunological as well as distinct biochemical properties strengthen the idea that SDL appears to belong to a new invertebrate's lipase group.

Animals↗
PubMed2002

Degradation of aliphatic polyester films by commercially available lipases with special reference to rapid and complete degradation of poly(L-lactide) film by lipase PL derived from Alcaligenes sp.

Commercial lipases were examined for their degradation efficiency of aliphatic polyester films. In 100 days immersion of polyester films in lipase solutions at 37 degrees C at pH 7.0, Lipase Asahi derived from Chromobacterium viscosum degraded polybutylene succinate-co-adipate (PBSA), poly (e-caprolactone) (PCL) and polybutylene succinate (PBS), and Lipase F derived from Rhizopus niveus degraded PBSA and PCL during 4-17 days. Lipase F-AP15 derived from Rhizopus orizae could degrade PBSA in 22 days. In these cases, PBS and PBSA were mainly degraded to dimers, whereas PCL was mainly degraded to monomers. Only poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHB/V) and poly (L-lactide) (PLA) were not degraded in the experiments. However, PLA degraded completely at 55 degrees C, pH 8.5 with Lipase PL during 20 days. This result could be explained with the sequential reactions of the chemical hydrolysis of the polymer to oligomers at higher pH and temperature, and the succeeding enzymatic hydrolysis of oligomers to the monomers.

Adipates↗
PubMed2004

Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization.

A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

Cellulase↗
PubMed1976

The inhibition in vivo of lipoprotein lipase (clearing-factor lipase) activity by triton WR-1339.

1. Lipoprotein lipase activity was measured in heart homogenates and in heparin-releasable and non-releasable fractions of isolated perfused rat hearts, after the intravenous injection of Triton WR-1339. 2. In homogenates of hearts from starved, rats, lipoprotein lipase activity was significantly inhibited (P less than 0.001) 2h after the injection of Triton. This inhibition was restricted exclusively to the heparin-releasable fraction. Maximum inhibition occurred 30 min after the injection and corresponded to about 60% of the lipoprotein lipase activity that could be released from the heart during 30 s perfusion with heparin. 3. Hearts of Triton-treated starved rats were unable to take up and utilize 14C-labelled chylomicron triacylglycerol fatty acids, even though about 40% of heparin-releasable activity remained in the hearts. 4. It is concluded that Triton selectively inhibits the functional lipoprotein lipase, i.e. the enzyme directly involved in the hydrolysis of circulating plasma triacylglycerols. 5. Lipoprotein lipase activities measured in homogenates of soleus muscle of starved rats and adipose tissue of fed rats were decreased by 25 and 39% respectively after Triton injection. It is concluded that, by analogy with the heart, these Triton-inhibitable activities correspond to the functional lipoprotein lipase.

Adipose Tissue↗
PubMed1995

Stereoselectivity of microbial lipases. The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases.

In the present study, the stereoselectivity of purified lipases from Candida rugosa, Chromobacterium viscosum, Pseudomonas species and Rhizopus arrhizus towards triacylglycerols in comparison to various structural analogs were investigated. Different triacylglycerol analogs with distinct polarities at position sn-2 of the glycerol backbone (1,3-diacyl-2-X-glycerol, where 2-X = 2-acyloxy, 2-alkyloxy, 2-deoxy-2-alkyl, or 2-deoxy-2-phenyl) were synthesized. Substrate hydrophobicity and steric requirement was modified by variation of the alkyl and acyl chain length. Hydrolysis of these substrates demonstrated that minor structural variations at C2 of triacylglycerol strongly affect the stereoselectivity of the lipases tested. It was noteworthy that the variation of substrate structure did not only affect the quantity of stereoselectivity expressed as percentage enantiomeric excess, but also resulted in a reversal of stereopreference in some cases. Replacement of the acylester in position 2 of glycerol by a non-ester-linked aliphatic moiety shifted the preference of Chromobacterium viscosum lipase from sn-3 to sn-1. Lipases from Chromobacterium viscosum. Pseudomonas species and Rhizopus arrhizus exhibited sn-3 preference with 2-deoxy-2-phenyl analogs, while towards substrates with a 2-deoxy-2-alkyl moiety sn-1 stereobias was recorded. Candida rugosa lipase was rather insensitive to substrate variations concerning the polarity at position 2 of the glycerol backbone. However, variation of the acyl chain length significantly influenced stereoselectivity of this lipase.

Candida↗
PubMed2002

Lipolysis in the absence of hormone-sensitive lipase: evidence for a common mechanism regulating distinct lipases.

