Adipose Tissue Lipase Activity Research Articles

Acute changes in triacylglycerol lipase activity of human adipose tissue during exercise

Although physical exercise is known to increase adipose tissue lipolysis, its effect on the activity of triacylglycerol (TG) lipase, the enzyme regulating TG breakdown, is not known. The aim of the present study was to monitor the acute changes in TG lipase activity of adipose tissue induced during moderate exercise. For this purpose a new assay, sensitive to the phosphorylation state of the enzyme, was developed. Ten young sedentary men cycled for 30 min at a heart rate of 120-130 beats min(-1). Needle adipose tissue biopsy was performed from the buttock area at rest, at 5, 15, and 30 min of exercise, as well as at 15 min of passive recovery. Five other men served as controls by being biopsied as above without exercising. TG lipase activity was determined by measuring the decrease of endogenous TG concentration during incubation of the homogenized tissue. TG lipase activity increased 6.4-fold above baseline at 5 min of exercise (P < 0.001) and fell gradually afterwards, whereas it did not change significantly in the control group. In conclusion, our data show that TG lipase activity in human adipose tissue peaks early during exercise and subsequently decreases despite the maintenance of the physical stimulus.

Effects of sirolimus on plasma lipids, lipoprotein levels, and fatty acid metabolism in renal transplant patients

Sirolimus (Rapammune, rapamycin, RAPA) is a potent immunosuppressive drug that reduces renal transplant rejection. Hyperlipidemia is a significant side effect of sirolimus treatment, and frequently leads to cardiovascular disease. This study was undertaken to determine the repeatability, reversibility, and dose dependence of the plasma lipid and apolipoprotein altering effects of sirolimus, and to elucidate the mechanism by which sirolimus induces hypertriglyceridemia in some renal transplant patients. Six patients with renal allografts maintained on cyclosporine A and prednisone were selected on the basis of their previous hyperlipidemic response to short term (14 days) sirolimus administration. For longer-term treatment, each patient was started on 10 mg/day sirolimus and continued as tolerated for 42 days to reinduce hyperlipidemia. Timed blood samples were analyzed for lipid, apolipoprotein, and sirolimus levels. During sirolimus administration, mean total plasma cholesterol increased from 214 mg/dl to 322 mg/dl (+50%; range 25-92%); LDL-cholesterol levels followed a similar pattern. Mean triglyceride level rose from 227 to 432 mg/dl (+95%; range 9-254%). ApoB-100 concentration rose from 124 to 160 mg/dl (+28%; P < 0.05). ApoC-III level increased from 28.9 to 55.5 mg/dl, +92%; (P < 0.013). These lipid and apolipoprotein changes were found to be repeatable, reversible, and dose dependent. [(13)C(4)]palmitate metabolic studies in four patients with hypertriglyceridemia indicated that the free fatty acid pool was expanded by sirolimus treatment (mean = 42.3%). Incorporation of [(13)C(4)]palmitate into triglycerides of VLDL, IDL, and LDL was decreased 38.3%, 42,1%, and 38.4%, respectively, by sirolimus treatment of these patients. These results suggest that sirolimus alters the insulin signaling pathway so as to increase adipose tissue lipase activity and/or decrease lipoprotein lipase activity, resulting in increased hepatic synthesis of triglyceride, increased secretion of VLDL, and increased hypertriglyceridemia.

The influence of fasting/refeeding on the lipoprotein lipase activity of adipose tissue and muscle.

Lipoprotein lipase activity in adipose tissue and muscle is modulated by changes in the pattern of food intake. We have measured total lipoprotein lipase activity in adipose tissue and muscle of male Wistar rats (N = 6-10), weighing 200-250 g (~12 weeks), during the refeeding/fasting state following 24 h of fasting. Lipoprotein lipase activity in tissue homogenates was evaluated using a [3H]-triolein-containing substrate, and released [3H]-free fatty acids were extracted and quantified by liquid scintillation. Adipose tissue lipoprotein lipase activity did not completely recover within 2 h of refeeding (60% of refed ad libitum values). Cardiac lipoprotein lipase activity remained increased even 2 h after refeeding (100% of refed ad libitum values), whereas no significant changes were observed in the soleus and diaphragm muscles. Adipose tissue lipoprotein lipase activities were consistently higher than the highest skeletal muscle or heart values. It is therefore likely that adipose tissue, rather than muscle makes the major contribution to triacylglycerol clearance. There was concomitant relatively high lipoprotein lipase activity in both adipose tissue and cardiac muscle during the first few hours of refeeding, therefore cardiac muscle may contribute significantly to triacylglycerol clearance during this period. The results suggest that during fasting, increased lipoprotein lipase activity provides a complementary source of free fatty acids from circulating triacylglycerol, allowing the heart to maintain its continuous, high-energy expenditure.

