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PubMed1986

Maturation and secretion of lipoprotein lipase in cultured adipose cells. II. Effects of tunicamycin on activation and secretion of the enzyme.

The effects of N-linked glycosylation on the activation and secretion of lipoprotein lipase were studied in Ob17 cells. The cells were first depleted of any activity and enzyme content by cycloheximide treatment and of precursors of oligosaccharide chains by tunicamycin. The repletion of lipoprotein lipase content was studied in these cells maintained in the presence of tunicamycin after cycloheximide removal. During the repletion phase, the EC50 values of inhibition by tunicamycin (approx. 0.2 microgram/ml) of the incorporation of labeled glucose, mannose or galactose into trichloroacetic acid-insoluble material were found to be identical. Under these conditions, the rate of protein synthesis was maximally decreased by 30%. The results showed clearly that the recovery in lipoprotein lipase activity was parallel to the recovery in hexose incorporation, no activity being recovered in the absence of glycosylation. An inactive form of lipoprotein lipase from tunicamycin-treated cells was detected by competition experiments with mature active lipoprotein lipase for the binding to immobilized antilipoprotein lipase antibodies, as well as by immunofluorescence staining. SDS-polyacrylamide gel electrophoresis and Western blots of cellular extracts and of extracellular media, obtained after tunicamycin-treated cells were exposed to heparin, revealed a single immunodetectable Mr 52 000 protein, whereas a single Mr 57 000 protein was detected in control cells. Therefore, the results indicate that the acquisition by lipoprotein lipase of a catalytically active conformation is linked directly or indirectly to glycosylation. Despite this lack of activation, the lipoprotein lipase molecule was able to migrate intracellularily and to undergo secretion after heparin stimulation of the tunicamycin-treated cells.

Adipose Tissue↗

PubMed2001

Oxidative modifications of LDL increase its binding to extracellular matrix from human aortic intima: influence of lesion development, lipoprotein lipase and calcium.

Retention of atherogenic lipoproteins in the arterial intima by extracellular matrix (ECM) is assumed to occur during early atherogenesis and its further development. Low density lipoprotein (LDL) trapped in the intima may undergo oxidative modifications, which initiate a chain reaction in atherogenesis. Lipoprotein lipase (LPL) has been found to mediate the binding of native and oxidized LDL to ECM produced by cultured cells and to contribute to foam cell formation by mildly oxidized LDL. In this study ECM, isolated from human aortic intima with different atherosclerotic lesions, was used for the first time to measure the binding to it in vitro of native and differently oxidized 125I-LDL. Oxidation of 125I-LDL increased its binding to the ECM, which was most prominent with the material isolated from intima at the early stage of atherogenesis. With the progression of atherosclerosis, the ability of the isolated intimal ECM to bind native and oxidized 125I-LDL decreased, and strongly oxidized 125I-LDL decreased more than native and moderately oxidized 125I-LDL. LPL increased the binding of moderately oxidized 125I-LDL to the ECM more than native 125I-LDL, while it had only a small effect on strongly oxidized 125I-LDL. LPL-mediated binding of native and oxidized 125I-LDL decreased with the development of atherosclerotic lesions. Calcium ions also increased the binding of LDL to the ECM. This enhanced binding increased with the extent of LDL oxidation, especially at the early stage of atherogenesis, and decreased with lesion progression. These data suggest that the ability of ECM to retain LDL in arterial intima depends on LDL oxidation status and changes with the progression of atherogenesis. In addition, LPL and calcium ions may participate in the retention of LDL in vivo.

Adult↗

PubMed1986

The lipoprotein lipase of white adipose tissue. Studies on the intracellular distribution of the adipocyte-associated enzyme.