Hormone-sensitive lipase (HSL) is presumed to be essential for lipolysis, which is defined as the mobilization of free fatty acids from adipocytes. In the present study, we investigated the effects of various lipolytic hormones on the lipolysis in adipocytes derived from mouse embryonic fibroblasts (MEF adipocytes) prepared from HSL-deficient mice (HSL-/-). HSL-/- MEF differentiated into mature adipocytes in a manner indistinguishable from that of wild-type mice. Both isoproterenol (ISO) and tumor necrosis factor (TNF)-alpha stimulated the rate of lipolysis in HSL-/- MEF adipocytes, although to a lesser extent than in wild-type cells, and these lipolytic activities were inhibited by H-89, a cAMP-dependent protein kinase inhibitor, and troglitazone, respectively. Thus, the responses of the residual lipolytic activity to lipolytic hormones and TNF-alpha were well conserved in the absence of HSL. Extracts from HSL-/- MEF adipocytes hydrolyzed triacylglycerol (TG) but not cholesterol ester, indicating that the residual lipolytic activity was mediated by another TG-specific lipase. The TG lipase activity, which was decreased in cytosolic fraction in response to ISO, was increased in fat cake fraction. Therefore, translocation of the TG lipase may explain, at least partially, the ISO-stimulated lipolysis in HSL-/- adipocytes. In conclusion, lipolysis is mediated not only by HSL but also by the non-HSL TG lipase, whose responses to lipolytic hormones are similar to those of HSL. We propose that both lipases are regulated by common mechanism of lipolysis.

Adipocytes↗
PubMed2006

Serum lipase activities and pancreatic lipase immunoreactivity concentrations in dogs with exocrine pancreatic insufficiency.

OBJECTIVE: To determine serum lipase activities and pancreatic lipase immunoreactivity (PLI) concentrations in dogs with exocrine pancreatic insufficiency (EPI). ANIMALS: 74 healthy dogs and 25 dogs with EPI. PROCEDURES: A diagnosis of EPI was made on the basis of clinical signs, low serum trypsin like immunoreactivity (TLI) concentration, and response to treatment with enzyme replacement. Median values for fasting serum lipase activity and serum PLI concentrations were compared between the 2 groups with a Mann-Whitney U test. RESULTS: Median fasting serum lipase activity was not significantly different between dogs with EPI (366.0 U/L) and healthy dogs (294.5 U/L), and only 1 dog with EPI had a serum lipase activity less than the lower limit of the reference range. Median serum PLI concentration was significantly lower in dogs with EPI (0.1 microg/L) than in healthy dogs (16.3 microg/L). All dogs with EPI had serum PLI concentrations less than the lower limit of the reference range. CONCLUSION AND CLINICAL RELEVANCE: Serum lipase activity is not limited to the exocrine pancreas in origin, whereas serum PLI is derived only from the exocrine pancreas. Unlike in serum TLI concentrations, there was a small degree of overlap in serum PLI concentrations between healthy dogs and dogs with EPI. Serum TLI concentration remains the test of choice for diagnosis of EPI.

Animals↗
PubMed1989

Assessment of lipoprotein activators of skim milk lipoprotein lipase and the relationship between lipoprotein lipase activity and milk fat synthesis.

Bovine plasma and lipoproteins isolated by gel filtration chromatography were examined for their ability to activate skim milk lipoprotein lipase. Addition of equal amounts of protein from either triglyceride-rich lipoprotein, low density lipoprotein, high density lipoprotein or plasma to a lipoprotein lipase assay resulted in 6.0, 2.2, 2.5, or 1.1% hydrolysis of radiolabelled triglyceride emulsion. Lipoprotein lipase activity in skim milk was evaluated as an indicator of mammary lipid secretory capacity. Skim milk lipoprotein lipase activity was significantly lower immediately prepartum as compared with activity immediately postpartum (.2 vs. 5.4% of substrate hydrolyzed). Skim milk lipoprotein lipase was significantly higher during the final 12 d of lactation than in samples obtained 12 d after machine milking was terminated (5.6 vs. less than 1% of substrate hydrolyzed). Although skim milk lipoprotein lipase activity appeared positively related to mammary lipid secretory capacity during the time immediately surrounding initiation and cessation of copious milk production, activity between those periods was not correlated to milk fat percentage, milk fat yield, or stage of lactation.

Animals↗
PubMed1989

Genetic and developmental regulation of the lipoprotein lipase gene: loci both distal and proximal to the lipoprotein lipase structural gene control enzyme expression.