Hypolipidemic effect of pantothenic acid derivatives in mice with hypothalamic obesity induced by aurothioglucose

The hypolipidemic effects of pantothenic acid derivatives (phosphopantothenate, panthenol and pantethine) were studied in mice with hypothalamic obesity. Hypothalamic obesity in mice was induced by single injection of aurothioglucose (300 mg/kg body wt, i.p.). All the tested substances were administered during the last 10 days before decapitation (i.m., of dosage equivalent to 150 mg/kg body wt of phosphopantothenate). The studied substances inhibited the weight gain of the animals with hypothalamic obesity over the last 10 days of the experiment. The treatment with aurothioglucose increased food intake and mean body weight, blood glucose level; insulin, serum total cholesterol, triglyceride, the sum of LDL + VLDL and LDL-cholesterol concentration; triglyceride and cholesterol fractions in the liver; triglyceride and FFA content as well as lipoprotein lipase activity in adipose tissue of experimental mice. The administration of the assay compounds lowered food intake and mean body weight, insulin and glucose levels and decreased the content of triglycerides, total cholesterol and cholesterol esters in serum and adipose tissue as well as raised the activity of lipoprotein lipase in adipose tissue and serum lipolytic activity in obese mice. Among the compounds studied the reverse effect of panthenol was especially pronounced. The mechanism of hypolipidemic effects of pantothenic acid derivatives can be related to the reduced resistance to insulin and activation of lipolysis in serum and adipose tissue.

Effect of gemfibrozil on triacylglycerol synthesis and secretion by liver and lipoprotein lipase activity in adipose tissue of rats

The role of gemfibrozil, a hypotriglyceridemic drug, in synthesis, secretion and catabolism of triacylglycerols (TG) in rats was assessed. Chow diet-fed Sprague–Dawley rats were given various doses of gemfibrozil (10, 30 and 100 mg/kg body weight) for 2 weeks. Rats receiving the drug at the lowest dose significantly lowered the concentration of serum TG and apolipoprotein (apo) B in comparison with control rats. Synthesis of fatty acids from [ 14C]acetate and esterification of [ 14C]oleate to TG by the liver were not suppressed by the drug. Secretion rates of TG and apo B, measured by the Triton method, were suppressed at the highest dose. Lipoprotein lipase activity of the acetone powder prepared from adipose tissue was not influenced by the drug. These results indicate that the primary cause of hypotriglyceridemic action of gemfibrozil is not due to suppressing synthesis and secretion of TG by the liver or enhancing lipoprotein lipase activity in adipose tissues.

Addition of fat to the diets of lactating sows: II. Effects on hormone-sensitive lipase activity, energy mobilization in response to epinephrine, and plasma insulin and glucose concentrations.

Four experiments were conducted to determine the effects of dietary fat on lipolysis in lactating sows. In Exp. 1, a 6 x 6 Latin square was used to determine the optimal dosage of epinephrine for use in a subsequent epinephrine challenge. Peak concentrations of plasma glucose and response area increased linearly (P < .10) with epinephrine dosage. However, plasma NEFA peak and response area were quadratically affected (P < .05 and .06, respectively) by epinephrine dosage, with a minimum NEFA peak concentration observed at .4 microg/kg and a maximum at 1.6 microg/kg. In Exp. 2, the effect of dietary tallow on the response to epinephrine infusion (1.6 microg/kg BW) was examined. No differences (P > .10) between treatments were observed in NEFA, glycerol, or peak concentrations of plasma glucose following epinephrine administration. In Exp. 3, the effect of dietary fat on hormone-sensitive lipase activity was examined. Sows (n = 36) were fed diets containing either 0 or 10% added tallow. Hormone-sensitive lipase activity on d 28 of lactation was increased by the addition of tallow to the diet (P = .06). No effect of dietary tallow was observed on hormone-sensitive lipase activity of adipose tissue on d 21 of lactation (P > .10) in Exp. 3 (n = 16 sows) and Exp. 4 (n = 30 sows). In summary, diets containing 10% added tallow did not alter the rate of lipolysis, as measured by exogenous epinephrine challenge, in adipose tissue of lactating sows.

