Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.34 (lipoprotein lipase)
7,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Accelerated clearance of circulating triglycerides has been observed in thermally injured patients, which suggests that lipoprotein lipase (LPL) activity may be increased. The present study was initiated to ascertain if heart, skeletal muscle, or adipose tissue LPL activities are affected by burn trauma in guinea pigs. Anesthetized guinea pigs were immersed into room temperature water (nonburned) or boiling water (burned) to the iliac crest for three seconds and sacrificed seven or 24 hours later. Myocardial and adipose tissue LPL activities were 60% and 125% greater, respectively, in burned guinea pigs 24 hours after injury than in nonburned animals. LPL activity in skeletal muscle from the burned region, red vastus, was significantly increased seven hours after injury, but the change after 24 hours was not significant. Muscle LPL activities examined in the nonburned region, diaphragm and red triceps, were increased 24 hours after thermal injury. Increased tissue LPL activities after thermal injury may enhance the clearance of circulating triglycerides.
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PMID:Increased tissue lipoprotein lipase activity in guinea pigs following burn trauma. 722 38

The biochemical basis for the observed depletion of adipose tissue in C57BL mice bearing a transplantable nonmetastasizing preputial gland tumor, ESR-586, has been investigated. The results have shown that there are a number of significant changes in both deposition and mobilization of lipid as the tumor grows. The first change, before the tumor reached 2 g, was a decline in the activity of adipose tissue lipoprotein lipase to levels normally found in starved animals. This was accompanied by a slight increase in lipoprotein lipase activity in heart and appearance of substantial activity in large tumors. Together, these would result in impaired uptake of exogenous fatty acids by adipose tissue, and dietary lipid would be directed away from storage. This was followed by a marked decline in endogenous lipid synthesis in adipose tissue which commenced when the tumor weighed between 2 and 3 g, as measured in vivo by the incorporation of radioactivity into lipid from tritiated water. The basal rate of lipolysis was enhanced 2-fold in epididymal fat pads from mice bearing tumors that weighed between 2 and 4 g, although there was no difference in the epinephrine-stimulated activity.
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PMID:Modified lipoprotein lipase activities, rates of lipogenesis, and lipolysis as factors leading to lipid depletion in C57BL mice bearing the preputial gland tumor, ESR-586. 724 77

Following a short period of fasting, with free access to water, lipid droplet accumulation (LDA) occurs in many glandular organs as well as in the heart of several species. The present work describes the changes in the hearts of male and female rats of different ages (6, 12, 18 and 24 weeks) deprived of food for 1, 2 and 3 days. LDA was demonstrated by staining with Oil Red O and a special "scoring" system was developed based on sections arbitrarily divided into five regions for each ventricle and two for each atrium. Three standard sections were studied from each heart. This system largely avoided problems arising from the uneven distribution of fats in different parts of the heart. In control animals very little fat was seen in any part of the heart. The pattern of changes was similar in males and females but the degree of LDA was usually much greater in the male. In both sexes LDA increased after 1 day and usually reached a peak by the second day, followed by a sharp decrease, returning to almost normal. However in both sexes the response in the 18-week-old animals was minimal, with no clear peak. The LDA was always maximal in the R ventricle, followed by the L ventricle. The heaviest deposition occurred in the superior parts of the ventricles, close to the atria. LDA was comparatively rare in the atria. Fat appeared to be retained longest in the most heavily loaded regions. Recovery from LDA was rapid, being almost complete 24 hr after returning to a normal diet. Again the most heavily loaded regions retained fat longest. These findings are discussed in related to possible anatomical factors such as the distribution of blood vessels. It is unlikely that such factors offer an adequate explanation abd it is suggested that since the uptake of fats into the heart is probably controlled by lipoprotein lipase the distribution of this enzyme in difference parts of the heart should be investigated. The histochemical changes are also discussed in relation to previous biochemical work. Finally it is pointed out that it is common procedure to fast experimental animals overnight and even such a brief period could bring about considerable histological and metabolic changes.
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PMID:Fat accumulation in the rat heart during fasting. 731 May 72

The effect of feeding various carbohydrates on the activity of lipoprotein lipase (LPL) released by heparin from perfused rat heart was investigated. Animals fasted for 8 to 12 hours were given a single 3-ml dose of 60% (w/v) glucose, sucrose or fructose solution or 3 ml water by intubation. After various time intervals, the hearts were removed and perfused with Krebs-Ringer bicarbonate buffer containing 1 unit heparin/ml. The perfusate was then assayed for LPL activity. From 35 to 80 minutes after feeding the LPL activity released by heparin from hearts of the glucose fed animals decreased 85% compared to the LPL activity released from hearts of the control group fed water. A similar decline in lipase activity was seen in the sucrose-fed group. In contrast to the glucose and sucrose data, fructose feeding produced no change in the heparin-releasable LPL activity compared with the control animals fed water. The LPL activity remaining in the heart tissue after perfusion with heparin was not significantly different in the experimental and control groups. The capacity of the hearts to hydrolyze 14C-labeled chylomicrons following glucose or sucrose feeding was also reduced by 70 to 85%.
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PMID:Rapid changes in rat heart lipoprotein lipase activity after feeding carbohydrate. 735 19