We report here a study of the developmental and genetic control of tissue-specific expression of lipoprotein lipase, the enzyme responsible for hydrolysis of triglycerides in chylomicrons and very low density lipoproteins. Lipoprotein lipase (LPL) mRNA is present in a wide variety of adult rat and mouse tissues examined, albeit at very different levels. A remarkable increase in the levels of LPL mRNA occurs in heart over a period of several weeks following birth, closely paralleling developmental changes in lipase activity and myocardial beta-oxidation capacity. Large increases in LPL mRNA also occur during differentiation of 3T3L1 cells to adipocytes. As previously reported, at least two separate genetic loci control the tissue-specific expression of LPL activity in mice. One of the loci, controlling LPL activity in heart, is associated with an alteration in LPL mRNA size, while the other, controlling LPL activity in adipose tissue, appears to affect the translation or post-translational expression of LPL. To examine whether these genetic variations are due to mutations of the LPL structural locus, we mapped the LPL gene to a region of mouse chromosome 8 using restriction fragment-length polymorphisms and analysis of hamster-mouse somatic cell hybrids. This region is homologous to the region of human chromosome 8 which contains the human LPL gene as judged by the conservation of linked genetic markers. Genetic variations affecting LPL expression in heart cosegregated with the LPL gene, while variations affecting LPL expression in adipose tissue did not. Furthermore, Southern blotting analysis indicates that LPL is encoded by a single gene and, thus, the genetic differences are not a consequence of independent regulation of two separate genes in the two tissues. These results suggest the existence of cis-acting elements for LPL gene expression that operate in heart but not adipose tissue. Our results also indicate that two genetic mutations resulting in deficiencies of LPL in mice, the W mutation on chromosome 5 and the cld mutation on mouse chromosome 17, do not involve the LPL structural gene locus. Finally, we show that the gene for hepatic lipase, a member of a gene family with LPL, is unlinked to the gene for LPL. This indicates that combined deficiencies of LPL and hepatic lipase, observed in humans as well as in certain mutant strains of mice, do not result from focal disruptions of a cluster of lipase genes.

Adipose Tissue↗
PubMed1988

[Comparison of fungal lipase and pancreatic lipase in exocrine pancreatic insufficiency in man. Study of their in vitro properties and intraduodenal bioavailability].

Assuming that acidic degradation of lipase was the major cause of failure for the correction of steatorrhea by pancreatic extracts, we compared the in vitro and in vivo activities of a fungal lipase (FL) (Rhizopus arrhizus) with classical porcine pancreatic extract (Eurobiol). The choice of FL was determined by its two optimum pH (3.5 and 7.4). Five factors known to modify lipase activity were tested: pH, biliary acids colipase, trypsin and albumin. Bioavailability was measured by using a double intubation method in 13 patients with severe pancreatic insufficiency. Each enzymatic preparation was given during a test meal in a randomized and cross-over fashion. Results of the in vitro study showed that FL differed from pancreatic lipase by the following properties: better resistance in acidic solution, inhibition by biliary salts, absence of effect of colipase and rapid degradation by trypsin. In vivo the percentage of lipase activity recovered was 14.2 +/- 10.6 p. 100 for FL and 56 +/- 50 p. 100 for the classical pancreatic preparation. Compared with placebo significant differences in the recovery rate of lipolytic activity were observed with the pancreatic preparation only and started at the 40th min after the end of the test meal. These results showed that lack of degradation in acidic milieu is not the only valuable criterion for the choice of an efficient lipase preparation. The role of other potential factors such as gastric emptying as well as proteolytic degradation of the enzyme should be considered as well.

Bile Acids and Salts↗
PubMed1974

Human milk lipases. I. Serum-stimulated lipase.

Lipase activity has previously been demonstrated in human milk. This study shows that there are two separate triglyceride lipases in human milk. One is mainly in the skim milk and is stimulated by bile salts; the other is mainly in the cream and is inhibited by bile salts but stimulated by serum. The serum-stimulated lipase was purified by affinity chromatography on heparin-substituted Sepharose 4B. This gave a 9500-fold purification over whole milk. Although polyacrylamide gel electrophoresis showed that the enzyme was not purified to homogeneity, it had the highest specific activity so far reported for a human serum-stimulated lipase. The purified enzyme was free from bile salt-stimulated lipase activity and had the characteristics of other serum-stimulated or so-called lipoprotein lipases. Thus, it was almost completely inhibited by 1 M NaCl. The purified enzyme was active against tributyrylglycerol also in the absence of exogenous serum factors.

Bile Acids and Salts↗
PubMedDate not supplied

Lipases production by Bacillus circulans under mesophilic and osmophilic conditions. Factors affecting lipases production.