Lipoprotein and hormone-sensitive lipases in porcine adipose tissue.

Lipoprotein lipase (LPL) is an adipocyte enzyme that cleaves fatty acids from circulating lipoproteins. Fatty acids enter the cell to be oxidized or esterified. Hormone-sensitive lipase (HSL) is an adipocyte enzyme that cleaves fatty acids from intracellular triacylglycerol. The HSL is activated by phosphorylation. Assays for the two lipases are complex because the hydrophobic substrate, triacylglycerol, must be presented as a gum-based suspension or as a detergent-based emulsion to a relatively hydrophilic enzyme. A convenient, stable glycerol/phospholipid suspension of the substrate was used for measurement of porcine adipose tissue LPL and HSL in vitro. This substrate was excellent for LPL. It produced rates five times those using a more complex and less convenient gum-based substrate suspension. The LPL activity was released by heparin, had a pH optimum of approximately 8.5, was activated by serum, and was inhibited by NaCl and protamine. This LPL assay measures enzyme capacity. The same substrate was used to measure an adipose tissue lipase activity that had a pH optimum below 7, was not activated by serum, and was not inhibited by NaCl or protamine. These are all characteristics of HSL. Despite the convenience, this substrate was not appropriate for porcine adipose tissue HSL because the rates were only 30 to 50% of those produced with a more complex, less convenient gum-based substrate suspension. Furthermore, incubation of enzyme or tissue slices with insulin, or agents that elevate cAMP concentration, did not modulate this lipase activity, as expected. These incubations poorly modulated LPL activity.

2] Regulation of hormone-sensitive lipase activity in adipose tissue

Hormone-sensitive lipase (HSL) is known to be phosphorylated at two distinct serine residues, termed the regulatory and basal sites, respectively. cAMP-PK phosphorylates HSL at the regulatory site. Studies in isolated rat adipocytes have shown the extent of phosphorylation at the regulatory site correlates with the rate of lipolysis. The mechanism underlying activation through phosphorylation the regulatory site of HSL by cAMP-PK is poorly understood. The basal site of HSL is located only two amino acids C terminal of the regulatory site. Phosphorylation of this site occurs without any direct effect on enzyme activity. Studies in isolated rat adipocytes have indicated that the basal site is phosphorylated to a large extent in unstimulated cells. This, together with the observation that phosphorylation of the two sites seems to be mutually exclusive, suggests that phosphorylation of the basal site has an antilipolytic role in vivo , and that phosphorylation of the regulatory site by cAMP-PK has to be preceded by a dephosphorylation of the basal site.

Lipoprotein lipase mRNA levels in adipose tissue in lactation.

In lactation metabolic adaptations occur to ensure that the mammary gland is continuously supplied with substrates for milk production. One of these changes is that the activity of lipoprotein lipase is decreased in adipose tissue but increased in mammary gland thereby aiding in the direction of lipid to mammary gland [l-31. AAer removal of the litter lipoprotein lipase activity increases again [4,5]. The aim of this work was to determine whether the low lipoprotein lipase activity in adipose tissue in lactation could be explained by a decrease in lipoprotein lipase mRNA levels. Lipoprotein lipase activity was measured in infranates of homogenates [6] of rat parametrial adipose tissue with Intralipid as substrate [7]. The results in Table 1 show that by 10 d of lactation lipoprotein lipase activity in parametrial adipose tissue had fallen to 33% of that in adipose tissue from virgin rats. At 24h after removal of the litter, lipoprotein lipase activity was still low. However, by 48h after removal of the litter lipoprotein lipase activity had returned to values similar to those in adipose tissue from virgin rats. Total RNA was extracted [8] and LPL and a-tubulin mRNA measured following Northern blotting [9]. The results in Table 2 show that lipoprotein lipase mRNA, but not a-tubulin mRNA, was decreased in parametrial adipose tissue compared to the values in virgin rats. Lipoprotein lipase mRNA levels had not increased by 24h after removal of the litter.