The separation of rat epididymal adipocytes into plasma-membrane, mitochondrial, microsomal and cytosol fractions is described. The fractions, which were characterized by marker-enzyme analysis and electron-micrographic observation, from the cells of fed and 24 h-starved animals were used to prepare acetone/diethyl ether-dried powders for the measurement of lipoprotein lipase activities. The highest specific activities and proportion of recovered lipoprotein lipase activity were found in the plasma-membrane and microsomal fractions. The two fractions from the cells of fed rats showed similar activities and enrichments of the enzyme, these activities being higher than the plasma-membrane and lower than the microsomal activities recovered from the cells of starved animals. Chicken and guinea-pig anti-(rat lipoprotein lipase) sera were prepared, and an indirect labelled-second-antibody cellular immunoassay, using 125I-labelled rabbit anti-(chicken IgG) or 125I-labelled sheep anti-(guinea-pig IgG) antibodies respectively, for the detection of cell-surface enzyme was devised and optimized. The amount of immunodetectable cell-surface lipoprotein lipase was higher for cells isolated from fed animals than for cells from 24 h-starved animals, when either anti-(lipoprotein lipase) serum was used in the assay. The amount of immunodetectable cell-surface lipoprotein lipase fell further when starvation was extended to 48 h. The lipoprotein lipase of plasma-membrane vesicles was shown to be a patent activity and to be immunodetectable in a modification of the cellular immunoassay. Although the functional significance of the adipocyte surface lipoprotein lipase is not known, the possibility of it forming a pool of enzyme en route to the capillary endothelium is advanced.

Adipose Tissue↗

PubMed2005

Low density lipoprotein non-esterified fatty acids and lipoprotein lipase in diabetes.

OBJECTIVES: Fatty acid metabolism is disturbed in poorly controlled diabetes. Low density lipoprotein (LDL) oxidation, thought to be an atherogenic modification, is partly dependent on LDL fatty acid content whether it be in the form of cholesteryl ester, phospholipids, triglyceride or non-esterified fatty acid (NEFA). Lipoprotein lipase (LPL) is deficient in diabetic patients. Lipoprotein lipase bound to LDL may facilitate cholesterol accumulation in the artery wall through the attachment of LDL to the proteoglycans expressed on endothelial cells and collagen. The purpose of this study was to examine the degree of binding of fatty acids and lipoprotein lipase to LDL in type 2 diabetic patients and to examine the relationship between non-esterified fatty acids attached to LDL and LDL oxidisability. SUBJECTS AND METHODS: Eight type 2 diabetic patients and eight control subjects were examined fasting and at 4 and 6h following a high fat meal. Six control subjects were examined fasting and 30 min after intravenous heparin. LDL was isolated by sequential ultracentrifugation. Individual LDL non-esterified fatty acids were measured by gas-liquid chromatography following transmethylation. LPL and oxidised LDL were measured by ELISA. RESULTS: The diabetic patients had HbA1c of 7.8 +/- 0.5% confirming moderate diabetic control. There was a large increase in the mean non-esterified fatty acids on LDL from diabetic subjects (0.66 +/- 0.40 mg/mg versus 0.06 +/- 0.02 mg/mg LDL protein, p < 0.01). Mean LDL cholesterol ester fatty acids were also significantly increased in the diabetic subjects (1.47 +/- 0.58 mg/mg versus 0.57 +/- 0.40 mg/mg LDL protein, p < 0.01). There was a significant increase in oxidised LDL (31.2 +/- 24 mg/mg versus 7.7 +/- 4.5 mg/mg LDL protein, p < 0.01) and a significant correlation between postprandial non-esterified fatty acid and LDL oxidation (r = 0.69, p < 0.05). LPL was significantly increased on the LDL but not in the plasma of diabetic subjects. Acute elevation in non-esterified fatty acids produced by heparin in control subjects did not increase LDL non-esterified fatty acids. CONCLUSIONS: This study demonstrates that the disturbance in fatty acid metabolism found in type 2 diabetic subjects is associated with a significant increase in non-esterified fatty acids attached to LDL. This may account, at least in part, for the increased oxidation of the LDL and therefore its atherogenicity. The finding of an increase in the amount of LPL bound to LDL suggests an important mechanism to facilitate the uptake of diabetic LDL by endothelial proteoglycans and collagen in the atherosclerotic plaque.

Aged↗

PubMed1996

Lipoprotein lipase stimulates the binding and uptake of moderately oxidized low-density lipoprotein by J774 macrophages.