A facultative osmophilic bacterium able to produce lipases (isolated from bee honey) was identified as Bacillus circulans. Factors affecting lipases production by such isolate were studied. Dox's liquid medium supplied with 2 and/or 30% sucrose was used as a basal medium, under static culture condition, for such a purpose. Results have showed that the optimal sucrose concentration at which the isolate produced its maximal yield of lipases was 30% after an incubation period of 24 hours at 40 degrees C, and this was corresponding to an incubation period of 48 hours at 40 degrees C in presence of 2% sucrose. The optimal pH value was 7 in the first case while, 6.5 in the second. Furthermore production of extracellular lipases by such isolate was achieved in presence and absence of tributyrin as a carbon source instead of sucrose when supplied to Dox's liquid medium. Also the production of extracellular lipases by such isolate was not enhanced in presence of tributyrin as a supplement to Dox's liquid medium when supplied with 2 and/or 30% sucrose as carbon sources. This might suggest that the extracellular lipases of such isolate is constitutive in nature.

Bacillus↗
PubMed1983

Simple, reproducible procedure for selective measurement of lipoprotein lipase and hepatic lipase.

Existing methods for determining the release of lipoprotein lipase (EC 3.1.1.34) and hepatic lipase (EC 3.1.1.3) into plasma after heparin injection give highly variable results, primarily traceable to errors in the isolation of labeled oleate from the substrate, triolein. Methods involving anion-exchange resin to bind oleate show high variability and have a low yield. Introducing a strong base in the last step of the assay may spuriously increase the counts from oleate, whereas a detergent such as Triton X-100, used to minimize this problem, has a strong quenching effect. We report a simple and rapid method in which we eliminate rather than correct for the sources of variation. The substrate, tri[1-14C]oleoyl-glycerol, is sonicated under strictly standardized conditions with gum arabic, 50 g/L. Incubation is stopped by addition of a benzene/chloroform/methanol mixture and NaOH, 0.2 mol/L. Labeled oleic acid is extracted with hexane after acidification of the alkaline aqueous (upper) phase, so that no alkali is introduced into the scintillation liquid. For lipoprotein lipase measurement, hepatic lipase is inactivated by a specific antiserum, whereas hepatic lipase is measured after lipoprotein lipase is inactivated by NaCl, 1.0 mol/L. The method is efficient and specific, and quenching and chemiluminescence artifacts are avoided.

Animals↗
PubMed1995

Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II.

Despite tremendous progress in the elucidation of three-dimensional structures of lipases, the molecular basis for their observed substrate preference is not well understood. In an effort to correlate the lipase structure with its substrate preference and to clarify the contradicting reports in the literature, we have compared the enzymic characteristics of two closely related recombinant lipases from the fungus Geotrichum candidum. These enzymes were expressed in the yeast Saccharomyces cerevisiae as fusions with an N-terminal poly(His) tag and were purified in a single step by metal-affinity chromatography. Their specific activities against a series of triacylglycerol substrates were compared using a titrimetric assay. The substrates varied in fatty acyl chain length, number of double bonds and their position along the chain. G. candidum lipases I and II (GCL I and GLC II) are markedly different with respect to their substrate preferences. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15), GCL I showed higher specific activity than GCL II, whereas GCL II showed higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14). We have constructed a hybrid molecule containing the N-terminal portion of GCL I (including the flap covering the active site) linked to the C-terminal portion of GCL II. The hybrid molecule showed a substrate preference pattern identical to that of GCL II. These results indicate that sequence variation within the N-terminal 194 amino acids of G. candidum lipases do not contribute to the observed variation in efficiency by which the lipases hydrolyze their substrates. Moreover, it also shows that the flap region in GCL is not directly involved in substrate differentiation, even though this region is thought to be involved in recognition of the interface and in the activation of the enzyme.

Base Sequence↗
PubMed1996

Chronic increased serum lipase without evidence of pancreatitis: tumor-derived lipase?

A 51-year-old man developed a large retroperitoneal tumor with liver and lymph node metastases; there was no radiological evidence of pancreatic involvement. Despite the progression of disease, results of laboratory tests, notably serum amylase, were normal except for minor increases in aspartate aminotransferase and gamma-glutamyltransferase and a marked increase in lipase. The increased lipase was not attributable to formation of macroenzyme. To determine the source of the lipase, we fractionated serum and a tumor biopsy homogenate, using electrophoresis. The lipase pattern obtained from the patient's serum differed from that seen in serum from a patient with acute pancreatitis. Additionally, the lipase pattern obtained from a homogenate of biopsy sample from the retroperitoneal tumor did not match the pattern observed for normal pancreas. Apparently, the source of this increased serum lipase activity was the nonpancreatic tumor.

Alanine Transaminase↗