Search PubMed⌕ Search

Biomedical subjects

P H Groot

Publications and source records attributed to P H Groot.

At least 55 records · Page 3Linked to original sources
PubMed1989

Effects of diets supplemented with lard fat or mackerel oil on plasma lipoprotein lipid concentrations and lipoprotein lipase activities in domestic swine.

Levels of plasma lipoproteins and lipoprotein lipase activities in post-heparin serum were measured in 24-h fasted pigs which were fed a diet containing either 21 energy % mackerel oil or 21 energy % lard fat for 8 weeks. Lipoprotein fractionation was performed separately by density gradient ultracentrifugation and agarose gel chromatography. After 8 weeks levels of plasma triacylglycerol (-62%) and cholesterol (-55%) were lower in the mackerel oil than in the lard fat-fed animals. The triacylglycerol decline was exclusively due to the VLDL fraction, while cholesterol was reduced in all lipoprotein fractions (VLDL, IDL, LDL and HDL). Lipoprotein lipase activity in post-heparin serum, taken 6 h after a meal, was 31% decreased in mackerel oil-fed animals. The results support the hypothesis that regular intake of fish oil reduces VLDL secretion.

Animals↗
PubMed1988

The long-term effect of alprenolol on plasma apolipoproteins A-I and B.

The concentration of lipids, lipoproteins and apolipoprotein A-I and B was measured in the plasma of 33 patients, enrolled in a double-blind, controlled trial of alprenolol in myocardial infarction, after one year on the study medication and again after 6 months off the medication. Sixteen patients received 200 mg alprenolol twice daily and 17 received placebo. There were no statistically significant differences between the parameters in the two groups after one year on medication. However, when medication was stopped, the ratio of apolipoprotein B to apolipoprotein A-I fell by 9% in the alprenolol group and increased by 2% in the placebo group. This difference was statistically significant. Our results suggest that alprenolol, a beta-blocker with weak intrinsic sympathomimetic effect, has slight effects on plasma lipoproteins. These effects were apparent only by measurements of apolipoproteins.

Adult↗
PubMed1988

Effect of dietary fat composition on the metabolism of triacylglycerol-rich plasma lipoproteins in the postprandial phase in meal-fed rats.

Rats conditioned to eating fixed-size meals (meals at 7 AM and 7 PM), consuming diets rich in palm oil or sunflower seed oil, were used to study the metabolism of chylomicrons and hepatic very low density lipoproteins (VLDL) as a function of time after meal consumption. Rats fed a palm oil diet had higher serum triacylglycerol levels at 7 AM, before the meal (1.96 +/- 0.25 mM vs. 1.09 +/- 0.09 mM) and reached higher levels postprandially (4.32 +/- 0.48 mM vs. 2.87 +/- 0.18 mM) than sunflower seed oil-fed animals, due to higher levels of hepatic VLDL (at 7 AM) and higher levels of chylomicrons and hepatic VLDL (in the postprandial phase). These differences in serum triacylglycerol concentrations between the diets tested were found not to be due to differences in hepatic VLDL triacylglycerol secretion (similar rate for both dietary groups and not very much affected by meal consumption) or chylomicron triacylglycerol secretion (similar response profiles on both diets), pointing towards differences in plasma triacylglycerol catabolism. Subsequent double-label studies on triacylglycerol catabolism of chylomicrons from palm oil- and sunflower seed oil-fed animals in chow-fed recipients showed that palm oil triacyglycerol is catabolized slower than sunflower seed oil triacylglycerol. Furthermore, activities of postheparin plasma lipoprotein lipase tended to be higher in sunflower seed oil-fed animals. From these data we conclude that the relative hypertriglyceridemia found in palm oil-fed animals is due to less efficient catabolism and not to increased synthesis of plasma triacylglycerol.

Animals↗
PubMed1986

Distribution of apolipoproteins A-I and A-IV among lipoprotein classes in rat mesenteric lymph, fractionated by molecular sieve chromatography.