Lipoprotein lipase (LPL) stimulates the uptake of low-density lipoprotein (LDL) and very-low-density lipoprotein (VLDL) in different cell types, including macrophages, through bridging of LPL between lipoproteins and extracellular heparan sulphate proteoglycans (HSPG). Because macrophages produce LPL and because modified lipoproteins are present in the arterial wall in vivo, we wondered whether LPL also enhances the uptake of oxidized LDL by J774 macrophages. LDL samples with different degrees of oxidation, as evaluated by relative electrophoretic mobility (REM) as compared with native LDL are used as well as native and acetylated LDL. Addition of 5 microg/ml LPL to the J774 cell culture medium stimulated the binding of both native LDL and moderately oxidized LDL (REM < 3.5) 50-100-fold, and their uptake was stimulated approx. 20-fold. The LPL-mediated binding of native LDL and moderately oxidized LDL was dose-dependent. Preincubation of the cells with heparinase (2.4 units/ml) inhibited the stimulatory effect of LPL, indicating that this LPL-mediated stimulation was due to bridging between the lipoproteins and HSPG. The binding to J774 macrophages of severely oxidized LDL (REM=4.3) was stimulated less than 3-fold by LPL, whereas its uptake was not stimulated significantly. The binding and uptake of acetylated LDL (AcLDL) were not stimulated by LPL, although the LPL-molecule itself does bind to AcLDL. Measurements of the cellular lipid content showed that addition of LPL also stimulated the accumulation in the cells of cholesteryl ester derived from both native LDL and moderately oxidized LDL in a dose-dependent manner. We conclude that our results present experimental evidence for the hypothesis that LPL serves as an atherogenic component in the vessel wall.

Acetylation↗

PubMed1993

In vitro degradation of very low density lipoprotein from diabetic patients by lipoprotein lipase.

Fatty acid release by incubation with lipoprotein lipase (LPL) in vitro from very low density lipoproteins (VLDL) obtained from diabetic patients was low compared with that from healthy subjects, though the compositions were similar in both VLDL. Percentages of the large size VLDL decreased and those of the small size VLDL increased after the incubation with LPL. At the same time, on polyacrylamide gel disk electrophoresis, the smaller catabolic products from these VLDL appeared at a similar position to that of low density lipoproteins (LDL) and at the running front where high density lipoproteins (HDL) had migrated. The amount of the small size VLDL and the LDL-like lipoproteins produced from diabetic VLDL were less than those from normal VLDL and inversely correlated with the percent decrease of the large original size VLDL. This fact suggests that VLDL from diabetic patients are poor substrates for LPL compared with normal VLDL.

Diabetes Mellitus, Type 2↗

PubMed1993

Low density lipoprotein receptor internalizes low density and very low density lipoproteins that are bound to heparan sulfate proteoglycans via lipoprotein lipase.

It has previously been shown that lipoprotein lipase (LPL) enhances the binding of low density lipoproteins (LDL) and very low density lipoproteins (VLDL) to HepG2 cells and fibroblasts, up to 80-fold. This increase in binding is LDL receptor-independent and is due to a bridging of LPL between extracellular heparan sulfate proteoglycans (HSPG) and the lipoproteins. In the present paper, we show that preincubation of the cells with LPL, followed by washing prior to the binding experiment, increased binding to the same extent as occurs when the binding is performed in the presence of LPL. This indicates that the formation of a complex of LPL with the lipoproteins is not a prerequisite of binding. Binding curves and Scatchard analyses reveal that both the number of binding sites and the affinity of the binding are increased 20-30-fold by the addition of 3.4 micrograms/ml LPL. The addition of LPL also resulted in an enhanced uptake and subsequent lysosomal degradation of both LDL and VLDL when compared with binding, although to a lesser extent (up to 25-fold when measured after 5 h at 37 degrees C). Strikingly, enhanced uptake did not occur in LDL receptor-negative fibroblasts. In addition, down-regulation of the LDL receptor activity by preincubation of the cells for 48 h with either LDL or beta-VLDL resulted in a parallel decrease in the uptake of LPL-mediated HSPG-bound LDL, whereas the LPL-mediated binding itself was not diminished. These observations indicate that the uptake of LPL-mediated HSPG-bound LDL and VLDL mainly proceeds via the LDL receptor. Binding of labeled LDL to the cells at 4 degrees C for 2 h followed by a chase period at 37 degrees C revealed that in absolute terms, the initial rate of internalization of HSPG-bound LDL is comparable with that of LDL receptor-bound LDL (0.58 and 0.44 ng/min/mg of cell protein, respectively). We conclude that in LDL receptor-positive cells, the LPL-mediated binding of LDL and VLDL to HSPG is followed by internalization of the lipoproteins mainly through the rapid process of the classical LDL receptor recycling system, whereas only a minor portion is internalized via the much slower process of HSPG uptake.

