Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LIPOPROTEIN LIPASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 163 records · Page 9Linked to original sources
PubMedDate not supplied

Increased removal of beta-very low density lipoproteins after ethinyl estradiol is associated with increased mRNA levels for hepatic lipase, lipoprotein lipase, and the low density lipoprotein receptor in Watanabe heritable hyperlipidemic rabbits.

The mechanism by which ethinyl estradiol (EE) decreases the concentration of lipids in the d less than 1.019 g/ml fraction (beta-very low density lipoprotein [beta-VLDL]) of homozygous Watanabe heritable hyperlipidemic (WHHL) rabbits was studied. Treatment with EE increased the activity of hepatic lipase (HL) twofold to threefold in postheparin plasma and in liver biopsies. Postheparin plasma and adipose tissue lipoprotein lipase (LPL) activities were also increased twofold to fourfold after EE. The effects of EE on HL and LPL activities were associated with a threefold to sixfold elevation in liver HL mRNA and a fourfold elevation in adipose tissue LPL mRNA steady-state levels, pointing to an effect of EE on HL and LPL gene transcription. EE also increased liver low density lipoprotein (LDL) receptor mRNA levels threefold to fivefold. These results suggest a concerted action of LPL, HL, and the LDL receptor in the removal of beta-VLDL in homozygous WHHL rabbits with a defective LDL receptor. In addition, the content of apolipoprotein E in the d less than 1.019 g/ml fraction changed toward normal after EE. Because the remaining particles contained apolipoprotein B-100 almost exclusively, it is likely that apolipoprotein E-containing beta-VLDLs are preferentially removed. This may be the result of the increased activity of LPL and HL influencing the conformation of apolipoprotein E on the beta-VLDL particle in such a way that it is directly removed from the circulation, possibly by the induced LDL receptor.

Adipose Tissue↗
PubMed1990

Inhibition of lipoprotein lipase activity by high density lipoprotein & apolipoproteins C, E & A in rhesus monkeys.

Experiments were conducted to study the effects of high density lipoprotein (HDL) and apolipoproteins C, E, and A on lipoprotein lipase activity in rhesus monkeys. The lipoprotein lipase activity was inhibited up to 32 +/- 6 per cent by monkey HDL. This inhibition was considerably decreased (2 +/- 0.02%) by using apolipoprotein-poor HDL. Apolipoproteins C and E inhibited the hydrolysis of activated intralipid by monkey lipoprotein lipase to a maximum of 83 +/- 7 and 57 +/- 5 per cent respectively. Apolipoprotein A produced little inhibition of lipoprotein lipase activity. The results of these studies demonstrate that HDL and apolipoproteins compete with the substrate for the binding to lipoprotein lipase in rhesus monkeys.

Animals↗
PubMed1990

Lipoprotein lipase deficiency resulting from a nonsense mutation in exon 3 of the lipoprotein lipase gene.

In DNA from a male patient of German and Polish ancestry who has lipoprotein lipase deficiency, sequencing of all nine exons and intron-exon boundaries corresponding to the coding region of the lipoprotein lipase gene detected a C----T transition leading to the substitution of a stop signal for the codon that normally determines a glutamine at position 106 of the mature enzyme. Hybridization with allele-specific oligonucleotides at this position established that the patient was homozygous for this mutation. This mutation must lead to the synthesis of a sharply truncated protein, accounting for the enzymatic deficiency noted in the patient.

Base Sequence↗
PubMed1986

Effect of combined lipase deficiency (cld/cld) on hepatic and lipoprotein lipase activities in liver and plasma of newborn mice.

