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From the Unidad de Lipidos y Arteriosclerosis, Hospital Universitario Reina Sofia, Cordoba, Spain (J.L.-M., M.A.O., C.M., S.J., J.S., A.B.-M., J.A.J.-P., F.L.-S., F.P.-J.), and the Lipid Metabolism Laboratory, USDA Human Nutrition Research Center on Aging, Tufts University, Boston (J.M.O.).
Correspondence and reprint request to Prof. Francisco Perez Jimenez, Unidad de Lipidos y Arteriosclerosis, Hospital Universitario Reina Sofia, Avda. Menendez Pidal, s/n. 14004 Cordoba, Spain.
| Abstract |
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Key Words: postprandial lipemia apolipoprotein B XbaI polymorphism triglycerides retinyl palmitate
| Introduction |
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Apolipoprotein (apo) B plays a dominant role in cholesterol
homeostasis. It is required for the assembly and secretion of
chylomicrons in intestine and VLDL in liver, and it also acts as the
ligand for the recognition of LDL by the LDL receptor. The apo B gene
extends over 43 Kb and resides in chromosome 2.33 34 35 36 37
Several polymorphic sites within or adjacent to the gene loci for
apo B have been detected, and numerous reports have associated some of
these polymorphisms with abnormal lipid levels and/or increased CAD
risk.38 39 40 41 42 43 44 Specifically, the X+ allele of the XbaI
restriction fragment polymorphism of the apo B gene has been found
associated with elevated serum cholesterol and/or
triglyceride (TG) levels in several adult
populations.39 40 41 45 46 This polymorphism involves the
third base of the threonine codon 2488 (ACC
ACT) and, although no
amino acid change results from the DNA change creating the XbaI
restriction site,47 this polymorphism is strongly
associated with the presence of certain Ag epitopes on the LDL
particle.48 49 Turnover studies have demonstrated that the
presence of the X+ allele is associated with a slower clearance of
LDL compared with the presence of the X- allele, suggesting that
an alteration in apo B could reduce its binding to the LDL receptor in
these subjects50 51 ; however, in a recent study this
effect was not found significant.52 The previous
hypothesis receives support from an in vitro study showing that LDL
from X-/X- subjects was degraded more rapidly by cultured human
fibroblasts than LDL from X+/X+ subjects.52 Furthermore,
Tikkanen et al53 showed that subjects bearing the X+
allele had a significantly greater LDL-C increase following a
high-fat diet than those subjects homozygous for the X- allele.
The present study was therefore designed to evaluate whether the
apo B XbaI polymorphism could explain some of the interindividual
variability observed in postprandial lipoprotein metabolism
in subjects homozygous for the apo E3 allele.
| Materials and Methods |
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Vitamin A Fat-Loading Test
After a 12-hour fast, subjects were given a fatty meal enriched
with 60 000 U/m2 of body surface area of vitamin A. The
fatty meal consisted of 2 cups of whole milk, eggs, bread, bacon,
cream, walnuts, and butter. The amounts given were 1 g of fat and
7 mg of cholesterol per kilogram of body weight. The meal
contained 65% of calories as fat, 15% as protein, and 25% as
carbohydrates and was eaten in 20 minutes. After the meal the subjects
ate no calories for 11 hours but were allowed to drink water. Blood
samples were drawn before the meal, every hour until the sixth hour,
and every 2 hours and 30 minutes until the 11th hour.
Lipoprotein Separations
Blood was collected in tubes containing EDTA to give a final
concentration of 0.1% EDTA. Plasma was separated from red cells by
centrifugation at 1500g for 15 minutes at
4°C. The chylomicron fraction of TRL (large TRL) was isolated from 4
mL of plasma overlayered with 0.15 mol/L NaCl, 1
mmol/L EDTA (pH 7.4, d 1.006 g/mL) by a single
ultracentrifugal spin (20 000 rpm, 30 minutes, 4°C) in a 50-type
rotor (Beckman Instruments). Chylomicrons contained in the top layer
were removed by aspiration after cutting the tubes and the infranatant
was centrifuged at a density of 1.019 g/mL for 24 hours
at 45 000 rpm in the same rotor. The nonchylomicron fraction of TRL
(also referred as small TRL) was removed from the top of the tube. All
operations were done in subdued light. Large and small TRL fractions
were stored at -70°C until assayed for retinyl palmitate (RP).
Lipid Analysis
Cholesterol and triglycerides in plasma
and lipoprotein fractions were assayed by enzymatic
procedures.54 55 Apo A-I and apo B were determined by
turbidimetry.56 HDL cholesterol (HDL-C) was
measured by analyzing the supernatant obtained following precipitation
of a plasma aliquot with dextran sulphate-Mg2+, as
described by Warnick et al.57 LDL cholesterol
(LDL-C) was obtained as the difference between the HDL-C and the
cholesterol from the bottom part of the tube after
ultracentrifugation at 1.019 g/mL.