Animals↗

PubMed1981

Impaired lipoprotein lipase activation by uraemic and post-transplant sera.

1. Lipoprotein lipase was separated from normal human post-heparin plasma by affinity chromatography and assayed with a 14C-labelled triolein emulsion. No enzyme activity was detected unless whole serum was included in the assay as a source of cofactor, apolipoprotein C-II. 2. After a 10 h fast, serum obtained from 46 normal subjects, eight patients with hypertriglyceridaemia but normal renal function, patients with chronic renal failure (24 undialysed, 20 haemodialysed) and 14 recipients of renal allografts, was added to incubation medium for the assay of lipoprotein lipase to determine the maximum activation of the enzyme. 3. When serum was obtained from normal subjects, maximum activation of the enzyme correlated positively with the concentration of triacylglycerol in the sample. Neither sex nor age had a significant effect on the maximum activation achieved by serum from control subjects. 4. The maximum lipoprotein lipase-activating capacity of serum from uraemic and transplant patients was significantly reduced when compared with serum from healthy controls or from the non-uraemic hypertriglyceridaemic patients. 5. Maximum enzyme activation correlated positively with high-density lipoprotein cholesterol in serum from undialysed patients, but did not correlate positively with total serum triacylglycerols in any of the patient groups. Only in transplant recipients was there a significant inverse relationship between serum creatinine concentrations and maximum enzyme activation. 6. Although lipoprotein lipase activation was impaired in uraemic subjects and renal transplant recipients, this appeared to be due more to the presence of an inhibitor than to cofactor deficiency.

Apolipoprotein C-II↗

PubMed1986

Clearance defects in primary chylomicronemia: a study of tissue lipoprotein lipase activities.

Tissue and postheparin lipoprotein lipase (LPL) activities were assayed in a heterogeneous group of eight chylomicronemic subjects ranging in age from 15 years to 55 years. Three patients, presenting with the classical genetic and clinical features of type I hyperlipoproteinemia, had virtually absent adipose tissue LPL activity and markedly reduced muscle LPL activity (between 5% and 20% of normal). A fourth patient, with a similar but more benign lipoprotein and clinical phenotype, showed reduced adipose tissue LPL activity (10% of control) but retained essentially normal muscle enzyme. This patient represents a variant form of familial LPL deficiency. Two of the four remaining patients presented with typical features of adult type V hyperlipoproteinemia associated with familial hypertriglyceridemia (type IV and V phenotypes) in first-degree relatives. Adipose tissue LPL activities were 25% to 35% of the control mean in these patients, but muscle activities were normal or elevated. A third patient had suggestively similar tissue enzyme levels, but a family study could not be carried out. The eighth patient presented with a brittle type V phenotype, normolipidemia in the two first-degree relatives available for study and normal lipolytic activity in adipose tissue, muscle, and postheparin plasma assayed against a 14C-triolein substrate. An oral fat load in this patient, however, led to a marked but transient increase in light scattering suggesting defective clearance. Mixing experiments in vitro using a chylomicron substrate strongly suggested an extrinsic defect of lipolysis due to the inhibitory effect of excess very low density lipoprotein peptides, presumably apo C-III.(ABSTRACT TRUNCATED AT 250 WORDS)

Adipose Tissue↗

PubMed1970

A rapid assay for lipoprotein lipase.

A rapid assay for lipoprotein lipase activity employing a (14)C-labeled substrate is described. The method is very sensitive and suitable for routine use.

Adipose Tissue↗

PubMed1992

Retention of glucose by N-linked oligosaccharide chains impedes expression of lipoprotein lipase activity: effect of castanospermine.