The distribution of apolipoproteins A-I and A-IV among lymph lipoprotein fractions was studied after separation by molecular sieve chromatography, avoiding any ultracentrifugation. Lymph was obtained from rats infused either with a glucose solution or with a triacylglycerol emulsion. Relative to glucose infusion, triacylglycerol infusion caused a 20-fold increase in the output of triacylglycerol, coupled with a 4-fold increase in output of apolipoprotein A-IV. The output of apolipoprotein A-I was only elevated 2-fold. Chromatography on 6% agarose showed that lymph apolipoproteins A-I and A-IV are present on triacylglycerol-rich particles and on particles of the size of HDL. In addition, apolipoprotein A-IV is also present as 'free' apolipoprotein A-IV. The increase in apolipoprotein A-I output is caused by a higher output of A-I associated with large chylomicrons only, while the increase in apolipoprotein A-IV output is reflected by an increased output in all lymph lipoprotein fractions, including lymph HDL and 'free' apolipoprotein A-IV. The increased level of 'free' A-IV, seen in fatty lymph, may contribute to, and at least partly explain, the high concentrations of 'free' apolipoprotein A-IV present in serum obtained from fed animals.

Absorption↗
PubMed1986

Is the ratio of apo B/apo A-I an early predictor of coronary atherosclerosis?

It is unknown which lipoprotein in childhood is the best predictor of atherosclerosis later on in life. We measured serum triglycerides, total cholesterol, its subfractions (LDL, HDL, HDL2, HDL3) and apoproteins (A-I, A-II, B) in two groups of children. They were offspring of fathers who had severe coronary atherosclerosis or no coronary sclerosis, as determined by coronary angiography. Fasting blood lipids were measured in 49 children of fathers with severe sclerosis, and in 37 children of fathers without sclerosis. Sons of fathers with severe coronary atherosclerosis had higher levels of apo B and of the ratio apo B/apo A-I than sons of fathers free of atherosclerosis. No differences in lipid levels in daughters were observed. These observations suggest that apolipoproteins play a part in early atherogenesis. They further indicate that it may be possible to detect children who have a high probability of developing severe coronary atherosclerosis later in life.

Adolescent↗
PubMed1985

Electroimmunoassay of rat apolipoproteins A-I, A-IV, and E. A procedure for sample treatment to increase the sensitivity in diluted fractions.

Methods for the quantitative determination of rat apolipoproteins A-I, A-IV, and E by electroimmunoassay are described. Apolipoproteins present in diluted samples of biological fluids (approx. 2 ml) were concentrated by precipitation with deoxycholate and trichloroacetic acid. The protein pellets were solubilized in 0.1 ml of 0.5 M NaOH and these samples were delipidated with tetramethylurea and assayed. This protocol enables the measurement of apolipoprotein concentrations that are at least 10 times lower than normally detectable; 0.2 micrograms of apolipoprotein A-IV, 0.2 micrograms of apolipoprotein A-I, and 0.8 micrograms of apolipoprotein E can be easily detected in samples of 2 ml.

Animals↗
PubMed1985

Coupling of photoactivatable glycolipid probes to apolipoproteins A-I and A-II in human high density lipoproteins 2 and 3.

High density lipoprotein (HDL) from human serum was subfractionated into HDL2 and HDL3 by rate-zonal density gradient ultracentrifugation. The orientation of apoproteins (apo) A-I and A-II in these subfractions was investigated by use of the photosensitive glycolipid probes, 2-(4-azido-2-nitrophenoxy)-palmitoyl[1-14C]glucosamine (compound A) and 12-(4-azido-2-nitrophenoxy)-stearoyl[1-14C]glucosamine (compound B). Both probes were added to the HDL-structures in a ratio of two or three probe molecules per particle and were photoactivated by irradiation at a wavelength above 340 nm. After delipidation the probe-apoprotein adducts were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both the "shallow" probe (compound A) and the "depth" probe (compound B) were coupled for 10-14% (of the label added) to apoA-I and apoA-II from HDL3 and for about 6% to apoA-I and apoA-II from HDL2. By taking into account the relative amounts of apoA-I and apoA-II, it was estimated that the "shallow" probe labeled apoA-I 40% more effectively than apoA-II in both HDL2 and HDL3; the "depth" probe labeled apoA-I and apoA-II equally well in both subfractions. The data suggest that towards the surface HDL2 and HDL3 contain a relatively larger portion of apoA-I than apoA-II, whilst towards the core both subfractions are occupied by an equal portion of apoA-I and apoA-II. Application of these photolabels has failed to point out differences in the structural organization of HDL2 and HDL3.