Combined lipase deficiency (cld/cld) is a recessive mutation in mice which results in massive hyperlipemia and death within 3 days after birth. We studied the effect of this deficiency on lipolytic activities in liver and in pre- and postheparin plasma of mice less than 2 days old. Anti-hepatic lipase serum inhibited more than 85% of the lipolytic activity in liver and plasma of normal newborn mice when assayed in high-salt medium, validating the use of this medium for measuring hepatic lipase activity in mice. Anti-lipoprotein lipase serum, in contrast, inhibited only two-thirds of the lipolytic activity in liver and plasma when assayed in serum low-salt medium, and anti-hepatic lipase serum inhibited the rest. This indicates that assay with serum low-salt medium alone is not specific for lipoprotein lipase activity in mice. Therefore, immunoinhibition was used, as needed, for measuring lipoprotein lipase activity. The livers of unaffected newborn mice contained high levels of both hepatic and lipoprotein lipase activities, 228 and 187 mU/g, respectively. The plasma of unaffected mice contained a high level of hepatic lipase activity, 244 mU/ml, but practically no lipoprotein lipase activity. Heparin injected intraperitoneally increased plasma lipoprotein lipase activity to 152 mU/ml, but had no effect on plasma hepatic lipase activity, in unaffected mice. Hepatic lipase activity was virtually absent from both liver and plasma of cld/cld mice. Lipoprotein lipase activity was present in the liver at a surprisingly high level, 40% of that in normals, but was barely detectable in plasma. Heparin injection increased plasma lipoprotein lipase activity in cld/cld mice, but the increment was less than 10% of that in unaffected mice. Heparin had no significant effect on plasma hepatic lipase activity in defective mice. These findings confirm preliminary observations that hepatic lipase activity in liver and plasma and lipoprotein lipase activity in plasma are markedly reduced in combined lipase deficiency. The unexpected high level of lipoprotein lipase activity in liver of cld/cld mice suggests that regulation of lipoprotein lipase activity in liver of neonatal mice is different from that in other tissues.

Animals↗
PubMed1995

Lipase evolution: trout, Xenopus and chicken have lipoprotein lipase and apolipoprotein C-II-like activity but lack hepatic lipase-like activity.

Lipoprotein lipase and hepatic lipase are members of a gene family which also contains pancreatic lipase. High activity of lipoprotein lipase is present in extrahepatic tissues in all mammals studied and also in birds. The activity of hepatic lipase varies more. To investigate the evolutionary relationship, lipase activities in tissues of some lower vertebrates were measured. In fish and in frog, low activities with the characteristics of lipoprotein lipase were found. Serum from frog and from fish, and plasma from chicken, stimulated lipoprotein lipase in vitro, indicating that these species contain analogues to human apolipoprotein C-II. Little or no hepatic lipase-like activity was found in post-heparin plasma or in liver homogenates of chickens. In fish liver, lipase activity with an apparent heparin affinity similar to, or even higher than lipoprotein lipase was found. Frog liver contained a small amount of lipase activity with high heparin affinity. This activity was inhibited both by apolipoprotein C-II and by 1 M NaCl. It is not clear whether the low lipase activities in livers from fish and from frog are variants of hepatic lipase. Since lipoprotein lipase and apolipoprotein C-II are already present in fish, this lipase probably evolved before hepatic lipase.

Animals↗
PubMed2005

Normal triglyceride levels despite insulin resistance in African Americans: role of lipoprotein lipase.

