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PubMed1982

Immunological studies on bovine milk lipoprotein lipase. Effects of Fab fragments on enzyme activity.

Rabbit antiserum was prepared against purified bovine mild lipoprotein lipase. Immunoelectrophoresis of lipoprotein lipase gave a single precipitin line against the antibody which was coincident with enzyme activity. The gamma-globulin fraction inhibited heparin-releasable lipoprotein lipase activity of bovine arterial intima, heart muscle and adipose tissue. The antibody also inhibited the lipoprotein lipase activity from adipose tissue of human and pig, but not that of rat and dog. Fab fragments were prepared by papain digestion of the gamma-globulin fraction. Fab fragments inhibited the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine vesicles and trioleoylglycerol emulsions to the same extent. The Fab fragments also inhibited the lipolysis of human plasma very low density lipoproteins. The change of the kinetic parameters for the lipoprotein lipase-catalyzed hydrolysis of trioleoylglycerol by the Fab fragments was accompanied with a 3-fold increase in Km and a 10-fold decrease in Vmax. Preincubation of lipoprotein lipase with apolipoprotein C-II, the activator protein for lipoprotein lipase, did not prevent inhibition of enzyme activity by the Fab fragments. However, preincubation with dipalmitoylphosphatidylcholine-emulsified trioleoylglycerol or Triton X-100-emulsified trioleoylglycerol had a protective effect (remaining activity 7.0 or 25.8%, respectively, compared to 1.0 or 0.4% with no preincubation). The addition of both apolipoprotein C-II and substrate prior to the incubation with the Fab fragments was associated with an increased protective effect against inhibition of enzyme activity; remaining activity with dipalmitoylphosphatidylcholine-emulsified trioleoylglycerol was 40.6% and with Triton X-100-emulsified trioleoylglycerol, 45.4%. Human plasma very low density lipoproteins also protected against the inhibition of enzyme activity by the Fab fragments. These immunological studies suggest that the interaction of lipoprotein lipase with apolipoprotein C-II in the presence of lipids is associated with a conformational change in the structure of the enzyme such that the Fab fragments are less inhibitory. The consequence of a conformational change in lipoprotein lipase may be to facilitate the formation of an enzyme-triacylglycerol complex so as to enhance the rate of the lipoprotein lipase-catalyzed turnover of substrate to products.

Animals↗

PubMed1997

Lipoprotein lipase (EC 3.1.1.34) targeting of lipoproteins to receptors.

Summarizing all available data on the role of lipases in targeting lipoproteins to their receptors, we propose the following model: TRL after hydrolysis by LPL have apo E exposed on their surface and might contain one or more molecules of LPL. Both 'apolipoproteins' direct the particles to the cell surface by high-affinity binding to cellular proteoglycans. HL, bound to the surface of hepatocytes can further hydrolyse the particles and together with apo E and LPL mediate the binding to cellular receptors. The most important receptors recognizing these remnants are LRP and VLDLR. The LRP seems to be mainly responsible for the hepatic uptake of remnant lipoproteins, while the VLDLR, mainly located in adipose tissue and muscle, might target the lipoproteins to these tissues for fatty acid delivery.

Humans↗

PubMedDate not supplied

[Lipoprotein lipase fractionation of very low density serum lipoproteins from healthy subjects and persons afflicted with atherosclerosis].

In vitro experiments showed that blood sera of the patients with atherosclerosis contained rather often the fraction of very low density lipoproteins (VLDL) with sf 100-400 S, which were cleaved by the lipoprotein lipase at the decreased rate as compared with that of normal people. The decrease in cleavage of the VLDL fraction was usually observed in patients with the increased concentration of the lipoprotein fraction in blood sera. These data suggest that separate constituents occurring in the VLDL fraction (sf 100-400 S) may be nonuniformly increased in hyperlipoproteinemia.

Adult↗

PubMed2002

Diurnal variation in lipoprotein lipase activity.