The rate at which lipoprotein lipase hydrolyzes triglycerides in lipoproteins and in synthetic emulsions decreases sharply with the amount of products formed unless albumin is present. Three factors which contribute to this inhibition as follows. (a) The fatty acids and the monoglycerides formed on hydrolysis locate at the lipid-water interface of the emulsion and, since they are substrates for the enzyme, act as competitive inhibitors of triglyceride hydrolysis. (b) The enzyme forms complexes with fatty acids. Therefore, as fatty acids accumulate in the system some of the enzyme will be sequestered into enzyme-fatty acid complexes. Albumin can prevent formation of such complexes since it has a higher affinity for fatty acids than the enzyme has. (c) Activator proteins do not enhance triglyceride hydrolysis unless a fatty acid acceptor is present. The strong inhibition of the enzyme itself and the loss of lipolysis-stimulating effects of activator proteins provide a feed-back regulation of the action of the lipase on lipoproteins at the capillary endothelium, ensuring that products are not generated more rapidly than they are utilized by the tissue.
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PMID:Lipoprotein lipase. Mechanism of product inhibition. 739 27

Purified bovine milk lipoprotein lipase has been covalently attached to CH-Sepharose with water-soluble carbodiimide. The immobilized enzyme retained enzymic activity and was stimulated 7-fold by the addition of human apolipoprotein C-II. Both [3H]heparin and 125I-labeled apolipoprotein C-II bound to the immobilized enzyme; unlabeled heparin and apolipoprotein C-II competed for binding of their respective labeled compounds. Apolipoprotein C-II did not compete for binding of [3H]heparin and vice versa. Human apolipoprotein C-III did not bind to the immobilized enzyme nor did it compete for apolipoprotein C-II binding. We conclude from these studies that both apolipoprotein C-II and heparin interact with immobilized lipoprotein lipase and that they have different binding sites.
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PMID:Preparation and properties of immobilized lipoprotein lipase. 743 56

Five microbial lipases from Chromobacterium viscosum, Candida cylindracea, Pseudomonas (source Fluka), Pseudomonas (source Genzyme) and lipoprotein lipase ex Microbial (Genzyme) have been screened for lactonisation activity towards 16-hydroxyhexadecanoic acid (HHA) in a variety of different w/o microemulsion systems. With the exception of Candida cylindracea (CC), all the lipases exhibited lactonisation activity although they were inherently more active in microemulsion systems based on the anionic surfactant sodium bis(2-ethylhexyl)sulphosuccinate (AOT) than in those based on the cationic surfactant cetyltrimethylammonium bromide (CTAB). Lactone yields are typically 50-60% and are markedly better than those reported previously using microemulsions in combination with chemical catalysts. Lipase stability is superior in the CTAB microemulsion systems, while lipase stability in the low water content AOT microemulsion systems was still good with the exception of CC lipase, which is rapidly inactivated. Buffering the water pools of AOT microemulsions using diglycine buffer at pH 8.0 improved biocatalyst stability. The lactonisation activity of lipases in CTAB w/o microemulsion systems compares favourably with that obtained using the same preparations as a solid suspension in the corresponding water-saturated organic solvent. In addition, the unusual solubility properties of microemulsions allowed the use of considerably higher concentrations of substrate in the microemulsion systems as compared to water-saturated organic solvents such as n-heptane. Lactone yields obtained at equivalent concentrations in the corresponding organic solvents containing conventional condensation catalysts were consistently measured at approx. 10%.
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PMID:Macrocyclic lactone synthesis by lipases in water-in-oil microemulsions. 754 59