Abstract Lipoprotein lipase (LPL), the enzyme responsible for hydrolyzing triglyceride (TG) in plasma lipoproteins, is a key regulator of plasma TG levels. In Caucasians, postheparin-LPL (PH-LPL) activity is impaired in the presence of insulin resistance and leads to elevated TG levels. However, African Americans are often both insulin-resistant and normotriglyceridemic. But in African Americans, the effect of insulin resistance on PH-LPL activity has not been studied. In African Americans, if insulin resistance is not associated with a decrease in PH-LPL activity, this could account for the simultaneous presence of insulin resistance and normotriglyceridemia. Therefore, our goal was to determine in African Americans the relationship between insulin resistance and PH-LPL activity. In a cross-sectional study of 107 nondiabetic African Americans (57 men and 50 women; age mean +/- SD, 35 +/- 8 years, range 22-50 years; body mass index 31.6 +/- 7.9 kg/m 2 , range 18.5-54.7 kg/m 2 ), fasting TG levels and PH-LPL activity were determined. Visceral adipose tissue was measured by abdominal computed tomographic scan. Insulin resistance was determined by the insulin sensitivity index ( S I ). Subjects were divided into tertiles by S I . The range of S I in each tertile was 12.75 to 3.99, 3.87 to 2.20, 2.06 to 0.17 mU . L -1 . min -1 . Insulin resistance was defined as being in the third tertile. TG levels in the men and women were 82.2 +/- 35.5 versus 56.4 +/- 30.1 mg/dL, P < .001. There were no sex difference in PH-LPL activity (8.9 +/- 2.5 vs 9.6 +/- 3.2 mmol/h per liter, P = .30) or S I (3.65 +/- 2.59 vs 3.23 +/- 1.89 L . mU -1 . min -1 , P = .49). Although 47% of the subjects were obese, only 4% of subjects had hypertriglyceridemia (TG > or =150 mg/dL). By 2 separate analyses, PH-LPL was a major determinant of TG levels. First, there was a significant inverse correlation between PH-LPL activity and TG levels (men: r = -0.46, P < .001; women: r = -0.28, P = .046). Second, in the multiple regression analysis with TG as the dependent variable and PH-LPL, age, sex, S I , and visceral adipose tissue as independent variables, adjusted R 2 was 54% and the effect of PH-LPL on TG levels was highly significant( P < .001). However, insulin resistance did not appear to influence PH-LPL activity. This is demonstrated in 3 ways: first, PH-LPL activity was not different in the S I tertiles (9.10 +/- 2.75, 9.52 +/- 2.91, 9.13 +/- 2.89 mmol/h per liter, P = .78); the correlation between PH-LPL and S I was not significant (men: r = 0.09, P = .51; women: r = -0.03, P = .78), and a multiple regression with PH-LPL as the dependent variable and age, S I , body mass index, and sex as independent variables, adjusted R 2 was <2% and the contribution of S I was not significant ( P = .53). Hence, in African Americans, increased PH-LPL activity is associated with a decrease in TG levels. The lack of an effect of insulin resistance on PH-LPL could allow LPL to clear TG even in the presence of insulin resistance and explain the coexistence of insulin resistance and normotriglyceridemia in African Americans.

Adipose Tissue↗
PubMed1991

[Structural characteristics of the human lipoprotein lipase gene].

Lipoprotein lipase plays a major role in the metabolism of circulating triglyceride-rich lipoproteins. In relation with this study, the fundamental results concerning the structure of human LPL gene are first summarized. Sequencing of this gene enabled us to characterize an Alu sequence. Interest of these repetitive sequences is exposed.

Base Sequence↗
PubMed1979

Activation and inhibition of lipoprotein lipase. Studies with artificial lipoproteins.

Human plasma very low density apolipoproteins C-I, C-II and C-III were recombined in vitro with triolein. The lipid-protein complexes were analyzed by ultracentrifugal flotation, agarose gel electrophoresis, immunoelectrophoresis and electron microscopy. Maximal protein/triolein ratios for apoprotein C-I, C-II, C-III-1 and C-III-2 were 50, 45, 95 and 55 microgram/mg, respectively. Electron micrographs exhibited spherical particles with diameters ranging from 200--2000 A comparable to native VLDL and chylomicrons. On agarose gel electrophoresis these complexes showed alpha-mobility. Kinetics of triolein hydrolysis by purified human plasma lipoprotein lipase were studied using these artificial lipoprotein substrates with different apoprotein/triolein ratios. The reaction followed the Michaelis-Menten equation. With increasing amounts of apo C-II, the apparent Km decreased from 0.60 to 0.11 mM. Incubation of the substrate with either rabbit anti-apo C-II gamma-globulins or digestion with trypsin prior to hydrolysis reversed this lowering effect on apparent Km. V was not altered significantly. Increasing amounts of apo C-I, apo C-III-1 or apo C-III-2 without apo C-II caused inhibition of triolein hydrolysis. In the presence of apo C-II, however, similar kinetic parameters were obtained as described above.

Apolipoproteins↗
PubMed1997

Differential effects of streptozotocin-induced diabetes on cardiac lipoprotein lipase activity.