Retinyl Palmitate Assay
The retinyl palmitate (RP) content of large and small TRL
fractions was assayed using a method previously
described.58 Briefly, different volumes of the various
fractions (100 µL for chylomicrons and 100-500 µL for remnant) were
placed in 13x100-mm glass tubes. The total volume in each tube was
adjusted, as necessary, to 500 µL using normal saline. Retinyl
acetate (40 ng in 200 µL of mobile phase buffer) was added to each
tube as internal standard. Methanol (500 µL) was added, followed by
the addition of 500 µL of the mobile phase buffer for a total volume
of 1.7 mL. The mobile phase buffer was prepared fresh on a daily basis
by combining 90 mL of hexane, 15 mL of n-butyl chloride, 5
mL of acetonitrile, and 0.01 mL of acetic acid (82:13:5 by volume
with 0.01 mL of acetic acid). The tubes were thoroughly mixed after
each step. The final mixture was centrifuged at 350g
for 15 minutes (at room temperature) and the upper layer was carefully
removed by aspiration and placed into individual autosampler vials. The
autoinjector was programmed to deliver 100 µL per injection and a new
sample every 10 minutes in a custom prepacked silica column SupelcoSil
LC-SI (5 µm, 25 cmxmm intradermal) provided by Supelco, Inc.
The flow was maintained at a constant rate of 2 mL/min and the peaks
were detected at 330 nm. The peak of RP and retinyl acetate was
identified by comparing its retention time with a purified standard
(Sigma) and the RP concentration in each sample was expressed as the
ratio of the area under the RP peak to the area under the RA
peak.59 Here, too, all operations were performed in
subdued light.
Determination Of Apo B-48 and Apo B-100
Apo B-48 and apo B-100 were determined by
SDS-Polyacrylamide gel electrophoresis as described by Karpe
and Hamsten.60 In summary, samples containing isolated
lipoprotein fractions were delipidated in a methanol/diethyl
ether solvent system and the protein pellet was dissolved in 100 to 500
µL of 0.15 mol/L of sodium phosphate, 12.5% glycerol, 2%
sodium dodecyl sulfate (SDS), 5% mercaptoethanol, and 0.001%
bromophenol blue, pH 6.8, at room temperature for 30 minutes followed
by denaturation at 80°C for 10 minutes. Electrophoresis was performed
with a vertical Hoefer Mighty Small II electrophoresis
apparatus connected to an EPS 400/500 (Pharmacia) power
supply on 3 to 20% gradient polyacrylamide gels. The upper and
lower electrophoresis buffers contained 25 mmol/L Tris,
192 mmol/L glycine, and 0.2% SDS adjusted to pH 8.5. Apo
B-100 derived from LDL was used as a reference protein and for standard
curve dilutions. A dilution curve ranging from 0.10 to 2 µg of apo
B-100 was applied to four of the gel lanes. Electrophoresis was run at
60 V for the first 20 minutes and then at 100 V for 2 hours. Gels were
fixed in 12% trichloroacetic acid for at least 30 minutes and stained
in 02% Coomassie G-250-40% methanol-10% acetic acid for at least 4
hours. Destaining was done in 12% methanol-7% acetic acid with four
changes of destaining solution for 24 hours. Gels were scanned with a
videodensitometer scanner (TDI, Madrid, Spain) connected to a personal
computer for integration of the signals. Background intensity was
calculated after scanning an empty lane. The coefficient of variation
for the SDS-PAGE was 7.3% for apo B-48 and 5.1% for apo B-100.
DNA Amplification and Genotyping
DNA was extracted from 10 mL of EDTA-containing blood.
Amplification of a region of exon 26 of the apo B was done by
polymerase chain reaction (PCR) with 250 ng of genomic DNA and 0.2
µmol of each oligonucleotide primer (P1,
5'-GGAGACTATTCAGAAGCTAA-3', and P2, 5'-GAAGAGCCTGAAGACTGACT-3') in
50 µL. DNA was denatured at 95°C for 5 minutes followed by 30
cycles of denaturation at 95°C for 1 minute, annealing at 56°C for
1.5 minutes and extension at 70°C for 2 minutes. Twenty microliters
of the PCR product were digested with 10 U of restriction enzyme
XbaI (BRL) in a total volume of 35 µL. Digested DNA was separated by
electrophoresis on an 8% nondenaturing polyacrylamide gel at
150 V for 2 hours. Bands were visualized by silver staining. Samples
containing the X- allele characterized by the absence of the
polymorphic XbaI cutting site were amplified a second time to
verify the genotype.
Amplification of a region of 266-bp of the apo E gene was done by PCR with 250 ng of genomic DNA and 0.2 µmol of each oligonucleotide primer (E1, 5'-GAACAACTGACCCCGGTGGCGGAG-3', and E2, 5'-TCGCGGGCCCCGGCCTGGTACACTGCCA-3') and 10% dimethyl sulfoxide in 50 µL. DNA was denatured at 95°C for 5 minutes followed by 30 cycles of denaturation at 95°C for 1 minute, annealing at 63°C for 1.5 minutes and extension at 72°C for 2 minutes. Twenty microliters of the PCR product were digested with 10 U of restriction enzyme CfoI (BRL) in a total volume of 35 µL. Digested DNA was separated by electrophoresis on an 8% nondenaturing polyacrylamide gel at 150 V for 2 hours. Bands were visualized by silver staining.
Statistical Analysis
The following variables were calculated to characterize the
postprandial responses of plasma triglycerides, large TRL,
and small TRL to the test meal: Area under the curve (AUC) was the area
between the plasma concentration versus time curve and a baseline drawn
parallel to the horizontal axis through the 0 hour concentration. We
calculated this area with a computer program using the trapezoidal
rule. Other variables were the normalized peak concentration, which
was the average of the peak and the second highest concentration above
the baseline; and the peak time, which was the average of the time to
peak concentration and the time to the second highest concentration.