The effect of castanospermine (CSTP), an inhibitor of glucosidase I, on processing, activity, and secretion of lipoprotein lipase was studied in 3T3-L1 adipocytes. Processing was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of endoglycosidase H (endo H)-digested subunits of lipoprotein lipase from cells incubated 1-2 h with [35S]methionine. Lipoprotein lipase in untreated cells consisted of two groups of subunits, M(r) = 55,000-58,000 and M(r) = 53,000-55,000. The heavier subunits were endo H-resistant, whereas the others were either totally or partially endo H-sensitive. The lipase secreted by untreated cells contained primarily endo H-resistant subunits. Immunofluorescent studies showed that lipoprotein lipase accumulated in Golgi in untreated cells. CSTP, 100 micrograms/ml for 18 h, decreased intracellular lipase activity by 80% and decreased secretion of lipase activity by 91%. Most of the lipase subunits in CSTP-treated cells were totally endo H-sensitive with M(r) = 57,000, some were partially endo H-sensitive, and a trace was endo-H resistant. Totally endo H-sensitive subunits in CSTP-treated cells had a M(r) 2,000-4,000 larger than that in untreated cells, indicating impaired trimming of sugar residues from oligosaccharide chains of the lipase in CSTP-treated cells. The small amount of lipase secreted by CSTP-treated cells consisted primarily of partially endo H-sensitive subunits, with one sensitive and one resistant chain per subunit. Immunofluorescent studies showed that lipoprotein lipase was excluded from Golgi in CSTP-treated cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Adipose Tissue↗

PubMed1986

Beta-adrenergic stimulation enhances translocation, processing and synthesis of lipoprotein lipase in rat heart cells.

Cells isolated from newborn rat hearts were cultured for 10-14 days, and lipoprotein lipase activity was present in an intracellular and heparin-releasable pool. Treatment of the cultures with 10(-7) M isoproterenol for 3 min resulted in a 3-fold increase in heparin-releasable lipoprotein lipase and a concomitant decrease in residual cellular enzyme activity. Similar results were obtained by treatment with dibutyryl cAMP. Treatment with isoproterenol or dibutyryl cAMP for 2 h affected glycosylation of immunoadsorbable lipoprotein lipase, so that the ratio of [3H]galactose to [14C]mannose in the heparin-releasable enzyme increased from 3.8 (control) to 13.0 (isoproterenol-treated). The change in the ratio of the sugars in the cellular fraction of the enzyme was from 3.1 to 9.9. 2 h treatment with isoproterenol did not enhance new enzyme synthesis, as determined by incorporation of [3H]leucine into immunoadsorbable lipoprotein lipase. 24 h after addition of either isoproterenol or dibutyryl cAMP to the culture medium, stimulation of enzyme synthesis was demonstrated. The present results permit three effects of isoproterenol on lipoprotein lipase to be distinguished: stimulation of translocation from a cellular to heparin-releasable pool; enhanced processing of mannose residues and terminal glycosylation; stimulation of synthesis of enzyme protein.

Animals↗

PubMed1990

Localization of lipoprotein lipase to discrete areas of the guinea pig brain.

Lipoprotein lipase is a key enzyme in lipoprotein metabolism present primarily in extrahepatic tissues with high turnover of fatty acids. Using immunocytochemistry we have explored where lipoprotein lipase is localized in guinea pig brain. The enzyme was found to be associated with neuronal cells and vascular endothelial surfaces. The distribution was strikingly uneven with intense reaction in some areas, and virtually no reaction in adjacent areas. The highest reactivity was in neocortex, in hippocampus, in Purkinje cells of the cerebellum and in some motor nuclei of the brainstem. The results suggest marked differences between individual brain areas in utilization of plasma lipoproteins.

Animals↗

PubMed1981

Lipoprotein lipase. Localization on plasma membrane fragments from lactating rat mammary tissue.

Subcellular fractionation studies were done using lactating rat mammary tissue. Lipoprotein lipase (E.C. 3.1.1.34) was found to be associated with plasma membrane-enriched and endoplasmic reticulum-enriched fractions. Considerable amounts of soluble lipoprotein lipase were found after homogenization of this tissue. The membrane-associated lipoprotein lipase activities described here were found to be resistant to release, by heparin, from their membrane sites. Buoyant density gradient fractionation experiments suggest that the lipoprotein lipase activity of lactating mammary tissue is located in part on the secretory epithelial cell plasma membrane. This conclusion is discussed in the context of the known site of action, in vivo, of mammary gland lipoprotein lipase, and of probable routes of its transport to that site.

Animals↗

PubMed1992

Lipoprotein lipase in heart and myocytes: characteristics with intralipid as substrate.