Lipoprotein lipase (LPL) is an endothelial-bound enzyme that is rate determining for the clearance of triacylglycerol-rich lipoproteins. Previous studies using rats with streptozotocin (STZ)-induced diabetes have reported inconsistent effects on cardiac LPL activity or immunoreactive protein. To examine the contribution of the severity and duration of diabetes on cellular and heparin-releasable cardiac LPL activity, Wistar rats were administered a high (100 mg/kg; D100) or moderate (55 mg/kg; D55) dose of STZ, and LPL activity was examined at various times after diabetes induction. Heparin perfusion of the isolated Langendorff control heart induced the release of LPL activity as an initial fast phase followed by a slow phase of release. With increasing age, the second phase of LPL release became more pronounced. Severe STZ-induced diabetes reduced heparin-releasable LPL activity by 1 week in the D100 rats. However, in D55 rat hearts, peak heparin-releasable LPL activity was higher than that in control animals at 2 and 12 weeks after STZ injection, with a complete absence of the delayed phase at 12 weeks. The elevated heparin-releasable LPL peak could not be explained by an enhanced LPL synthesis because both cellular and surface-bound LPL activities in myocytes from D55 rats were low, relative to control. Chronic (12-day) insulin treatment of D55 rats prevented the rise in heparin-releasable LDL and the reduction in cell-associated LPL activity. Moreover, acute (90-min) treatment of D55 rats with rapid-acting insulin also reduced the heparin-releasable LPL activity to normal levels, although it had no effect on the low cellular LPL activity. When the heparin-releasable LPL pool was allowed to recover for 1 h after removal of the enzyme, D55 rat hearts continued to demonstrate a higher peak LPL activity after a second heparin perfusion. These studies demonstrate that in moderate but not severe diabetes, there is an augmented peak heparin-releasable LPL activity. Whether or not this enhanced heparin-releasable LPL activity has a pathological role in the diabetic heart has yet to be determined.

Animals↗
PubMed1991

Effect of magnesium deficiency on post-heparin lipase activity and tissue lipoprotein lipase in the rat.

Previous studies have provided evidence that Mg deficiency affects lipid metabolism. The present experiments were designed to assess whether the hypertriglyceridemia associated with Mg deficiency was related to alterations in post-heparin lipase activity (PHLA). Mg-deficient and control diets were pair-fed to weanling Wistar rats for eight days and plasma lipoproteins were separated into various density classes by sequential preparative ultracentrifugation. Triglycerides were significantly increased in chylomicrons and in the very low density lipoprotein, low density lipoprotein and high density lipoprotein (HDL) fractions. Cholesterol and phospholipid levels were significantly lower in the HDL fraction. PHLA in deficient rat was substantially lower than in control rats. The inverse correlation between plasma triglyceride concentration and PHLA strongly suggests that hypertriglyceridemia is the result of defective lipolysis of plasma triglycerides in Mg-deficient rats. Further examination of the PHLA was carried out by salt-mediated inhibition of lipoprotein lipase (LPL) and by heparin sepharose affinity chromatography and purified rat LPL antiserum. The results indicate that hepatic lipase is significantly decreased in Mg-deficient rats but the low PHLA is due mainly to a decline in LPL. However, total LPL activity, that is, both the intracellular and the extracellular pools of LPL in adipose tissue, heart and diaphragm, were unaffected by Mg deficiency. The results suggest that the decrease of LPL activity in the plasma of Mg-deficient rats may be due to a selective decrease in the heparin-releasable pool of enzyme.

Adipose Tissue↗
PubMed1997

Relationship between lipoprotein lipase and high density lipoprotein cholesterol in mice: modulation by cholesteryl ester transfer protein and dietary status.

Plasma lipoprotein lipase (LPL) activity correlates with high density lipoprotein (HDL) cholesterol levels in humans. However, in several mouse models created either through transgenesis or targeted inactivation of LPL, no significant changes in HDL cholesterol values have been evident. One possible explanation for this species difference could be the absence of plasma cholesteryl ester transfer protein (CETP) activity in mice. To explore this possibility and further investigate interactions between LPL and CETP modulating HDL cholesterol levels in vivo, we examined the relationship between LPL activity and HDL levels in mice expressing the simian CETP transgene, compared with littermates not carrying the CETP gene. On a chow diet, increasing LPL activity was associated with a trend towards increased HDL levels (51 +/- 29 vs. 31 +/- 4 mg/dL highest vs. lowest tertiles of LPL activity, P = 0.07) in mice expressing CETP, while no such effects were seen in the absence of CETP (65 +/- 12 vs. 61 +/- 15 mg/ dL). Furthermore, in the presence of CETP, a significant positive correlation between LPL activity and HDL cholesterol was evident (r = 0.15, P = 0.006), while in the absence of CETP no such correlation was detected (r = 0.15, P = 0.36), highlighting the interactions between LPL and CETP in vivo. When mice were challenged with a high fat, high carbohydrate diet, strong correlations between LPL activity and HDL cholesterol were seen in both the presence (r = 0.45, P = 0.03) and absence (r = 0.73, P < 0.001) of CETP. Therefore, under altered metabolic contexts, such as those induced by dietary challenge, the relation between LPL activity and HDL cholesterol may also become evident. Here we have shown that both genetic and environmental factors may modulate the association between LPL activity and HDL cholesterol, and provide explanations for the absence of any changes in HDL values in mice either transgenic or with targeted disruption of the LPL gene.