Data were tested for statistical significance between genotypes
by ANOVA and the Kruskal-Wallis test, and between genotypes and
time by ANOVA for repeated measures. BMI and age were introduced as
covariates in all analyses. When statistical significance was
found, the Tukeys post hoc comparison test was used to identify group
differences. A probability value less than .05 was considered
significant. Stepwise multiple regression analyses were carried
out using small and large TRL-triglycerides, and small and
large TRL-RP, and apo B-48 AUC as dependent variables, and age,
BMI, apo B genotypes, basal cholesterol, and
triglyceride values as independent variables. Discrete
variables were divided into classes for analysis. All data
presented in text and tables are mean±SD.
| Results |
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Plasma cholesterol and triglyceride responses
following the fat load test are presented in Fig 1
. Significant time effects were seen for
both total cholesterol (P=.022) and
triglycerides (P<.0001), showing that the
cholesterol levels decreased during the postprandial
period, whereas the opposite effect was seen for
triglycerides. Plasma triglyceride levels
remained significantly elevated over the baseline for all time points
except the last determination (11 hours). There were no differences in
total cholesterol and triglyceride response
between X- and X+ subjects (P=.760 and P=.831,
respectively). The distribution of plasma triglyceride
within the different lipoprotein fractions examined is
presented in Fig 2
.
Triglyceride levels in large TRL particles (Fig 2A
)
remained significantly elevated over the baseline in X- subjects
during the entire period; however, these values were not significantly
different at the end of the experimental period in those subjects with
the X+ allele. Triglycerides in the small TRL (Fig 2B
)
fraction increased over baseline during the first 6 hours of the
postprandial period for both X- and X+ subjects. No significant
genotype effects were observed by ANOVA for repeated measures
(interaction between genotype and time) for
triglyceride levels in either of the TRL fractions.
Subjects with the X- genotype appear to have elevated levels
of large TRL and small TRL triglycerides (Fig 2
) and AUC
(Table 2
); however, these effects did not
reach statistical significance.
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The distribution of plasma cholesterol within the different
TRL fractions examined is presented in Fig 3
. Cholesterol in large TRL
(Fig 3A
) was significantly elevated over baseline in X- and X+
subjects during the first 9 hours of the fat load. No significant
genotype effect was observed by ANOVA. Cholesterol
in the small TRL fraction (Fig 3B
) increased over the baseline during
the first 6 hours of the postprandial period for both X- and X+
subjects and decreased below the baseline at the 11 hours time point.
No significant differences were noted between genotypes with
regard to postprandial response for this parameter.
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In X- subjects, the plasma LDL cholesterol (Fig 4A
) levels showed a significant decrease
for time points 1-6 hours compared with baseline levels. On the other
hand, in X+ subjects, plasma LDL-C levels showed a significant decrease
only at 4 hours. There were no significant differences in postprandial
LDL-Cholesterol response as demonstrated by ANOVA for
repeated measures. In X- subjects, the plasma apo B levels (Fig 4B
)
showed a significant decrease for the 3 and 4 hour time points compared
with baseline levels, whereas no significant changes in postprandial
apo B was observed in X+ subjects. There were no significant
differences in postprandial apo B response.
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HDL-Cholesterol levels (Fig 4C
) decreased during the first
half of the postprandial period (1-5 hours) in X+ subjects and returned
to the baseline afterward; however, the changes did not reach
statistical significance versus the baseline. In X- subjects, HDL
levels remained unchanged except at the 11 hour time point that was
significantly elevated over the baseline (P=.0007). No
genotype effect could be demonstrated by ANOVA for repeated
measures. The postprandial apo AI changes (Fig 4D
) were similar to
those observed for HDL-Cholesterol; however, a significant
genotype effect was seen (P=.047), with X- subjects
having greater apo A-I levels compared with X+ subjects.
RP and apo B-48 were used as markers for intestinal lipoprotein
production. Large and small TRL-RP responses in X- and X+
subjects are shown in Fig 5
. RP levels in
large TRL and small TRL were significantly elevated over the baseline
in X- and X+ subjects during the entire period. A significant
genotype effect was also observed by ANOVA for repeated
measures, with X- subjects showing a significantly greater
postprandial response (P=.04) in the large TRL RP (Fig 5A
)
and a greater (P=.023) AUC than X+ subjects (Table 2
).
Furthermore, a significant genotype by time interaction was
also observed in this fraction (P=.005). The small TRL RP
response (Fig 5B
) was also significantly greater in X- than X+
subjects, as suggested by a significant genotype effect
observed by ANOVA (P=.010) and a greater AUC
(P=.007) (Table 2
).
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Large and small apo B-48 responses in X- and X+ subjects are shown in
Fig 6
. Apo B-48 levels (as determined by
densitometric scanning) in large TRL and small TRL were significantly
elevated over the baseline in X- and X+ subjects during the entire
period. A significant genotype effect was also observed by
ANOVA for repeated measures, with X- subjects showing a significantly
greater postprandial response (P=.016) in the large apo B-48
(Fig 6A
) and a greater (P=.030) AUC than X+ subjects (Table 2
). The small TRL apo B-48 response (Fig 6B
) was also significantly
greater in X- than X+ subjects, as suggested by a significant
genotype effect observed by ANOVA (P=.040) and a
greater AUC (P=.040) (Table 2
). No significant
genotype effects were observed for apo B-100 in large or small
TRL particles (Table 2
).
