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

Little is known about the effects of pre- and early postnatal protein malnutrition on energy storage (e.g., carcass lipid) and expenditure (e.g., brown adipose tissue [BAT] thermogenesis) and their reversibility by nutritional rehabilitation. Therefore, the purpose of these experiments was to examine the permanence of prenatal and early postnatal protein malnutrition on energy balance in rats. Five weeks before mating and through gestation adult female rats were fed either a 25 or 8% casein diet (designated 25 or 8). Diet reversals were performed at birth and/or at weaning (designated B or W) and the pups were cross-fostered at birth. Thus, the groups were: 25-25B (controls), 8-25W (gestational and lactational protein malnutrition, 8-25B (gestational protein malnutrition), and 25-8B-25W (lactational protein malnutrition). Animals were weighed and sacrificed 200-250 days postpartum for carcass composition. Retroperitoneal white adipose tissue (RWAT) and interscapular BAT (IBAT) wet weights and lipoprotein lipase (LPL) activity were also measured in the 25-25B and 8-25W groups. Nutritional rehabilitation at birth (8-25B) resulted in normal body weights as adults. Lactational protein malnutrition (25-8B-25W) resulted in intermediate body weights to the controls (25-25W), which had the greatest weights, and the 8-25W group, which had the lowest weights. The 8-25W and 25-8B-25W rats also had significantly decreased carcass wet weight and total body water, fat and fat-free dry mass relative to the 25-25B and 8-25B groups, the latter two of which did not differ in their carcass composition.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of pre- and early postnatal protein malnutrition on carcass composition and lipoprotein lipase activity in male rats. 360 24

The effects of bovine serum albumin on rat pancreatic lipase and bovine milk lipoprotein lipase were studied in a system of triacylglycerol emulsions stabilized by 1 1 mg/ml albumin. At concentrations greater than 1 mg/ml, albumin inhibited the activity of pancreatic lipase and interfered with enzyme binding to emulsified triacylglycerol particles. These effects could be countered by occupying five fatty acid binding sites on albumin with oleic acid. Following an initial lag period which increased with albumin concentrations, enzyme activity escaped from inhibition presumably due to saturation of fatty acid sites on albumin with oleic acid. Pancreatic lipase was active at 1 mg/ml albumin and 1 mM emulsion-bound oleic acid in the system. The effects of albumin on lipoprotein lipase were diametrically opposed to the above; enzyme activity was completely inhibited by 0.1 mM oleic acid, it increased with increasing fatty acid-free albumin concentrations and decreased as the fatty acid sites on albumin were filled. At 1 mM oleic acid and no added albumin the enzyme failed to bind at the oil water interface, whereas fatty acid-free or saturated albumin had no effect on binding. It is concluded that if the inhibition of pancreatic lipase by albumin is due to the inaccessibility of the enzyme to an oil-water interface blocked by denatured albumin, then albumin saturated with oleic acid would seem to be protected from unfolding at the interface and more readily displaced by the lipase. Pancreatic lipase and lipoprotein lipase, although sharing a number of common features, are distinct enzymes both functionally and mechanistically.
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PMID:The effects of bovine serum albumin and oleic acid on rat pancreatic lipase and bovine milk lipoprotein lipase. 360 28

The fatty acyl (lipid) p-nitrophenyl esters p-nitrophenyl caprylate, p-nitrophenyl laurate and p-nitrophenyl palmitate that are incorporated at a few mol % into mixed micelles with Triton X-100 are substrates for bovine milk lipoprotein lipase. When the concentration of components of the mixed micelles is approximately equal to or greater than the critical micelle concentration, time courses for lipoprotein lipase-catalyzed hydrolysis of the esters are described by the integrated form of the Michaelis-Menten equation. Least square fitting to the integrated equation therefore allows calculation of the interfacial kinetic parameters Km and Vmax from single runs. The computational methodology used to determine the interfacial kinetic parameters is described in this paper and is used to determine the intrinsic substrate fatty acyl specificity of lipoprotein lipase catalysis, which is reflected in the magnitude of kcat/Km and kcat. The results for interfacial lipoprotein lipase catalysis, along with previously determined kinetic parameters for the water-soluble esters p-nitrophenyl acetate and p-nitrophenyl butyrate, indicate that lipoprotein lipase has highest specificity for the substrates that have fatty acyl chains of intermediate length (i.e. p-nitrophenyl butyrate and p-nitrophenyl caprylate). The fatty acid products do not cause product inhibition during lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl esters that are contained in Triton X-100 micelles. The effects of the nucleophiles hydroxylamine, hydrazine, and ethylenediamine on Km and Vmax for lipoprotein lipase catalyzed hydrolysis of p-nitrophenyl laurate are consistent with trapping of a lauryl-lipoprotein lipase intermediate. This mechanism is confirmed by analysis of the product lauryl hydroxamate when hydroxylamine is the nucleophile. Hence, lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl esters that are contained in Triton X-100 micelles occurs via an interfacial acyl-lipoprotein lipase mechanism that is rate-limited by hydrolysis of the acyl-enzyme intermediate.
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PMID:Interfacial reaction dynamics and acyl-enzyme mechanism for lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl esters. 374 78