Animals↗
PubMed1990

Cellular and secreted lipoprotein lipase revisited.

Lipoprotein lipase (LPL) of adipose cells is present only in membrane compartments, mainly in the Golgi apparatus. LPL is a typical secretory protein which appears to be active as a homodimer. The process of LPL synthesis and maturation requires multiple steps. LPL is synthesized in the endoplasmic reticulum as an inactive monomer of Mr 51,000; a high-mannose, inactive monomer of Mr 55,500 is then formed. An active homodimer form, bearing two complex oligosaccharide chains per monomer of Mr 58,000, forms in the Golgi apparatus. This mature form, present in secretory vesicles, can be secreted constitutively or after exposure to heparin. A model is proposed in which LPL is present in secretory vesicles in a potentially active, condensed, or "polymerized" form. This model, which applies to various LPL-containing tissues in different species - including human - would explain the "activation" of LPL.

Adipose Tissue↗
PubMed1989

A major insertion accounts for a significant proportion of mutations underlying human lipoprotein lipase deficiency.

Lipoprotein lipase (LPL; triacylglyceroprotein acylhydrolase, EC 3.1.1.34) is an important enzyme involved in triacylglycerol metabolism. Primary LPL deficiency is a genetic disorder that is usually manifested by a severe elevation in triacylglycerol levels. We have used a recently isolated LPL cDNA clone to study 15 probands from 11 families with this inherited disorder. Surprisingly, 7 of the probands from 4 families, of different ancestries, had a similar insertion in their LPL gene. In contrast to other human genetic disorders, where insertions are rare causes of mutation, this insertion accounts for a significant proportion of the alleles causing LPL deficiency. Detailed restriction mapping of the insertion revealed that it was unlikely to be a duplication of neighboring DNA and that it was not similar to the consensus sequence of human L1 repetitive elements. This suggests that there must be other mechanisms of insertional mutagenesis in human genetic disease besides transposition of mobile L1 repetitive elements.

Adult↗
PubMed1998

DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene.

Lipoprotein lipase plays a central role in lipid metabolism and the gene that encodes this enzyme (LPL) is a candidate susceptibility gene for cardiovascular disease. Here we report the complete sequence of a fraction of the LPL gene for 71 individuals (142 chromosomes) from three populations that may have different histories affecting the organization of the sequence variation. Eighty-eight sites in this 9.7 kb vary among individuals from these three populations. Of these, 79 were single nucleotide substitutions and 9 sites involved insertion-deletion variations. The average nucleotide diversity across the region was 0.2% (or on average 1 variable site every 500 bp). At 34 of these sites, the variation was found in only one of the populations, reflecting the differing population and mutational histories. If LPL is a typical human gene, the pattern of sequence variation that exists in introns as well as exons, even for the small number of samples considered here, will present challenges for the identification of sites, or combinations of sites, that influence variation in risk of disease in the population at large.

Base Sequence↗
PubMed1983

The comparative kinetics of soluble and heparin-Sepharose-immobilized bovine lipoprotein lipase.