Fuel metabolism in growth hormone-deficient adults

Apart from being a stimulator of longitudinal growth, growth hormone (GH) regulates fuel metabolism in children and adults. A halfmark is mobilization of lipids, which involves an inhibition of lipoprotein lipase activity in adipose tissue and activation of the hormone sensitive lipase. Suppression of basal glucose oxidation and resistance to insulin are other important effects. This may cause concern during GH substitution in GH-deficient adults, some of whom may present with insulin resistance due to concomitant abdominal obesity. However, there are data to suggest that the GH-induced reduction in fat mass and increase in lean body mass may offset the insulin antagonistic actions of the hormone. The nitrogen-retaining effects of GH seem to involve a direct stimulation of protein synthesis in addition to secondary effects such as generation of insulin-like growth factor-I (IGF-I), hyperinsulinemia, and promotion of lipolysis. Thus, during periods of substrate affluence, GH acts in concert with insulin and IGF-I to promote protein anabolism. Postabsorptively, GH is primarily lipolytic and thereby indirectly protein-sparing. This effect becomes further accentuated with more prolonged fasting. In that sense, GH is unique by its preservation of protein during both feast and famine. These fuel metabolic effects add merit to the principle of GH substitution in hypopituitary adults.

Effects of somatostatin-25 on lipid mobilization from rainbow trout, Oncorhynchus mykiss, liver and adipose tissue incubated in vitro. Comparison with somatostatin-14

The physiological effects of the pancreatic peptides somatostatin-14 and somatostatin-25 on lipid metabolism in rainbow trout were evaluated by in vitro culture of liver and adipose tissue. The culture medium was subsequently analyzed for glycerol and fatty acid content and triacylglycerol lipase activity was measured within the tissues. Both somatostatin-14 and somatostatin-25 stimulated hepatic fatty acid and glycerol release within 3 h after treatment. Liver triacylglycerol lipase activity was elevated following treatment with somatostatin-14 (76% above control) or somatostatin-25 (94% above control). Somatostatin-14 and somatostatin-25 also significantly stimulated the release of fatty acid and glycerol from adipose tissue. Triacylglycerol lipase activity in adipose tissue also was enhanced by both somatostatins. These results indicate that somatostatin-14 and somatostatin-25 directly stimulate the mobilization of triacylglycerol from liver and adipose tissue, suggesting that these peptides are important systemic modulators of lipid metabolism in fish.

Experimental nephrotic syndrome: removal and tissue distribution of chylomicrons and very-low-density lipoproteins of normal and nephrotic origin

Lymph chylomicrons and plasma VLDL, 14C-labelled in vivo, were isolated from normal and nephrotic rats and injected into normal or nephrotic recipients. In normal recipients, the half-life of chylomicrons of nephrotic vs. normal origin was significantly longer (5.2 ± 0.5 vs. 3.5 ± 0.4 min −1). The nephrotic chylomicrons were larger in size, deficient in apo-E and apo A-I, rich in triacylglycerol and cholesterol, but poor in phospholipids, indicating that factors related to composition affected their removal. The half-life of nephrotic vs. normal VLDL, given to normal recipients, was unexpectedly shorter, (4.5 ± 0.2 vs. 5.8 ± 0.2 min −1). The nephrotic VLDL were also triacylglycerol- and cholesterol-rich and phospholipid-poor, but had a large diameter spread and contained a dense fraction according to the zonal ultracentrifugation pattern, suggesting the presence of faster removable IDL-like particles. When nephrotic rats received normal particles, a pronounced removal delay was seen, paralleling the extent of plasma triacylglycerol elevation. The half-life of chylomicrons was 8.3 ± 1.4 and 15.2 ± 2.5 min −1 in moderately and severely nephrotic rats, respectively, that of VLDL was 11.72 ± 2.1 and 37.8 ± 7.1 min −1 correspondingly. The chylomicron-triacylglycerol uptake was reduced both by adipose tissues and muscles of normal or nephrotic recipients, with some increase in entry into lungs, kidneys and spleen. Tissue distribution patterns of VLDL-triacylglycerol was similar to that of chylomicrons, except that the liver took up approx. 90% of the label. The low share of triacylglycerol uptake by tissues rich in lipoprotein lipase indicates that the activity of this enzyme was unlikely to limit the rate of removal. Lipoprotein lipase activity in adipose tissue and heart was slightly decreased in moderately nephrotic rats and declined only by approx. 35% in severely nephrotic ones. These results indicate that the removal defect in nephrosis seems to be due, in part, to changes in the composition of triacylglycerol-rich particles, compromising their accessibility to lipolysis and, in part, to their abundance, saturating the lipolytic capacity.