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Multiple regression analyses (Table 3
) revealed that the XbaI
polymorphism at the apo B gene was the only significant
(P=.03) predictor of the variability on large TRL-RP
postprandial response (AUC) in our study population, accounting for
10.1% of the variance, whereas the apo B genotype
(P=.01) and baseline plasma cholesterol
(P=.02) were both significant predictors of small TRL-RP
postprandial response, accounting for 14.1 and 10% of the variance,
respectively. When large TRL apo B-48 was used as a dependent
variable using the same variables in the model as for TRL-RP,
only the apo B genotype entered the model as a predictor
(P=.008) accounting for 20.1% of the variance. When small
TRL apo B-48 was introduced in the model as a dependent variable,
the XbaI genotype, age, and BMI were significant predictors,
accounting for 36.4% of the variance (Table 3
). The XbaI
polymorphism did not enter the model when large or small TRL-TG
were used as dependent variables.
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| Discussion |
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The X+ allele of the XbaI polymorphism has been found associated with increased serum levels of cholesterol and triglycerides by others.39 40 41 45 46 These results could not be confirmed in ours or in other studies,65 possibly due to our reduced sample size or the population studied, young healthy normolipemic males. In agreement with our results, previous studies have shown that in young normolipemic subjects no significant difference was observed between the degradation rate of LDL derived from X- versus X+ subjects.52
Subjects with the X- genotype showed a significantly greater postprandial response in the intestinally derived TRL particles, suggested by the increase in small and large TRL-RP response. Retinyl esters (predominantly RP) are incorporated into the core of chylomicrons in the intestine following the absorption and esterification of vitamin A.66 In the circulation they remain associated with chylomicrons during triglyceride lipolysis and are taken up by the liver within chylomicron remnants.67 Retinyl esters are either stored in the liver or resecreted as unesterified retinol bound to retinol-binding protein.68 The normal liver does not resecrete esterified retinol.69 Since their exchange with other lipoproteins in the circulation is small during the first 8 hours after consumption of a fat load,70 71 retinyl esters have been used as markers for intestinal lipoproteins, thus providing a means for measuring parameters of chylomicrons and chylomicron-remnant metabolism.71 72 73 74 75 In this study we verified the results obtained using retinyl palmitate by determining apo B-48 levels60 in both large and small triglyceride particles. Both markers provided similar results with regard to the XbaI associations with differential postprandial response.
Many factors control the concentration of triglyceride in the circulation. Chylomicron secretion by the intestine, VLDL secretion by the liver, conversion of TRL to triglyceride-depleted lipoproteins, and tissue uptake of triglyceride-depleted lipoproteins are all processes that could be responsible for fluctuations in postprandial triglyceride and lipoprotein concentrations. The greater increases in X- than in X+ subjects in plasma RP concentration in large and small TRL suggest intestinal secretion of TRL as the most plausible mechanism. Since chylomicron catabolism is a relatively fast and efficient process,76 it is unlikely that these phenomena could be due to fluctuations in chylomicron clearance. Several mechanisms can be proposed to explain why TRL secretion by the intestine might not be constant after fat ingestion. Variation in gastric emptying, gastrointestinal motility, or the rate of fat digestion in the intestine,77 potentially could cause postprandial peaks in plasma triglyceride. Postprandial triglyceride peaks could also result from differences in the abilities of the proximal and distal intestine to transport absorbed fat or fluctuations in the availability of phospholipids78 and/or newly synthesized chylomicron apolipoproteins in the enterocyte.79 Alternatively, it has been reported that X+ polymorphism is associated with less efficient binding of LDL to its receptor,50 51 which may result in less efficient down-regulation of the LDL receptor. Consequently, X+ subjects could express more LDL receptor, leading to greater elimination of triglyceride-rich lipoproteins via this receptor and thus to the differences observed with respect to X- carriers.
The DNA change that results in the absence of the XbaI restriction site
in the apo B gene occurs at the third base of triplet coding for
threonine at amino acid 2488. No amino acid changes result from this
base change in apo B-100.47 This polymorphism is in
strong linkage disequilibrium with the apo B Val591
Ala
polymorphism (Ag a1/d), however, which may be the functional
sequence change.80 Another tentative hypothesis relates to
the fact that this mutation is close to the editing site at position
2153. In humans, Apo B-48 is synthesized only in the
intestine81 and is the product of an intestinal mRNA
identical in structure to apo B-100 mRNA except for a single C to U
base substitution, the first base of the codon CAA for Gln-2153,
changing it to UAA, a stop codon.82 83 The mechanism
behind the C to U conversion or editing could involve a form of
cytidine deaminase,84 although other possibilities have
not been ruled out. The mooring sequence model for the editosome
suggests that the recognition and binding sequences of nuclear factors
that both identify the specific site for editing and "moor" the
editing activity are distal to and different from the sequences in the
immediate vicinity of the editing site.84 85 86 The mooring
sequences might be a specific primary sequence or a unique secondary
structure of apo B mRNA. It is possible that the XbaI mutation, close
to the editing site, could affect these "mooring sequences" and
modify the editing activity of apo B mRNA that results in changes of
apo B-48 and intestinal TRL secretion observed in this study.
Alternatively, the XbaI polymorphism may be functionally silent and
may be in linkage disequilibrium with a functionally important sequence
change in the coding or the regulating regions of the apo B
gene.80 Both kinetic and in vitro studies favor the latter
hypothesis.