BACKGROUND: We investigated whether variations in lipoprotein lipase activity, a key post-prandial enzyme involved in the removal of circulating dietary triglycerides, could contribute to the previously described nocturnal lipid intolerance. METHODS: We studied lipoprotein lipase activity in 12 healthy volunteers (five women, seven men) at 11:30 h and 23:30 h on two separate occasions. Subjects consumed a high-fat mixed meal at 07:30 h for the morning study or 19:30 h for the evening study. Then, after a 4-h fast, subjects were given an intravenous bolus of 7,500 U heparin. Blood samples were collected before and 15 min after heparin administration for measurement of lipoprotein lipase, hepatic lipase, triglycerides and non-esterified fatty acids concentrations. RESULTS: Post-prandial post-heparin lipoprotein lipase activity was greater in the morning than in the evening (16.5 +/- 1.4 versus 14.4 +/- 1.0 micromol oleate/mL/h; P< 0.05). Post-prandial post-heparin hepatic lipase activity was also greater in the morning than in the evening (8.7 +/- 1.5 versus 81 +/- 1.6 micromol oleate/mL/h; P= 0.002). There were no other significant diurnal differences. CONCLUSION: We report a diurnal variation in post-prandial lipoprotein lipase activity. This is consistent with the notion that decreased nocturnal insulin sensitivity extends to insulin's actions on lipoprotein lipase and provides a possible explanation for nocturnal lipid intolerance.

Adult↗

PubMed2006

Haplotypes in the lipoprotein lipase gene influence high-density lipoprotein cholesterol response to statin therapy and progression of atherosclerosis in coronary artery bypass grafts.

Lipoprotein lipase (LPL) hydrolyzes circulating triglycerides (TGs). We previously showed that 3'-end haplotypes in the LPL gene influence atherosclerosis and insulin resistance. This study asked whether these LPL haplotypes influence response to lipid-lowering therapy among 829 subjects from the Post-Coronary Artery Bypass Graft trial. Lipid profiles were obtained at baseline and 4-5 years after treatment with lovastatin. Haplotypes were based on 12 SNPs. The fourth most frequent haplotype, 12-4, was associated with a decreased increment in high-density lipoprotein-cholesterol (HDL-C) following treatment. Haplotypes 12-6, 12-7 and 12-8 were each associated with increased HDL-C response to therapy, and haplotype 12-2 with decreased TG response. The most common haplotype, 12-1, was protective against graft worsening or occlusion. Haplotype 12-4 reduced HDL-C response to lovastatin, possibly consistent with our prior observations of this haplotype as predisposing to coronary artery disease. LPL may influence atherosclerosis risk through pleiotropic effects on each aspect of the metabolic syndrome.

Adult↗

PubMedDate not supplied

Enhanced lipoprotein lipase secretion from human monocyte-derived macrophages caused by hypertriglyceridemic very low density lipoproteins.

We studied the effects of very low density lipoprotein (VDL) obtained from hypertriglyceridemic subjects on the secretion of lipoprotein lipase and lipid accumulation in human monocyte-derived macrophages. The incubation of macrophages with VLDL obtained from different subjects caused different effects on the secretion of lipoprotein lipase (6.8 to 137.7 nM free fatty acid/min/mg cell protein) and triglyceride accumulation (184 to 507 micrograms/mg cell protein) in human monocyte-derived macrophages. VLDL from subjects with marked hypertriglyceridemia (approximately 1000 mg/dl) had a fourfold greater effect on lipoprotein lipase activity and a twofold greater effect on cellular triglyceride accumulation when compared with the effects of VLDL from normolipidemic subjects. Both lipoprotein lipase activity and triglyceride accumulation correlated positively with plasma VLDL triglyceride levels (r = 0.50 and 0.45, respectively, p less than 0.05). From these data, we suggest that the activity of lipoprotein lipase secreted from macrophages incubated with VLDL was dependent on triglyceride concentrations, and that the secretion of lipoprotein lipase enhanced by hypertriglyceridemic VLDL was closely related to the intracellular accumulation of triglyceride.

Cell Line↗

PubMed2002

Insulin sensitivity is impaired in heterozygous carriers of lipoprotein lipase deficiency.