Affinity Labels↗
PubMed1985

Distribution of apolipoprotein A-IV among lipoprotein subclasses in rat serum.

The distribution of apolipoproteins (apo) A-I, A-IV, and E in sera of fed and fasted rats was studied using various methods for the isolation of lipoproteins. Serum concentrations of apoA-I and apoA-IV decreased significantly during fasting (16 and 31%, respectively), while apoE concentrations remained essentially the same. Chromatography of sera on 6% agarose columns showed that apoA-IV is present on HDL and as so-called "free" apoA-IV. The concentration of "free" apoA-IV decreased six- to seven-fold during fasting, explaining the decrease in total serum apoA-IV. Serum apoA-I and apoE are almost exclusively associated with HDL-sized particles. When sera are centrifuged at a density of 1.21 g/ml, marked quantities of apoA-I (8-9%) and apoE (11-22%) are recovered in the "lipoprotein-deficient" infranatant, suggesting that ultracentrifugation affects the integrity of serum HDL. The nature of the chromatographically separated carriers of serum apoA-IV was investigated by quantitative immunoprecipitation. From these studies, it is concluded that apoA-IV in rat serum is present in at least three fractions: 1) particles with the size and composition of HDL, containing both apoA-I and apoA-IV and possibly minor quantities of apoE; 2) HDL-sized particles containing apoA-IV, but no apoA-I or apoE; 3) "free" apoA-IV probably containing small amounts of bound cholesterol and phospholipid.

Animals↗
PubMed1984

Effects of fat ingestion on high density lipoprotein profiles in human sera.

Serum concentrations of triacylglycerol, apolipoprotein A-I, apolipoprotein A-II, HDL2, and HDL3 were determined in sera of nine normolipidemic adult males, just before and 3, 5, and 8 hr after ingestion of 250 ml of cream (100 g of triacylglycerol). In all individuals a rapid hypertriglyceridemic response was observed. Triacylglycerol concentrations increased from 624 +/- 124 mg/liter of serum to 1435 +/- 350 mg/liter of serum 3 hr after cream ingestion. In most individuals the hypertriglyceridemic response was followed by a decline in serum triacylglycerol concentration to below basic levels. As a result of cream ingestion, small but statistically highly significant increases in serum cholesterol and apolipoprotein A-I concentrations were observed that persisted till the end of the observation period. In most individuals a small rise in the apolipoprotein A-II concentration in serum was also present. Marked changes were observed in serum HDL as illustrated in the HDL absorption at 280 nm and cholesterol profiles obtained by single-spin rate-zonal density gradient ultracentrifugation of the sera. Due to a prominent increase in phospholipids (up to about 18%) and a smaller increase in protein (up to about 6%), flotation rates and concentrations of HDL2 as well as HDL3 increased. These changes in HDL subclass flotation characteristics and chemical composition are best explained by uptake of surface material from chylomicrons by existing HDL2 and HDL3 particles. The data do not support a previously proposed concept in which HDL3 is converted into HDL2 by uptake of surface remnants formed during catabolism of triglyceride-rich lipoproteins.

Adult↗
PubMed1983

Effect of apolipoproteins E and C-III on the interaction of chylomicrons with parenchymal and non-parenchymal cells from rat liver.