Previous studies have shown that the X- allele was found significantly more frequently among patients with CAD and with peripheral arterial disease than among healthy control subjects.87 88 89 Nevertheless, in some studies, the X- subjects have lower LDL-C and apo B levels than the X+ subjects, although this effect may be dependent on age and sex.90 It is possible that the higher postprandial response observed in this study in subjects with the X- genotype compared with subjects with the X+ genotype could be involved in the higher risk of CAD previously reported in X- subjects. At least five lines of evidence implicate postprandial lipoprotein metabolism in the genesis of CAD. First, receptor-mediated uptake of TRL remnant particles by monocyte-derived macrophages promotes the formation of lipid-laden foam cells in the vessel wall.91 Second, chylomicron and VLDL remnants make a substantial contribution to the lipid content of the vessel wall in cholesterol-fed rabbits.92 Third, the level of HDL-C, an established risk factor for CAD, is dependent on both the metabolism of TRL particles and the extent of postprandial lipemia.93 Fourth, patients with familial dysbetalipoproteinemia are at high risk of CAD and show a build up of TRL remnants of both intestinal and hepatic origin.94 Fifth, cross-sectional case-control studies have found that increased postprandial triglycerides and RP concentrations are associated with angiographically verified CAD and carotid artery wall thickness.5 6
In conclusion, subjects with the X- genotype of the XbaI polymorphism of apo B have a higher postprandial response than do X+ subjects. These differences observed in postprandial lipoprotein metabolism could be involved in the higher risk of coronary heart disease observed in these subjects.
| Selected Abbreviations and Acronyms |
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| Acknowledgments |
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Received January 9, 1996; accepted January 20, 1997.
| References |
|---|
|
|
|---|
2.
Castelli WP, Garrison RJ, Wilson PWF, Abbot RD,
Kalousian S, Kannel WB. Incidence of coronary heart
disease and lipoprotein cholesterol levels: the Framingham
Study. JAMA.. 1986;256:2835-2838.
3.
Zilversmit DB. Atherosclerosis:
A postprandial phenomenon. Circulation.. 1979;60:473-485.
4. Cohn JS, McNamara JR, Cohn SD, Ordovas JM, Schaefer EJ. Postprandrial plasma lipoprotein changes in human subjects of different ages. J Lipid Res.. 1988;29:469-479.[Abstract]
5.
Ryu JE, Howard G, Craven TE, Bond MG, Hagaman AP,
Crouse JR, III. Postprandial triglyceridemia and
carotid atherosclerosis in middle-aged
subjects. Stroke.. 1992;23:823-828.
6.
Groot PHE, Van Stiphout W-AHJ, Krauss XH, Janse HC,
Van Tol A, Van Ramshorst E, Chin-On S, Hofman A, Cresswell SR, Havekes
L. Postprandial Lipoprotein metabolism in
normolipidemic men with and without coronary artery
disease. Arterioscler Thromb.. 1991;11:653-662.
7. Cavallero E, Dachet C, Neufcour D, Wirquin E, Mathe D, Jacotot B. Postprandial amplification of lipoprotein abnormalities in controlled type II diabetic subjects: relationship to postprandial lipemia and C-peptide/glucagon levels. Metabolism.. 1994;43:270-278.[Medline] [Order article via Infotrieve]
8. Karpe F, Steiner G, Uffelman K, Olivecrona T, Hamsten A. Postprandial lipoproteins and progression of coronary atherosclerosis. Atherosclerosis.. 1994;106:83-97.[Medline] [Order article via Infotrieve]
9.
Uiterwaal CSPM, Grobbee DE, Witteman JCM, Van Stiphout
W-AHJ, Krauss XH, Havekes LM, De Bruijn AM, Van Tol A, Hofman A.
Postprandial triglyceride response in young adult
men and familial risk for coronary
atherosclerosis. Ann Intern Med.. 1994;121:576-583.
10. Castro Cabezas M, Erkelens DW, Kock LAW, De Bruin TWA. Postprandial apolipoprotein B100 and B48 metabolism in familial combined hyperlipidaemia before and after reduction of fasting plasma triglycerides. Eur J Clin Invest.. 1994;24:669-678.[Medline] [Order article via Infotrieve]
11.
Zilversmit DB. Atherogenic nature of
triglycerides, postprandial lipidemia, and
triglyceride-rich remnant lipoproteins. Clin
Chem.. 1995;41:153-158.
12.
Patsch JR, Miesenböck G, Hopferwieser T,
Mühlberger V, Knapp E, Dunn JK, Gotto AM Jr, Patsch W.
Relation of triglyceride metabolism and
coronary artery disease: studies in the postprandial
state. Arterioscler Thromb.. 1992;12:1336-1345.
13. Hughes TA, Elam MB, Applegate WB, Bond MG, Hughes SM, Wang X, Tolley EA, Bittle JB, Stentz FB, Kang ES. Postprandial lipoprotein responses in hypertriglyceridemic subjects with and without cardiovascular disease. Metabolism.. 1995;44:1082-1098.[Medline] [Order article via Infotrieve]
14. Cohn JS, McNamara JR, Cohn SD, Ordovas JM, Schaefer EJ. Plasma apolipoprotein changes in the triglyceride-rich lipoprotein fraction of human subjects fed a fat-rich meal. J Lipid Res.. 1988;29:925-936.[Abstract]
15.
Ginsberg HN, Karmally W, Siddiqui M, Holleran S, Tall
AR, Rumsey SC, Deckelbaum RJ, Blaner WS, Ramakrishnan R. A
dose-response study of the effects of dietary cholesterol
on fasting and postprandial lipid and lipoprotein
metabolism in healthy young men. Arterioscler
Thromb.. 1994;14:576-586.
16.
Grant KI, Marais MP, Dhansay MA. Sucrose in a
lipid-rich meal amplifies the postprandial excursion of serum and
lipoprotein triglyceride and cholesterol
concentrations by decreasing triglyceride
clearance. Am J Clin Nutr.. 1994;59:853-860.