Lipid lowering effect of omega-3 fatty acids in genetically obese zucker rats

Omega-3 fatty acids (n-3 FA) are known to reduce blood lipid levels. Recent data, however, suggested that n-3 FA supplementation may worsen glycemic control in diabetic humans. This study was designed to explore the effects of n-3 FA feeding on lipid metabolism and glycemic control in a strain of genetically obese, hyperlipidemic rats. Lean and obese Zucker rats were fed a semi-purified diet made with either n-3 FA or corn oil (n-6, 10% w/w for both diets). After 16 weeks feeding, lean and obese rats fed the n-3 FA diet showed a significant reduction in blood triglyceride (TG) levels. Obese rats had significantly elevated TG levels in comparison with lean rats. Lean n-3 FA fed rats had elevated lipoprotein lipase activity in adipose tissue while hepatic triglyceride lipase activity was lowered by n-3 FA feeding in both lean and obese rats. Hepatic lipogenic enzyme activities were suppressed by fish oil feeding. However, fish oil feeding significantly increased hepatic gluconeogenic enzyme activity in lean rats. Therefore, n-3 FA feeding may exert different effects on blood lipid and glucose levels in lean and obese subjects.

Two different mechanisms are involved in nutritional regulation of lipoprotein lipase in guinea-pig adipose tissue.

Lipoprotein lipase activity in adipose tissue responds rapidly to changes in the physiological state. To study what mechanisms are involved in the regulation, guinea pigs were fasted and the decrease in adipose-tissue lipoprotein lipase activity was compared with the decreases in mRNA and lipase synthesis. The mRNA pattern (three species) did not change. There was a close parallelism between the abundance of lipase mRNA and relative lipase synthesis (immunoprecipitable 35S-labelled lipoprotein lipase as fraction of total [35S]protein after pulse-labelling with [35S]methionine). Total protein synthesis decreased on fasting, compounding the decrease in relative lipase synthesis. Lipoprotein lipase mRNA changed similarly in fat-pads and in isolated adipocytes, whereas lipase activity changed more in the pads, indicating disproportionally large changes in extracellularly located lipase. In old guinea pigs the decreases in lipoprotein lipase activity and lipase synthesis were comparable, but in young animals the change in lipase activity was substantially larger than the change in lipase synthesis. Refeeding of fasted young guinea pigs with glucose resulted in a rapid increase in lipoprotein lipase activity, but there was only a small change in lipase mRNA. Old animals responded slowly to refeeding. The results indicate that in older animals the major mechanism for regulation of adipose lipoprotein lipase activity is a relatively slow change in lipase mRNA, whereas in younger animals an additional, more rapid, regulation is exerted on the transport and turnover of the enzyme.

Effects of Doxazosin on Lipids, Lipoprotein Lipases, and Cholesterol Synthesis in the Golden Hamster

The effects of treatment with adrenoceptor blockers on sites regulating lipid metabolism were studied in golden hamsters. In hamsters fed a standard chow, doxazosin, propranolol, and atenolol did not affect plasma cholesterol or triglycerides. After hypercholesterolemia was induced by feeding a cholesterol-enriched diet, doxazosin lowered plasma cholesterol by 12%. Lipoprotein lipase activity in adipose tissue and in the heart was not changed by any of the treatments. Hepatic lipase activity in the liver and blood was lowered by 31% in the doxazosin-treated animals. Hepatic cholesterol synthesis, measured as acetate incorporation into cholesterol and hydroxymethylglutaryl coenzyme A (HMG-CoA) reductase activity, was also lowered in the doxazosin-treated hamsters. After norepinephrine administration to cholesterol-fed hamsters, atenolol increased (+8%) and doxazosin decreased (-35%) plasma triglycerides. Plasma cholesterol levels and hepatic cholesterol synthesis were no longer significantly affected by doxazosin. In norepinephrine-treated animals, adipose tissue lipoprotein lipase activity was enhanced (+30%) by doxazosin. Hepatic lipase activity in plasma and liver, which was lowered by norepinephrine, was increased by doxazosin. In hamsters not treated with norepinephrine, adrenoceptor blockers had no effect on plasma insulin or thyroid hormone, but with norepinephrine, levels of both insulin and thyroid hormone were increased by doxazosin. These data indicate that selective alpha 1-inhibition with doxazosin may interfere with lipid metabolism at several regulatory sites. The effects depend to a large extent on nutritional and hormonal status. Doxazosin might exert these effects partly via influences on other hormones.

Biochemical indicators of fatness in meat-type chickens: lack of correlation between lipoprotein lipase activity in post-heparin plasma and body fat.