AIMS/HYPOTHESIS: Several studies have investigated the lipoprotein phenotype in heterozygous carriers of a defective lipoprotein lipase allele. We studied whether heterozygosity for lipoprotein lipase deficiency also affects glucose metabolism beyond its effect on plasma lipids. METHODS: To address this question 85 heterozygous carriers of either a missense mutation (Gly188Glu) or a splice site mutation (C-->A in position -3 at the acceptor splice site of intron 6) in the LPL gene which both result in a catalytically inactive product were compared with 108 unaffected subjects from the same families. RESULTS: Carriers for one of these mutations had higher fasting insulin levels but only a trend towards increased fasting blood glucose concentrations could be detected. HOMA index values were significantly higher in carriers than in non-carriers. Furthermore, in carriers, a significantly higher BMI and a trend towards higher systolic and diastolic blood pressure were observed. Carriers also had significantly higher fasting triglycerides, lower HDL cholesterol, and lipoprotein lipase particles of smaller size, confirming previous reports. Among carriers, subjects with one rare allele of the SstI polymorphism in the apo CIII gene had significantly higher plasma triglyceride levels than those with two common SstI alleles. This difference could not be observed in non-carriers of a mutant lipoprotein-lipase allele. The mean intima media thickness of the carotid arteries was slightly, but not significantly higher in carriers when compared with non-carriers. CONCLUSION/INTERPRETATION: This study shows that carrier status of one defective lipoprotein-lipase allele is associated with impaired insulin sensitivity, an atherogenic lipoprotein profile and other characteristics of the metabolic syndrome, which are risk factors for atherosclerotic vascular disease. A higher incidence of atherosclerotic vascular disease, however, could not be firmly established in carriers of this study population.

Adipose Tissue↗

PubMed2004

Alteration in lipoprotein lipase activity bound to triglyceride-rich lipoproteins in the postprandial state in type 2 diabetes.

Postprandial lipid metabolism is largely dependent upon lipoprotein lipase (LPL), which hydrolyses triglycerides (TGs). The time course of LPL activity in the postprandial state following a single meal has never been studied, because its determination required heparin injection. Recently, we have shown that LPL activity could be accurately measured in nonheparinized VLDL using a new assay aiming to determine the LPL-dependent VLDL-TG hydrolysis. Based on the same principle, we used in this study TG-rich lipoprotein (TRL)-bound LPL-dependent TRL-TG hydrolysis (LTTH) to compare the time course of LPL activity of 10 type 2 diabetics to that of 10 controls, following the ingestion of a lipid-rich meal. The peak TG concentration, reached after 4 h, was 67% higher in diabetics than in controls (P < 0.005). Fasting LTTHs were 91.3 +/- 15.6 in controls versus 70.1 +/- 4.8 nmol NEFA/ml/h in diabetics (P < 0.001). LTTH was increased 2 h postprandially by 190% in controls and by only 89% in diabetics, resulting in a 35% lowering of the LTTH area under the curve in diabetics. Postprandial LTTH was inversely correlated with TG or remnant concentrations in controls but not in diabetics, and with insulin resistance in both groups. These data show that TRL-bound LPL activity increases in the postprandial state and is strongly reduced in type 2 diabetes, contributing to postprandial hypertriglyceridemia.

Apolipoprotein C-II↗

PubMed2000

Endogenously produced glycosaminoglycans affecting the release of lipoprotein lipase from macrophages and the interaction with lipoproteins.

Macrophages are intimately involved in the pathogenesis of atherosclerotic diseases. A key feature of this process is their uptake of various lipoproteins and subsequent transformation to foam cells. Since lipoprotein lipase (LPL) is believed to play a role in foam cell formation, we investigated if endogenously produced proteoglycans (PGs) affect the release of this enzyme from macrophages. The human leukaemic cell line THP-1 which differentiates into macrophages by treatment with phorbol ester (phorbol 12-myristate 13-acetate) served as a model. The differentiation of THP-1 macrophages promoted the release of PGs into the cell medium which caused the detachment of LPL activity from the cell surface, and prevented LPL re-uptake and inactivation. These PGs were mainly composed of chondroitin sulfate type and exerted a heparin-like effect on LPL release. LPL is known to increase the cell association of lipoproteins by the well known bridging function. Exogenous bovine LPL at a concentration of 1 microg/ml enhanced low density lipoprotein (LDL)-binding 10-fold. Endogenously produced PGs reduced LPL-mediated binding of LDL. It is proposed that the differentiation-dependent increase in the release of PGs interferes with binding of LPL and reduces lipoprotein-binding to macrophages.

Arteriosclerosis↗

PubMed1994

Parathyroid hormone is not an inhibitor of lipoprotein lipase activity.