[3H]Triacylglycerol-labelled chylomicrons were isolated from intestinal lymph, obtained from rats made hypolipidaemic by treatment with pharmacological amounts of 17 alpha-ethynyloestradiol. Oestrogen treatment results in a large reduction in the content of apolipoproteins (apo) E and C of lymph chylomicrons. Upon incubation in vitro with freshly isolated parenchymal and non-parenchymal cells the apo E-, apo C-poor chylomicrons became readily cell-associated. With increasing chylomicron concentrations this cell-association was saturable and half-maximal cell-association was achieved at about 0.55 mg of triacylglycerol/ml. The cell-association was time- and temperature-dependent. A more than 90% inhibition of the cell-association of the [3H]triacylglycerol moiety was observed with both parenchymal and non-parenchymal cells when pure apo C-III (12.6 micrograms/mg of triacylglycerol) was incorporated into the chylomicrons. These data indicate that apo E-, apo C-poor chylomicrons are bound to both parenchymal and non-parenchymal liver cells at a high-affinity site of limited capacity and that binding to this site is strongly inhibited by apo C-III. With apo C-III-enriched chylomicrons simultaneous determination of the cell-association of the 125I-apo C-III and the [3H]triacylglycerol moiety indicated that more 125I-apo C-III becomes associated to the cells than expected on the basis of [3H]triacylglycerol radioactivity measurements. It is suggested that upon cell-association of apo C-III its binding to the chylomicron particles is lost. Consequently the occupation of the cellular recognition site by apo C-III prevents further chylomicron binding and thus leads to a decrease of the cell-association level of the [3H]triacylglycerol moiety. Apo E enrichment of the chylomicrons led to an increased cell-association rate with parenchymal cells and to a marked increase of the cell-association level with non-parenchymal cells. The cell-association of the apo E radioactivity followed closely the [3H]triacylglycerol radioactivity, indicating that the particle-apo E complex is bound as a unity. The apo E effects were opposed by apo C-III. With apo E-, apo C-III-enriched chylomicrons more 125I-apo E became associated with the cells than could be expected on the basis of the [3H]triacylglycerol measurements. It is concluded that apo C-III can weaken the interaction of apo E with the chylomicrons leading to the cell-association of free apo E. It appears that subtle changes in the apo E and/or apo C-III content of chylomicrons can influence the interaction with both parenchymal and non-parenchymal liver cells.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1983

Liver lipase and high-density lipoprotein. Lipoprotein changes after incubation of human serum with rat liver lipase.

Human sera were incubated with rat liver lipase after inactivation of lecithin:cholesterol acyltransferase, and the changes in serum lipoprotein composition were measured. In the presence of liver lipase serum triacylglycerol and phosphatidylcholine were hydrolyzed. The main changes in the concentrations of these lipids were found in the high-density lipoprotein fraction. Subfractionation of high-density lipoprotein by rate-zonal ultracentrifugation showed a prominent decrease in all constituents of high-density lipoprotein2, a smaller decrease in the 'light' high-density lipoprotein3 and an increase in the 'heavy' high-density lipoprotein3. These data support a concept in which liver lipase is involved in high-density lipoprotein2 phospholipid and triacylglycerol catabolism and suggest that as a result of this action high-density lipoprotein2 is converted into high-density lipoprotein3.

Animals↗
PubMed1983

Influence of diets on acyl-CoA:cholesterol acyltransferase and on acyl-CoA:retinol acyltransferase in villous and crypt cells from rat small intestinal mucosa and in the liver.

Cholesterol and retinol are both esterified with long-chain fatty acid within the mucosal cells of the small intestine. The reactions are catalyzed by microsomal acyl-CoA:cholesterol and acyl-CoA:retinol acyltransferases (EC 2.3.1.26, and EC 2.3.1.-, respectively). To gain more insight into the physiological importance of these acyltransferases, they were studied in villous and crypt cells from rats either fasting or on diets which varied in fat and cholesterol content. Both enzymes had a higher activity in villous than in crypt cells. The activities in villous cells varied with feeding and fasting and the composition of diet when the animals were killed postprandially. Acyl-CoA:cholesterol acyltransferase activity went up upon cholesterol feeding whereas retinol acyltransferase in the mucosa was reduced by high-fat diets. The liver cholesterol acyltransferase activity varied with diet, it increased with both cholesterol and fat feeding, whereas retinol acyltransferase activity remained relatively constant. The results obtained suggest that different diets are of importance for cholesterol and retinol acyltransferase activities both in the intestinal mucosa and in the liver. The variation in activities of the two acyltransferases suggests that they may be different enzymes.