17.
Dubois C, Armand M, Azais-Braesco V, Portugal H, Pauli
A-M, Bernard P-M, Latgé C, Lafont H, Borel P, Lairon D.
Effects of moderate amounts of emulsified dietary fat on
postprandial lipemia and lipoproteins in normolipidemic adults.
Am J Clin Nutr.. 1994;60:374-382.
18. Dubois C, Armand M, Mekki N, Portugal H, Pauli A-M, Bernard P-M, Lafont H, Lairon D. Effects of increasing amounts of dietary cholesterol on postprandial lipemia and lipoproteins in human subjects. J Lipid Res.. 1994;35:1993-2007.[Abstract]
19. Sandström B, Hansen LT, Sorensen A. Pea fiber lowers fasting and postprandial blood triglyceride concentrations in humans. J Nutr.. 1994;124:2386-2396.
20. Muesing RA, Griffin P, Mitchell P. Corn oil and beef tallow elicit different postprandial responses in triglycerides and cholesterol, but similar changes in constituents of high-density lipoprotein. J Am Coll Nutr.. 1995;14:53-60.[Abstract]
21. Barr SI, Kottke BA, Mao SJ. Postprandial distribution of apolipoproteins C-II and C-III in normal subjects and patients with mild hypertriglyceridemia: comparison of meals containing corn oil and medium-chain triglyceride oil. Metabolism.. 1985;34:983-992.[Medline] [Order article via Infotrieve]
22. Harris WS, Connor WE, Alam N, Illingworth DR. Reduction of postprandial triglyceridemia in humans by dietary n-3 fatty acids. J Lipid Res.. 1988;29:1451-1460.[Abstract]
23. Weintraub MS, Zechner R, Brown A, Eisenberg S, Breslow JL. Dietary polyunsaturated fats of the W-6 and W-3 series reduce postprandial lipoprotein levels: chronic and acute effects of fat saturation on postprandial lipoprotein metabolism. J Clin Invest.. 1988;82:1884-1893.
24.
De Bruin TWA, Brouwer CB, Van Linde-Sibenius Trip M,
Jansen H, Erkelens DW. Different postprandial
metabolism of olive oil and soybean oil: a possible
mechanism of the high-density lipoprotein conserving effect of olive
oil. Am J Clin Nutr.. 1993;58:477-483.
25.
Lichtenstein AH, Ausman LM, Carrasco W, Jenner JL,
Gualtieri LJ, Goldin BR, Ordovas JM, Schaefer EJ. Effects of
canola, corn, and olive oils on fasting and postprandial plasma
lipoproteins in humans as part of a National Cholesterol
Education Program step 2 diet. Arterioscler Thromb.. 1993;13:1533-1542.
26. Salomaa V, Rasi V, Pekkanen J, Jauhiainen M, Vahtera E, Pietinen P, Korhonen H, Kuulasmaa K, Ehnholm C. The effects of saturated fat and n-6 polyunsaturated fat on postprandial lipemia and hemostatic activity. Atherosclerosis.. 1993;103:1-11.[Medline] [Order article via Infotrieve]
27. Kesaniemi YA, Ehnholm C, Miettinen TA. Intestinal cholesterol absorption efficiency in man is related to apoprotein E phenotype. J Clin Invest.. 1987;80:578-581.
28. Weintraub MS, Eisenberg S, Breslow JL. Dietary fat clearance in normal subjects is regulated by genetic variation in apolipoprotein E. J Clin Invest.. 1987;80:1571-1577.
29.
Brown AJ, Roberts DCK. The effect of fasting
triacylglyceride concentration and apolipoprotein E polymorphism on
postprandial lipemia. Arterioscler Thromb.. 1991;11:1737-1744.
30. Nikkilä M, Solakivi T, Lehtimäki T, Koivula T, Laippala P, Astrom B. Postprandial plasma lipoprotein changes in relation to apolipoprotein E phenotypes and low density lipoprotein size in men with and without coronary artery disease. Atherosclerosis.. 1994;106:149-157.[Medline] [Order article via Infotrieve]
31. Superko HR, Haskell WL. The effect of apolipoprotein E isoform difference on postprandial lipoproteins in patients matched for triglycerides, LDL-cholesterol, and HDL-cholesterol. Artery.. 1991;18:315-325.[Medline] [Order article via Infotrieve]
32. Boerwinkle E, Brown S, Sharrett AR, Heiss G, Patsch W. Apolipoprotein E polymorphism influences postprandial retinyl palmitate but not triglyceride concentrations. Am J Hum Genet.. 1994;54:341-360.[Medline] [Order article via Infotrieve]
33. Kane JP. Apolipoprotein B: structural and metabolic heterogeneity. Ann Rev Physiol.. 1983;45:637-650.[Medline] [Order article via Infotrieve]
34. Olofsson SO, Bjursell G, Bostrom K, Carlsson P, Elovson J, Protter AA, Reuben MA, Bondjers G. Apolipoprotein B: structure, biosynthesis and role in the lipoproteine assembly process. Atherosclerosis.. 1987;68:1-17.[Medline] [Order article via Infotrieve]
35.
Deeb SS, Motulsky AG, Albers JJ. A partial cDNA
clone for the human apolipoprotein B. Proc Natl Acad Sci
U S A.. 1985;82:4983-4986.
36.