Brown fat lipoprotein lipase activity did not change in the first two weeks of pregnancy whereas it decreased on day 18 of gestation and was lower during late pregnancy and lactation. Fatty acid synthesis rate, measured in vivo with (3H)H2O, showed a progressive increase until day 18 of gestation followed by a decrease on day 20 of pregnancy and a reduced lipogenesis rate throughout lactation. The early reduction in the pathways of fatty acid uptake and synthesis in brown fat during the breeding cycle of the rat suggests the possibility that a decline in the substrate supply was a factor contributing to the reduced thermogenic activity of brown adipose tissue after parturition.
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PMID:Changes in brown adipose tissue lipoprotein lipase activity and lipogenesis rate during pregnancy and lactation in the rat. 379 Jan 43

The cholesterol esterase and lipoprotein lipase catalyzed hydrolyses of the water-soluble substrate p-nitrophenyl butyrate are competitively inhibited by butaneboronic acid and phenylboronic acid. Phenyl-n-butylborinic acid has been synthesized and characterized as an ultrapotent transition state analog inhibitor: Ki = 2.9 +/- 0.6 nM and 1.7 +/- 0.3 microM for the cholesterol esterase and lipoprotein lipase reactions, respectively. These results are interpreted in terms of transition state structure and stabilization.
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PMID:Phenyl-n-butylborinic acid is a potent transition state analog inhibitor of lipolytic enzymes. 394 31

Ten murine monoclonal antibodies have been produced that are specific for bovine milk lipoprotein lipase. One monoclonal antibody, bLPL-mAb-7, inhibited completely the apolipoprotein C-II (apo-C-II)-dependent enzymic hydrolysis of trioleoylglycerol in a phospholipid-stabilized emulsion, but had no effect on the hydrolysis of the water-soluble substrate p-nitro-phenylacetate. Four times more bLPL-mAb-7 was required to achieve 50% inactivation of lipoprotein lipase activity when the enzyme was preincubated with excess apo-C-II. Disruption of the binding of a dansyl-labeled apo-C-II peptide to lipoprotein lipase by bLPL-mAb-7 was demonstrated by resonance energy transfer, both in the presence and absence of lipid. This antibody thus appears to recognize the apo-C-II binding site of lipoprotein lipase. In addition, bLPL-mAb-7 also inhibited the lipoprotein lipase activity of human post-heparin plasma.
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PMID:Monoclonal antibodies against bovine milk lipoprotein lipase. Characterization of an antibody specific for the apolipoprotein C-II binding site. 396 71

Diethyl-p-nitrophenyl phosphate is an active site-directed irreversible inhibitor of bovine milk lipoprotein lipase catalyzed hydrolysis of the water-soluble substrate, p-nitrophenyl butyrate. Interaction of lipoprotein lipase and the inhibitor in the absence of substrate gives a biphasic kinetics profile, which is consistent with rapid formation of a phosphoryl-lipoprotein lipase intermediate which hydrolyzes slowly. The magnitude of the absorbance increase accompanying formation of the intermediate provides an analytical method for determining lipoprotein lipase active site concentration.
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PMID:Diethyl-p-nitrophenyl phosphate: an active site titrant for lipoprotein lipase. 399 64