1. Possible relationships between fatness and lipoprotein lipase activity in adipose tissue and plasma from heparinised birds were examined in 7-week-old male and female broilers. 2. Total lipoprotein lipase activity in abdominal fat was significantly correlated (r = 0.5) with fat pad weight, but there was no correlation between specific activity of the enzyme and fat pad weight. 3. Lipoprotein lipase activity in post-heparin plasma showed no correlation with either abdominal fat or total body fat content. 4. The results indicate that measurements of lipoprotein lipase activity in biopsy samples or in post-heparin plasma are of no value in predicting the fat content of live birds.

The Effect of Gari Feeding on the Changes in Lipid Levels and Lipoprotein Lipase Activity in Adipose Tissue

The Effect of Gari Feeding on the Changes in Lipid Levels and Lipoprotein Lipase Activity in Adipose Tissue

Increased lipoprotein lipase content in the adipose tissue of suckling and weaning obese Zucker rats.

The aim of this study was to determine whether the increase in lipoprotein lipase activity displayed by the adipose tissue of obese (fa/fa) rats as compared with that of lean (Fa/fa) rats could be ascribed to a change in the content or in the catalytic properties of the enzyme. The question was addressed in rats of two ages: in 7-day-old suckling and in 30-day-old post-weaning pups. Inguinal fat-pads were removed surgically (7 days of age) or after killing (30 days of age), and acetone-extract powders were prepared. The relative quantity of enzyme was assessed by immunotitration using an antiserum raised in goat against purified lipoprotein lipase from rat adipose tissue. The results indicate that increases in enzyme activity in obese animals were strictly paralleled by increases in the amount of enzyme in suckling as well as in post-weaning pups. Moreover, the apparent Km values of lipoprotein lipase for its substrate triacylglycerol were identical in the two genotypes. In conclusion, the genotype-mediated increase in lipoprotein lipase activity in adipose tissue of obese Zucker rats was fully accounted for by an increase in the content of the enzyme. In addition, this work documents the mechanism of the increase in lipoprotein lipase activity during weaning, which is mediated mainly through changes in the adipose-tissue enzyme content.

Basal and postprandial lipoprotein lipase activity in adipose tissue during caloric restriction and refeeding

The effect of a ten-day caloric restriction period and of subsequent refeeding on adipose tissue lipoprotein lipase (LPL) activity was studied in 14 moderately obese women. The enzyme assays were made from subcutaneous fat taken from three separate regions (gluteal, femoral, and abdominal) after overnight fasting and from one region also after a standard meal. There was a close correlation between the activities measured from the different subcutaneous sites. The caloric restriction was followed by a decrease of the basal LPL activity to one fifth of the value recorded during the isocaloric diet. However, the relative postprandial increase of LPL activity was greater during the low-calorie diet than during the isocaloric diet. During refeeding the basal LPL activity rose but remained at a lower level than before the caloric restriction. The postprandial LPL response was markedly exaggerated after ten days of refeeding (21% increase before dieting and 250% after refeeding). The changes of LPL during caloric restriction and subsequent refeeding were not correlated to plasma insulin levels. The mechanism of the exaggerated LPL response to meal during refeeding remains obscure.

Multiple effects of tumor necrosis factor on lipoprotein lipase in vivo.

A single dose of recombinant murine tumor necrosis factor (TNF) suppressed lipoprotein lipase activity in adipose tissue of fed rats, mice, and guinea pigs for 48 h, even though TNF itself is rapidly metabolized in vivo. Immunoprecipitation of [35S]lipoprotein lipase from fat pads pulse-labeled with [35S]methionine showed a decrease in relative synthesis of the enzyme, which correlated to the decrease in activity. There was no decrease in general protein synthesis and no change in distribution of the enzyme between adipocytes and extracellular locations in the tissue. This is in contrast to fasting in which case there is redistribution of the enzyme within the tissue, decrease in general protein synthesis, but no change in relative synthesis of lipoprotein lipase. TNF did not decrease lipoprotein lipase activity in any tissue other than the adipose but increased the activity in several cases, most markedly in the liver. No [35S]methionine was incorporated into lipoprotein lipase by liver slices from normal or TNF-treated animals. Thus, the increased activity can not be ascribed to enhanced hepatic synthesis of the enzyme. There was an increase in lipoprotein lipase activity in plasma, which correlated to the increase in liver. Thus, TNF suppresses lipoprotein lipase synthesis in adipocytes, but not in other tissues, and has some as yet undefined effect on lipoprotein lipase turnover in extrahepatic tissues, which results in increased transport of active lipase through plasma to the liver.