Blackhart BD, Ludwig EM, Pierotti VR, Caiati L, Onasch
MA, Powell L, Pease R, Knott TJ, Chu ML, Mahley RW, Scott J, McCarthy
BJ, Levy-Wilson B. Structure of the human apolipoprotein B
gene. J Biol Chem.. 1986;261:15364-15367.
37.
Law S, Lackner KJ, Hospattanakar AV, Anchors JM,
Sakaguchi AY, Naylor SL, Brewer HB Jr. Human apolipoprotein
B-100: cloning, analysis of liver mRNA, and assignment of the
gene to chromosome 2. Proc Natl Acad Sci U S A.. 1985;82:8340-8344.
38. Genest JJ, Ordovas JM, McNamara JR, Robbins AM, Meade T, Cohn SD, Salem D, Wilson PWF, Masharani U, Frossard P, Schaefer EJ. DNA polymorphisms of the apolipoprotein B gene in patients with premature coronary artery disease. Atherosclerosis.. 1990;82:7-17.[Medline] [Order article via Infotrieve]
39. Law A, Wallis SC, Powell LM, Pease RJ, Brunt H, Priestley LM, Knott TJ, Scott J, Altman DG, Miller GJ, Rajput J, Miller NE. Common DNA polymorphism within coding sequence of apolipoprotein B gene associated with altered lipid levels. Lancet.. 1986;1:1301-1302.[Medline] [Order article via Infotrieve]
40. Berg K. DNA polymorphism at the apolipoprotein B locus is associated with lipoprotein level. Clin Genet.. 1986;30:515-520.[Medline] [Order article via Infotrieve]
41. Talmud PJ, Barni N, Kessling AM. Apolipoprotein B gene variants are involved in the determination of serum cholesterol levels: a study in normo- and hyperlipidemic individuals. Atherosclerosis.. 1987;67:81-89.[Medline] [Order article via Infotrieve]
42.
Hixson JE, McMahan CA, McGill HC Jr, Strong JP, PDAY
Research Group. Apo B insertion/deletion polymorphisms are
associated with atherosclerosis in young black but not
young white males. Arterioscler Thromb.. 1992;12:1023-1029.
43. Saha N, Tay JSH, Chew LS. Influence of apolipoprotein B signal peptide insertion/deletion polymorphism on serum lipids and apolipoproteins in a Chinese population. Clin Genet.. 1992;41:152-156.[Medline] [Order article via Infotrieve]
44. Xu C-F, Tikkanen MJ, Butler R, Huttunen JK, Pietinen P, Humphries S, Talmud P. Apolipoprotein B signal peptide insertion/deletion polymorphism is associated with Ag epitopes and involved in the determination of serum triglyceride levels. J Lipid Res.. 1990;31:1255-1261.[Abstract]
45. Aalto-Setälä K, Tikkanen M, Taskinen MR, Nieminen M, Homberg P, Kontula K. XbaI and c/g polymorphism of the apolipoprotein B gene locus are associated with serum cholesterol and LDL cholesterol levels in Finland. Atherosclerosis.. 1988;74:47-54.[Medline] [Order article via Infotrieve]
46. Aalto-Setälä K, Kontula K, Mänttäri M, Huttunen J, Manninen V, Koskinen P, Frick HM. DNA polymorphisms of apolipoprotein B and AI/CIII genes and response to gemfibrozil treatment. Clin Pharmacol Ther.. 1991;50:208-214.[Medline] [Order article via Infotrieve]
47. Carlsson P, Darnfors C, Olofsson SO, Bjursell G. Analysis of the human apolipoprotein B gene: complete structure of the B74 region. Gene.. 1986;49:29-51.[Medline] [Order article via Infotrieve]
48.
Berg K, Powell JT, Wallis S, Pease R, Knott TJ, Scott
J. Genetic linkage between the antigenic group (Ag) variation
and the apolipoprotein B gene: assignment of the Ag locus.
Proc Natl Acad Sci U S A.. 1986;83:7367-7370.
49. Dunning AM, Tikkanen MJ, Ehnholm C, Butler R, Humphries SE. Relationships between DNA and protein polymorphisms of apolipoprotein B. Hum Genet.. 1988;78:325-329.[Medline] [Order article via Infotrieve]
50. Demant T, Houlston RS, Caslake MJ, Series JJ, Shepherd J, Packard CJ, Humphries SE. The catabolic rate of low density lipoprotein is influenced by variation in the apolipoprotein B gene. J Clin Invest.. 1988;82:797-802.
51. Houlston RS, Turner PR, Revill J, Lewis B, Humphries SE. The fractional catabolic rate of low density lipoprotein in normal individuals is influenced by variation in the apolipoprotein B gene. Atherosclerosis.. 1988;71:81-85.[Medline] [Order article via Infotrieve]
52. Series JJ, Cameron IM, Caslake M, Gaffney D, Packard CJ, Shepherd J. The XbaI polymorphism of the apolipoprotein B gene influences the degradation of low density lipoprotein in vitro. Biochim Biophys Acta.. 1989;1003:183-188.[Medline] [Order article via Infotrieve]
53. Tikkanen MJ, Xu C-F, Hamalainen T, Talmud P, Sarna S, Huttunen JK, Pietinen P, Humphries S. XbaI Polymorphism of the apolipoprotein B gene influences plasma lipid response to diet intervention. Clin Genet.. 1990;37:327-334.[Medline] [Order article via Infotrieve]
54. Bucolo G, David H. Quantitative determination of serum triglycerides by use of enzymes. Clin Chem.. 1973;19:476-482.[Abstract]
55. Allain CC, Poon LS, Chang CSG, Richmond W, Fu PC. Enzymatic determination of total serum cholesterol. Clin Chem.. 1974;20:470-475.[Abstract]
56. Riepponen P, Marniemi J, Rautaoja T. Immunoturbidimetric determination of apolipoproteins A-1 and B in serum. Scand J Clin Lab Invest.. 1987;47:739-744.[Medline] [Order article via Infotrieve]
57.