Solvent deuterium isotope effects on the rates of lipoprotein lipase (LpL) catalyzed hydrolysis of the water-soluble esters p-nitrophenyl acetate (PNPA) and p-nitrophenyl butyrate (PNPB) have been measured and fall in the range 1.5-2.2. The isotope effects are independent of substrate concentration, LpL stability, and reaction temperature and hence are effects on chemical catalysis and not due to a medium effect of D2O on LpL stability and/or conformation. pL (L = H or D) vs. rate profiles for the Vmax/Km of LpL-catalyzed hydrolysis of PNPB increase sigmoidally with increasing pL. Least-squares analysis of the profiles gives pKaH2O = 7.10 +/- 0.01, pKaD2O = 7.795 +/- 0.007, and a solvent isotope effect on limiting velocity at high pL of 1.97 +/- 0.03. Because the pL-rate profiles are for the Vmax/Km of hydrolysis of a water-soluble substrate, the measured pKa's are intrinsic acid-base ionization constants for a catalytically involved LpL active-site amino acid side chain. Benzeneboronic acid, a potent inhibitor of LpL-catalyzed hydrolysis of triacylglycerols [Vainio, P., Virtanen, J. A., & Kinnunen, P. K. J. (1982) Biochim. Biophys. Acta 711, 386-390], inhibits LpL-catalyzed hydrolysis of PNPB, with Ki = 6.9 microM at pH 7.36, 25 degrees C. This result and the solvent isotope effects for LpL-catalyzed hydrolysis of water-soluble esters are interpreted in terms of a proton transfer mechanism that is similar in many respects to that of the serine proteases.
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PMID:Solvent isotope effects for lipoprotein lipase catalyzed hydrolysis of water-soluble p-nitrophenyl esters. 402 37

Biochemical mechanisms underlying the development of alcoholic fatty liver was investigated. Acute ethanol (EtOH) administration for 3 days by an inhalation method, and continuous EtOH treatments by feeding with liquid diet or drinking water containing EtOH induced a significant increase of hepatic triglycerides (TG). A small but significant increase of TG was also observed in the blood serum. Although hepatic acetyl CoA carboxylase activity, measured in the presence and absence of citrate, was not altered by either acute or chronic EtOH administrations, fatty acid synthetase and malic enzyme activities in the liver were increased by continuous EtOH administration, but not in the acutely EtOH-treated animals. The incorporations of [14C]palmitate and [14C]acetate into hepatic RG were also increased significantly in animals treated continuously with EtOH. The lipoprotein lipase activity in adipose tissues was activated by both acute and continuous EtOH treatments, whereas lipase activity in adipose tissues and the epinephrine-stimulated and cyclic AMP-mediated release of free fatty acid (FFA) from this tissue were not altered by these treatments. These results indicate that acute alcoholic fatty liver is caused mostly by the increased mobilization of FFA from peripheral adipose tissues via the activation of lipoprotein lipase, whereas alcoholic fatty liver induced by continuous EtOH administration involves the increased synthesis of FFA due to the activation of fatty acid synthetase and malic enzyme in the liver in addition to the increased mobilization of peripheral FFA.
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PMID:Hepatic lipogenesis and mobilization of peripheral fats in the formation of alcoholic fatty liver. 612 Oct 72

Adult male voles were maintained for 10 wk in long or short photoperiods (14 or 10 h of light/day). A third group of animals housed in the long photoperiod was implanted with capsules containing melatonin. Body weight and food intake were measured weekly; various tissues were weighed and analyzed at the time of autopsy. After 10 wk, voles in the short photoperiod weighed 20% less and consumed 30% less food than those housed in the long photoperiod. Total body water and lean body mass were reduced in the short-day animals, although the size of the brown adipose tissue was not affected. White adipose tissue lipoprotein lipase (LPL) activity was markedly reduced in the short-day voles who also manifested gonadal regression and suppression of spermatogenesis. Melatonin mimicked the effects of short photoperiods on LPL activity and on lean body mass; other parameters for melatonin-treated animals were intermediate between those of untreated long- and short-day voles. We hypothesize that winter weight losses experienced by meadow voles in the field are mediated by decreases in the duration of the daily photophase and that the reduction in body mass permits overwintering voles to reduce their energy requirements and the amount of time devoted to foraging. At least part of the seasonal decline in body mass appears due to a decrease in gonadal hormone secretion.
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PMID:Photoperiodic regulation of body mass, food intake, and reproduction in meadow voles. 635 38


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