The reduced lipoprotein lipase (LPL) activities in uraemia are reflected by increased serum triglyceride concentrations and reduced HDL cholesterol concentrations. Both hyperparathyroidism and circulating inhibitor(s) of LPL have been associated with the disturbances of lipid metabolism in uraemia. The aim of the present study was to investigate if parathyroid hormone (PTH) had an inhibitory effect on LPL activity. Plasma post-heparin LPL activities, plasma LPL inhibitory activities, serum PTHintact and serum PTHC-terminal concentrations were analysed in 20 patients on haemodialysis and 20 healthy controls. The effects of purified, human PTHintact and a carboxyterminal fragment of PTH (PTH39-84) on LPL activities in post-heparin plasma from healthy individuals and on the enzyme activity of purified, bovine milk LPL, activated with apolipoprotein CII, were studied. Patients had significantly higher plasma LPL inhibitory activities than controls, but there was no correlation between plasma LPL inhibitory activities and serum PTH concentrations. Neither PTHintact nor PTH39-84 had a significant effect on LPL activities in vitro. Thus there was no evidence of a direct inhibition of LPL activity by PTH under the present in-vivo or in-vitro conditions.

Adult↗

PubMed1978

Increase of the lipoprotein-lipase activity in human skeletal muscle during clofibrate administration.

Lipoprotein-lipase activity was determined in tissue from the skeletal muscle of the leg and the subcutaneous adipose tissue of the abdomen in fourteen patients before and after 1 month of clofibrate administration. The concentrations of serum triglycerides decreased by, on the average, 37% in a group of thirteen patients which mainly consisted of subjects with type-IV hyperlipoproteinaemia. Clofibrate administration was associated with an average increase of the skeletal muscle-tissue lipoprotein-lipase activity of 50% (P less than 0.005). There was a significant correlation between the percentage changes in skeletal muscle-tissue lipoprotein-lipase activity and those of the triglycerides concentrations and the K2-values in an intravenous fat tolerance test during clofibrate treatment. Adipose-tissue lipoprotein-lipase activity did not change significantly. One patient with type-I hyperlipoproteinaemia had very low values of skeletal muscle-tissue lipoprotein-lipase activity and moderately low adipose-tissue lipoprotein-lipase activity. In this patient, neither the tissue lipoprotein-lipase activity nor the triglycerides concentration changed during clofibrate therapy. Fasting serum insulin concentrations decreased significantly during clofibrate administration and the percentage decrease was significantly correlated to the percentage increase of skeletal-muscle lipoprotein-lipase activity. It is suggested that the lowering of insulin levels is a possible mechanism through which glucagon activity is enhanced and this may increase skeletal muscle-tissue lipoprotein-lipase activity.

Adipose Tissue↗

PubMed1990

Smoking depresses adipose lipoprotein lipase response to oral glucose.

Adipose tissue lipoprotein lipase was studied in smokers (n = 17) aged 18-47 years and compared with enzyme activity in non-smokers of comparable age (n = 8) and a second time in some of the subjects 5-9 weeks after cessation of smoking (n = 7). Serum cotinine levels served to validate the smoking status of the subjects. Fasting enzyme activity was similar in smokers and non-smokers, when expressed per 10(6) cells, but was significantly increased when normalized for cell size. When lipoprotein lipase was determined in the same individual 4 h after an oral glucose load, a significant decrease (P less than 0.002) occurred in the smokers, while enzyme activity rose in the nonsmokers (P less than 0.02). A tendency for enzyme activity to rise after oral glucose was seen in ex-smokers, which did not reach statistical significance. Even though the mean serum insulin and glucose levels did not differ in the three groups of subjects, the per cent decrease in lipoprotein lipase after oral glucose in smokers was negatively correlated with insulin release into serum in the same subject, i.e., the greater the insulin release, the less the decrease in lipoprotein lipase activity. We would like to propose that the lower body weight in smokers is related to the paradoxical response of adipose tissue lipoprotein lipase to carbohydrate and that the reversal of this behaviour contributes to the weight gain often observed after cessation of smoking.

Adipose Tissue↗

PubMed1999

Epinephrine stimulates human muscle lipoprotein lipase activity in vivo.