Acyltransferases↗
PubMed1983

The effects of colestipol hydrochloride on serum lipoprotein lipid and apolipoprotein B and A-I concentrations in children heterozygous for familial hypercholesterolemia.

The effects of colestipol hydrochloride on serum lipoprotein lipid and apolipoprotein B and A-I concentrations in children heterozygous for familial hypercholesterolemia. Acta Paediatr Scand, 72:81, 1983.--Colestipol hydrochloride was administered to 28 children with familial hypercholesterolemia type II-A, and its effects on serum lipoproteins were tested against a placebo in a cross-over design. All children consumed a diet low in cholesterol and high in linoleic acid. Colestipol therapy resulted in a 15.7% decrease in serum very low plus low density lipoproteins and in a 13.5% decrease in serum apolipoprotein B. High density lipoprotein cholesterol, serum apolipoprotein A-I and serum triglycerides remained unaltered.

Adolescent↗
PubMed1982

A one-step separation of human serum high density lipoproteins 2 and 3 by rate-zonal density gradient ultracentrifugation in a swinging bucket rotor.

A method was developed for the separation of the high density lipoprotein subclasses HDL2 and HDL3 from human serum. Six serum samples are fractionated in a single-step ultracentrifugal procedure using the Beckman (SW-40) swinging bucket rotor. The method is based on a difference in flotation rate of the high density lipoprotein subclasses. Separation of HDL2 and HDL3 is accomplished by a discontinuous NaBr density gradient applied on top of 2 ml of serum brought to a density of 1.40 g/ml. After centrifugation, high density lipoprotein subclass profiles were obtained using a specially designed gradient fractionator. Contamination of the isolated high density lipoprotein subclasses by serum albumin or by apolipoprotein B-containing lipoproteins was minimal while only a slight overlap between the HDL2 and HDL3 profiles was observed. Chemical and immunochemical analyses of the high density lipoprotein subclasses isolated by the present method were in close agreement with the results obtained by rate-zonal density gradient ultracentrifugation in zonal rotors (Patsch, et al. 1980. J. Biol. Chem. 255: 3178-3185). The major advantage of the method presented in this paper as compared with the zonal rotor method is the possibility to analyze as many as six serum samples simultaneously.

Adult↗
PubMed1981

Relative contributions of parenchymal and non-parenchymal (sinusoidal) liver cells in the uptake of chylomicron remnants.

The relative contributions of parenchymal cells and non-parenchymal (sinusoidal) cells to the in vivo hepatic uptake of chylomicron remnants was measured 30 min after intravenous injection into rats. The chylomicron remnants were labeled with [3H]leucine, which was almost exclusively present in apolipoprotein B. The isolated non-parenchymal cells (a mixture of Kupffer cells and endothelial cells) contained 6.7 times more apolipoprotein B radioactivity per mg cell protein than the isolated parenchymal cells. It was calculated that the contributions of non-parenchymal and parenchymal liver cells to the total hepatic uptake of chylomicron remnants are 35% and 65%, respectively.

Adenine↗
PubMed1981

The effect of a virtually cholesterol-free, high-linoleic-acid vegetarian diet on serum lipoproteins of children with familial hypercholesterolemia (type II-A).

The effect of a virtually cholesterol-free, high-linoleic-acid vegetarian diet and a high-linoleic-acid "normal" diet with a moderate cholesterol content was tested in 39 children heterozygote for hypercholesterolemia type II-A. The diets were administered in an outpatient cross-over design of two periods of 10 weeks each and the serum lipoproteins were analyzed at the end of the two 10-week periods. The vegetarian diet induced a decrease in serum concentrations of LDL-II total and free cholesterol and of apo-B, by an average of 10%, whereas HDL cholesterol and apo-A-I decreased by 4%. The disproportionately large change in LDL compared to the small change in HDL was interpreted as an antiatherogenic effect of the vegetarian diet.

Adolescent↗