1. Intralipid is a suitable substrate for measuring lipoprotein lipase activity in the presence of other triacylglycerol lipases in heart and myocytes. 2. Triacylglycerol lipase activity in heart and myocytes was increased 10-fold in the presence of serum at pH 7.4 and 8.1. The serum-stimulated activity in myocytes was 95% inhibited by saturating concentrations of antiserum to lipoprotein lipase. 3. Both heparin-releasable and non-releasable lipoprotein lipase fractions had similar Km values for Intralipid and a similar pattern of inhibition by high density lipoprotein but different responses to heparin. 4. Isoproterenol did not alter lipoprotein lipase activity in cardiac myocytes.

Animals↗

PubMed1976

Interaction of concanavalin A with membrane-bound and solubilized lipoprotein lipase of rat heart.

Concanavalin A was used to study the configuration of lipoprotein lipase at the surface of capillary endothelium. Incubation of heart homogenates with increasing concentrations of concanavalin A for 5-60 min resulted in inhibition of up to 50% of enzyme activity. The inhibition was related to the concentration of lectin and the time of incubation and was fully reversible by postincubation with alpha-methyl-D-mannoside. Rat hearts were perfused for 5-60 min and lipoprotein lipase activity determined in postheparin perfusates and in the perfused heart. When the lectin was introduced into the perfusate a significant reduction of heparin-releasable enzyme was found after 30 min of perfusion. The missing enzyme could be recovered by postperfusion with alpha-methyl-D-mannoside, but not by addition of the sugar to the perfusate withdrawn from the apparatus. These results suggested binding of lectin to the surface-located enzyme and support for such a binding was obtained by the finding of release of labeled lectin into the perfusate by heparin. Perfusion of hearts with concanavalin A for 60 min resulted also in a fall in nonreleasable lipoprotein lipase. The mechanism of this fall is not due to impairment of enzyme synthesis, as leucine incorporation into protein was not reduced. Since neither perfusion nor postincubation with alpha-methyl-D-mannoside restored enzyme activity, the fall was most probably due to irreversible inhibition. It is concluded that mannose residues of lipoprotein lipase in heart homogenates and at the endothelial surface of heart capillaries are available to interact with a specific lectin. Such an interaction renders the enzyme less releasable by heparin during perfusion and causes a significant inhibition of enzyme activity in homogenates.

Animals↗

PubMed1987

Inhibition of purified bovine milk lipoprotein lipase by propranolol and other beta-adrenergic blockers in vitro.

Numerous clinical studies have shown that propranolol administration causes hypertriglyceridemia and a decrease in high-density lipoprotein in man. Although these findings have been attributed to diminution of triacylglycerol-rich lipoprotein catabolism by lipoprotein lipase, biochemical studies of the effects of propranolol on lipoprotein lipase activity in vitro have not been previously reported. We purified lipoprotein lipase from raw bovine skimmed milk and examined the effect of propranolol using as substrate phospholipid-stabilized, triolein emulsions containing purified human apolipoprotein C-II. These studies demonstrate that propranolol inhibits lipoprotein lipase activity. The inhibition was found to be noncompetitive with a Ki for propranolol of 0.55 mM. In addition, propranolol was shown to bind to phospholipid-stabilized triolein emulsions reaching local concentrations at the particle surface many times higher than its bulk concentration. Metoprolol, timolol and practolol, which are less hydrophobic than propranolol, were less inhibitory. Atenolol was the weakest inhibitor of purified bovine lipoprotein lipase in vitro.

Adrenergic beta-Antagonists↗

PubMed1983

Effects of heparin and a semi-synthetic heparin analogue on platelet aggregation, lipoprotein lipase and other laboratory tests in surgical patients.

Platelet aggregation, lipoprotein lipase activity, coagulation parameters and routine blood chemistry were measured in a randomised study of 21 surgical patients before, immediately after and 3 months after operation. Sodium heparin 5000 IU was given subcutaneously to 11 patients every 12 hours for 7 days, the first injection 2 hours preoperatively; 10 patients received a semi-synthetic heparin analogue (SSHA 75 mg) in the same manner. The groups were sex and age matched. No conclusive changes were found in platelet aggregation. The increase in lipoprotein lipase activity in SSHA patients 2 hours after injection was significantly greater than in heparin patients. Neither of the two drugs induced significant changes in coagulation parameters or routine blood chemistry. The results indicate a difference in the effect on lipoprotein lipase release between heparin and SSHA at the used dosage schedules.

Aged↗