Lipoprotein lipase (LPL) is involved in lipoprotein metabolism and nutrient partitioning in both adipose tissue and skeletal muscle, and LPL activity is regulated by various hormones and the nutritional state. However, the action of catecholamines has not been thoroughly investigated in humans. Therefore, the effects of exogenous epinephrine on skeletal muscle LPL (SM-LPL) activity and whole-body lipid oxidation were studied. Muscle biopsies were obtained from eight healthy subjects before, during, and after epinephrine infusion. Somatostatin was infused to suppress endogenous insulin production and insulin was infused at a constant rate to maintain basal insulin levels throughout the study. After an equilibrium period (120 minutes), epinephrine (0.05 microg/kg/min) was infused for another 120 minutes. Epinephrine stimulated SM-LPL activity by 21.8%+/-6.8% above basal levels from 1.44+/-0.25 to 1.69+/-0.28 micromol free fatty acid (FFA)/h/g muscle (P<.02), increased plasma FFA 270% from 0.147 to 0.544 mmol/L (P<.05), and increased lipid oxidation 45% from 4.37 to 6.36 mg/kg/min (P<.05). The increase in SM-LPL activity was positively correlated with the increase in whole-body lipid oxidation (R=.75, P<.05). Finally, lipid oxidation and SM-LPL activity were negatively correlated with whole-body glucose oxidation. Overall, the results demonstrate that epinephrine is able to stimulate SM-LPL activity in humans, and thus may have opposite effects on adipose tissue and SM-LPL activity.

Adrenergic alpha-Agonists↗

PubMed1989

Lipoprotein lipase in myocytes and capillary endothelium of heart: immunocytochemical study.

Lipoprotein lipase was immunolocalized by electron microscopy in hearts of young mice; 78% of lipoprotein lipase was in myocytes, 3-6% in extracellular space, and 18% in capillary endothelium. Lipoprotein lipase in myocytes was located primarily in sarcoplasmic reticulum, Golgi sacs, and transport vesicles and also in secretory vesicles at the cell periphery. Lipoprotein lipase in extracellular space was present near the orifice of secretory vesicles of myocytes and in narrow zones spanning the space between myocytes and capillary endothelium. The lowest concentration of lipase associated with endothelial cells was at the basal plasma membrane, whereas the highest concentration was at the surface of luminal projections. Lipoprotein lipase was associated with chylomicrons at the capillary surface but not with chylomicron remnants. Fasting mice for 48 h increased, in heart, lipoprotein lipase activity by 120% and immunolocalized lipase by 270%. The greatest increase (5-fold) occurred at the surface of intraluminal endothelial projections. The findings indicate that lipoprotein lipase in heart is synthesized by myocytes, transferred across extracellular space along cell surfaces and across endothelial cells via vesicles or intracellular channels, and concentrated at the surface of luminal projections of endothelium where the enzyme hydrolyzes triacylglycerol of chylomicrons and very low-density lipoproteins.

Animals↗

PubMedDate not supplied

Roles of lipoprotein lipase and hepatic triglyceride lipase in the catabolism in vivo of triglyceride-rich lipoproteins.

To define the roles, in vivo, of hepatic triglyceride lipase and lipoprotein lipase in the catabolism of triglyceride-rich lipoproteins, we investigated the relationship between the activities of the above enzymes in postheparin plasma and the fractional removal rates of very low density lipoproteins (VLDL) and VLDL remnant particles. In 22 patients, the fractional removal rates of VLDL and VLDL-remnant particles were determined from analyses of the disappearance of radioiodinated Sf 60-400 and Sf 12-60 lipoprotein B apoprotein. The maximal activities of hepatic triglyceride lipase and lipoprotein lipase were determined in plasma samples drawn 2-60 minutes after heparin injection (60 U/kg). A positive correlation was observed between the fractional removal rate of VLDL and postheparin plasma lipoprotein lipase activity (r = 0.65). When all 22 patients were considered together, no relationship was demonstrable between remnant fractional removal and postheparin plasma lipoprotein lipase activity. However, humans may be subdivided with respect to the way in which they catabolize remnants. In some, all remnant may be catabolized to form LDL. In others, some of the remnant may also be directly removed from the circulation. Those subjects in whom previous studies indicate that all remnant is converted to LDL demonstrated a positive correlation between remnant fractional removal rate and postheparin plasma lipoprotein lipase activity (n = 8, r - 0.83). No correlations between postheparin plasma hepatic triglyceride lipase activity and any of the fractional removal rates were found. These data are consistent with the following: 1) lipoprotein lipase plays a key regulatory role in the catabolism of triglyceride-rich lipoproteins; 2) this role applies only to those catabolic involving the formation of particles of higher density VLDL remnants and low density lipoprotein; and 3) hepatic triglyceride lipase plays no rate-limiting role in the catabolism of VLDL or VLDL-remnant particles.