While lipoprotein lipase (LPL) acts in vivo as an immobilized enzyme, its kinetics are commonly studied with soluble LPL (S-LPL). Hence kinetic parameters of S-LPL and heparin-Sepharose-immobilized LPL (B-LPL) were compared. A modified purification procedure for bovine milk, LPL gave a 56% yield of S-LPL, purified 7250-fold, and a specific activity of 27,000 mumol fatty acid/mg LPL/h when assayed with triolein (TG) emulsions in the presence of serum. The purified LPL also showed low but detectable esterase activity with p-nitrophenylacetate and p-nitrophenylbutyrate as substrates. Apolipoprotein C-II (C-II) had no effect on the esterase activity of LPL. Dixon plots of experiments with S-LPL indicated that heparin is a competitive inhibitor against both C-II and TG, and that the binding of either C-II or heparin to the enzyme is a mutually exclusive event. Similarly, the binding of TG and heparin to the enzyme is mutually exclusive. From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Comparative studies with B-LPL and S-LPL, using triolein as substrate and apolipoprotein C-II or serum as activator, indicated that S-LPL has a higher apparent Km and lower apparent Vmax than B-LPL. It is concluded that most of the LPL bound to heparin-Sepharose is probably inaccessible to substrate, hence a low Vmax. However, Km (C-II) and Km (TG) were higher for B-LPL due to the competitive inhibitory effect of heparin on LPL. Consistent with these kinetic analyses and with the use of human very low density lipoproteins (VLDL) as substrate, S-LPL, even in the presence of heparin, was found to have an apparent rate of lipolysis of VLDL approximately ninefold greater than B-LPL.

Animals↗
PubMed2004

Advanced glycation end products potentiate the stimulatory effect of glucose on macrophage lipoprotein lipase expression.

Lipoprotein lipase (LPL) secreted by macrophages in the arterial wall promotes atherosclerosis. We have shown that macrophages of patients with type 2 diabetes overproduce LPL and that metabolic factors, including glucose, stimulate macrophage LPL secretion. In this study, we determined the effect of advanced glycation end products (AGEs) on LPL expression by macrophages cultured in a high-glucose environment and the molecular mechanisms underlying this effect. Our results demonstrate that AGEs potentiate the stimulatory effect of high glucose on murine and human macrophage LPL gene expression and secretion. Induction of macrophage LPL mRNA levels by AGEs was identical to that elicited by physiologically relevant modified albumin and was inhibited by anti-AGE receptor as well as by antioxidants. Treatment of macrophages with AGEs resulted in protein kinase C (PKC) and mitogen-activated protein kinase (MAPK) activation. Inhibition of these kinases abolished the effect of AGEs on LPL mRNA levels. Finally, exposure of macrophages to AGEs increased the binding of nuclear proteins to the activated protein-1 consensus sequence of the LPL promoter. This effect was inhibited by PKC and MAPK inhibitors. These results demonstrate for the first time that AGEs potentiate the stimulatory effect of high glucose on macrophage LPL expression. This effect appears to involve oxidative stress and PKC/MAPK activation.

Animals↗
PubMed1994

[Molecular genetics and lipoprotein lipase deficiency].

Lipoprotein lipase (LPL) deficiency is the main cause of familial chylomicronemia, a disease characterised by high fasting plasma triglyceride levels, that can be complicated with acute pancreatitis. This autosomal recessive disorder is rare (1/10(6) in the general population). Classically this disorder is non atherogenic, and the heterozygotes are asymptomatic. To date, 35 gene mutations have been described throughout the world. We have studied 12 families in which the molecular basis for LPL deficiency had been established (direct sequencing of PCR products) by the presence of mutations on the LPL gene, in the 18 homozygous probands. We have found 13 mutations: 7 missense mutations in exons 5 and 6, 3 deletions of few bases in exons 3 and 4, 1 insertion one base in exon 2, one large deletion of exon 9, and one partial duplication of exon 6. PCR and enzymatic restriction of the LPL gene were used as methods for screening mutations or analysing polymorphic markers. This allowed a discrimination between heterozygote carriers (C, n = 35) and non carriers (NC, n = 26). Both groups were comparable for age, sex ratio, body mass index, life style habits, and other risk factors for atherosclerosis. Comparison (U-test Mann Whitney) of plasma lipid values revealed a lower HDL cholesterol level (C: 0,47 +/- 0,11 g/l vs NC: 0,58 +/- 0,18 g/l, p < 0.05) and a higher triglyceride level (C: 1,15 +/- 0,73 g/l vs NC: 0,77 +/- 0,43 g/l, p < 0.05) in heterozygotes. Conversely to the homozygous state, heterozygous LPL deficiency predisposes to a lipid profile that may be atherogenic evenly frequent (approximately 1/500) in the general population.

Heterozygote↗