We synthesized enantiomeric 1-O-alkyl-2,3-diacyl-sn-glycerol and 3-O-alkyl-1,2-diacyl-sn-glycerol containing pyrene as a fluorescent reporter and the trinitrophenylamino residue as a fluorescence quencher; both reporter groups were covalently bound to the omega end of the acyl chains at positions sn-2 and sn-3(1), respectively. The fluorescence of the intact substrate molecules was very low. Chemical or enzymic release of the fatty acyl chains lead to fluorescence dequenching. The rate of lipolysis could be measured from the time-dependent increase in fluorescence intensity. We used the respective substrates for the continuous determination of activity and stereopreference of four different microbial lipases from Chromobacterium viscosum, Candida rugosa, Pseudomonas sp., Rhizopus arrhizus, as well as cutinase from Fusarium solani and lipoprotein lipase from bovine milk. The stereopreference of the lipases depended, in general, on how the substrate was solubilized in the reaction medium. All lipases under investigation preferentially hydrolysed the sn-1 acyl ester bond, if the lipid analog was dispersed in albumin-containing Tris/HCl buffer in the absence of detergent or organic solvent. In mixtures of 1:1 (by vol.) water/ethanol, the enzymes showed higher activity toward the sn-3 acyl ester bond, except for lipoprotein lipase which preferred the sn-1 acyl isomer under all conditions tested. Different stereopreferences were observed with the different lipases if the substrate was solubilized by amphiphiles (micelles of N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate). C. rugosa lipase and F. solani cutinase showed high stereopreference for the sn-3 acyl ester, whereas Pseudomonas sp. lipase and C. viscosum lipase hydrolysed both enantiomers at similar rates. From spectroscopic studies, it can be inferred that the conformation of the fluorescent lipids is probably similar in water, mixtures of water and organic solvents, and in micelles. The possible effects of reaction conditions on substrate accessibility and enzyme conformation on stereoselectivity of the respective lipases are discussed.
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PMID:Inversion of lipase stereospecificity for fluorogenic alkyldiacyl glycerols. Effect of substrate solubilization. 762 84

The decrease in myocardial lipoprotein lipase (LPL) activity observed previously in acute, severe models of insulin-deficient diabetes may be a compensatory response to hypertriglyceridemia and a sustained increase in fatty acid delivery to cardiomyocytes. The administration of fructose (10% solution in the drinking water for 4 days) to rats produced hypertriglyceridemia, but heparin-releasable LPL activity from perfused hearts and total and heparin-releasable LPL activities in isolated cardiomyocytes were not reduced. The acute (4 day) induction of a mild diabetic state (60 mg/kg streptozotocin) resulted in modest hypertriglyceridemia, and a selective decrease in heparin-releasable LPL activity in perfused hearts; LPL activity in cardiomyocytes from diabetic rat hearts was not reduced. Therefore, the diabetes-induced fall in myocardial LPL activity is not secondary to hypertriglyceridemia, since fructose treatment did not change LPL activity. Perfusion of rat hearts with 100 microM lysophosphatidylcholine (LPC) released a small amount of LPL activity into the perfusate, but only if albumin was omitted from the perfusion solution. Thus, the selective reduction in heparin-releasable LPL activity in perfused diabetic hearts is probably not the consequence of displacement by LPC, a lipolytic product of the LPL-catalyzed degradation of triacylglycerol-rich lipoproteins. Circulating LPL activity in the plasma of diabetic rats was not decreased relative to control plasma enzyme activity; therefore, the reduction in heparin-releasable LPL activity is not because circulating LPL was less available for uptake by the endothelium in diabetic hearts.
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PMID:Myocardial lipoprotein lipase activity: regulation by diabetes and fructose-induced hypertriglyceridemia. 764 16

Previous studies with healthy volunteers and non-insulin-dependent diabetic (NIDDM) patients have shown a strong association between overall glucose metabolism and hepatic microsomal enzyme activity. In this study, the effects of 10-day oral administration of phenobarbital (PB), a potent inducer of the hepatic microsomal mixed-function oxidase system, on carbohydrate and lipid metabolism in the basal state and on glucose kinetics during submaximal hyperinsulinemic (5 mU.kg-1.min-1 insulin) clamps were investigated in nondiabetic rats and in rats made diabetic by the intravenous (IV) administration of either low-dose (40 mg/kg) or high-dose (55 mg/kg) streptozocin (STZ). In control rats receiving PB in drinking water (0.5 mg/mL), serum insulin and triglyceride levels were diminished without any change in glucose and cholesterol concentrations in the fed state. Administration of PB in drinking water (0.25 mg/mL) to both groups of diabetic rats decreased their water intake and serum triglyceride levels in the absence of an effect on glucose, insulin, and cholesterol concentrations in the fed state. However, fasting serum glucose levels and basal glucose turnover rates were lower in both groups of diabetic rats receiving PB. PB treatment increased the heparin-releasable lipoprotein lipase (LPL) activity of epididymal fat in both control and low-dose diabetic groups; this was not assessed in the high-dose diabetic group. Neither peripheral glucose utilization nor hepatic glucose production during submaximal insulin clamps was modified by PB treatment in nondiabetic rats. In contrast, PB administration enhanced insulin-mediated peripheral glucose utilization, as well as suppression of hepatic glucose production, in both low-dose and high-dose diabetic groups.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phenobarbital treatment enhances insulin-mediated glucose metabolism and improves lipid metabolism in the diabetic rat. 813 83


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