Adult↗

PubMed1975

Human adipose tissue lipoprotein lipase: comparison of assay methods and expressions of activity.

There was a positive correlation in normal man between heparin releasable lipoprotein lipase and lipoprotein lipase of ammonium hydroxide homongenate of acetoneether powder in adipose tissue. Heparin releasable as lipoprotein lipase activity was about twice as high as the enzymatic activity in acetone powder, even though 40-70% of the original activity remained in the tissue after incubation with heparin. This might indicate that activation of the enzyme is associated with its release by heparin from tissue. The lipoprotein lipase activity per unit weight and per fat cell were affected differently by obesity: In obese subjects lipoprotein lipase per unit weight was propotionally lower than the activity per fat cell. The expression of activity per fat cell appears to avoid the effect of obesity, and hence increased fat cell size, on values obtained.

Acetone↗

PubMed1980

Postprandial adipose tissue lipoprotein lipase activity in primary hypertriglyceridemia.

The fasting activity of adipose tissue lipoprotein lipase has been previously reported to be either normal or reduced in subjects with a primary form of hypertriglyceridemia. The postprandial activity of adipose tissue lipoprotein lipase has not been previously reported in these subjects. In subjects with primary hypertriglyceridemia the fasting lipoprotein lipase activity eluted from pieces of adipose tissue by heparin and the enzyme activity present in extracts of acetone--ether tissue powders were similar to the level of enzyme activity found in normal subjects. There also was no difference in the postprandial adipose tissue heparin-elutable lipoprotein lipase activity between these two groups when measured after high carbohydrate feeding. When the subjects with primary hypertriglyceridemia were further subdivided by genetic diagnosis, there was no difference in the level of adipose tissue lipoprotein lipase of subjects with familial hypertriglyceridemia, familial combined hyperlipidemia, or in those in whom no specific genetic diagnosis could be made. The change in lipoprotein lipase activity after feeding was inversely related to the fasting enzyme level in both the normal subjects (r = -0.58, p less than 0.05, n = 12) and the hypertriglyceridemic subjects (r = -0.92, p less than 0.01, n = 11). In the normal subjects, the plasma triglyceride response to feeding correlated inversely with the postprandial change in lipoprotein lipase activity (r = -0.76, p less than 0.02, n = 12). Adipose tissue lipoprotein lipase activity in patients with primary lipoprotein lipase deficiency was markedly reduced in the fasting state and remained essentially zero after feeding. This suggests that a functional role exists for the enzyme activity as measured.

Adipose Tissue↗

PubMedDate not supplied

The effect of acute and chronic administration of nicotine on lipoprotein lipase activity.

Nicotine was injected intraperitoneally to rats and 2 h later lipoprotein lipase was determined in isolated perfused hearts. There was a significant increase in heparin releasable lipoprotein lipase activity which represents the functional pool without increase in total enzyme activity. When 1 microliter/h of a solution of nicotine (120 mg/ml) was delivered for 3 days from subcutaneously implanted miniosmotic pumps, total lipoprotein lipase activity in the heart increased 1.5-3.0 fold. Endogenous lipoprotein lipase activity in plasma doubled and there was a significant fall in plasma triglyceride levels. The effect of nicotine on heart lipoprotein lipase activity was evident also after 6 days of continuous delivery and was accompanied by a fall in adipose tissue lipoprotein lipase activity. No effect was seen when the dose of nicotine was halved. A positive correlation was seen between plasma nicotine levels and heart lipoprotein lipase activity, while adipose tissue lipoprotein lipase correlated negatively with plasma nicotine levels. Chronic administration of nicotine was accompanied by either weight loss or diminished weight gain. It is concluded that in the rat the acute effect of nicotine on the shift of lipoprotein lipase to the functional pool could be related to enhanced beta-adrenergic stimulation. The chronic effect of nicotine could have been mediated by the loss in body weight, due to reduced caloric intake.

Animals↗