Warnick R, Benderson J, Albers JJ. Dextran
Sulfate-Mg precipitation procedure for quantitation of high density
lipoprotein cholesterol. Clin Chem.. 1982;28:1379-1388.
58. Ruotolo G, Zhang H, Bentsianov V, Le N-A. Protocol for the study of the metabolism of retinyl esters in plasma lipoproteins during postprandial lipemia. J Lipid Res.. 1992;33:1541-1549.[Abstract]
59.
De Ruyter MGM, De Leeheer AP.
Simultaneous determination of retinol and retinyl
esters in serum or plasma by reversed-phase high performance
liquid chromatography. Clin Chem.. 1978;24:1920-1923.
60. Karpe F, Hamsten A. Determination of apolipoproteins B-48 and B-100 in triglyceride-rich lipoproteins by analytical SDS-PAGE. J Lipid Res.. 1994;35:1311-1317.[Abstract]
61. Patsch JR, Prasad S, Gotto AM Jr, Bengtsson-Olivecrona G. Postprandial lipemia. A key for the conversion of high density lipoprotein2 into high density lipoprotein3 by hepatic lipase. J Clin Invest.. 1984;74:2017-2023.
62.
Brown SA, Chambless LE, Sharrett AR, Gotto AM Jr,
Patsch W. Postprandial lipemia: Reliability in an epidemiologic
field study. Am J Epidemiol.. 1992;136:538-545.
63.
Calabresi L, Cassinotti M, Gianfranceschi G, Safa O,
Murakami T, Sirtori CR, Franceschini G. Increased postprandial
lipemia in Apo A-IMilano carriers.
Arterioscler Thromb.. 1993;13:521-528.
64. Brenninkmeijer BJ, Stuyt PMJ, Demacker PNM, Stalenhoef AFH, Van't Laar A. Catabolism of chylomicron remnants in normolipidemic subjects in relation to the apoprotein E phenotype. J Lipid Res.. 1987;28:361-370.[Abstract]
65.
Paulweber B, Friedl W, Krempler F, Humphries SE,
Sandhofer F. Association of DNA polymorphism at the
apolipoprotein B gene locus with coronary heart disease and
serum very low density lipoprotein levels.
Arteriosclerosis.. 1990;10:17-24.
66. Goodman DS, Blomstrand R, Wenner B. The intestinal absorption and metabolism of vitamin A and beta carotene in man. J Clin Invest.. 1966;45:1615-1623.
67.
Blomhoff R, Helgerud P, Rasmussen M. In vivo
uptake of chylomicron [3H] retinyl ester by rat liver: Evidence for
transfer from parenchymal to nonparenchymal cells. Proc
Natl Acad Sci U S A.. 1982;79:7326-7330.
68. Goodman DS. Vitamin A metabolism. Fed Proc.. 1980;39:2716-2722.[Medline] [Order article via Infotrieve]
69. Lenich CM, Ross AC. Chylomicron remnant-vitamin A metabolism by the human hepatoma cell line Hep G2. J Lipid Res.. 1987;28:183-194.[Abstract]
70. Wilson DE, Chan I-F, Ball M. Plasma lipoprotein retinoids after vitamin A feeding in normal man: Minimal appearance of retinyl esters among low density lipoproteins. Metabolism.. 1983;32:514-517.[Medline] [Order article via Infotrieve]
71. Berr F, Kern F Jr. Plasma clearance of chylomicrons labeled with retinyl palmitate in healthy human subjects. J Lipid Res.. 1984;25:805-812.[Abstract]
72. Cohn JS, McNamara JR, Krasinski SD, Russell RM, Schaefer EJ. Role of triglyceride-rich lipoproteins from the liver and intestine in the etiology of postprandrial peaks in plasma triglyceride concentration. Metabolism.. 1989;38:484-490.[Medline] [Order article via Infotrieve]
73. Cohn JS, Johnson EJ, Millar JS, Cohn SD, Milne RW, Marcel YL, Russell RM, Schaefer EJ. Contribution of apoB-48 and apoB-100 triglyceride-rich lipoproteins (TRL) to postprandial increases in the plasma concentration of TRL triglycerides and retinyl esters. J Lipid Res.. 1993;34:2033-2040.[Abstract]
74. Berr F, Eckel RH, Kern F Jr. Plasma decay of chylomicron remnants is not affected by heparin-stimulated plasma lipolytic activity in normal fasting men. J Lipid Res.. 1985;26:852-859.[Abstract]
75. Weintraub MS, Eisenberg S, Breslow JL. Different patterns of postprandial lipoprotein metabolism in normal, type IIa, type III, and type IV hyperlipoproteinemic individuals. Effects of treatment with cholestyramine and gemfibrozil. J Clin Invest.. 1987;79:1110-1119.
76. Stalenhoef AFH, Malloy MJ, Kane JP. Metabolism of apolipoproteins B-48 and B-100 of triglyceride-rich lipoproteins in normal and lipoprotein lipase deficient humans. Proc Natl Acad Sci U S A.. 1984;81:1829-1843.
77. Carey MC, Small DM, Bliss CM. Lipid digestion and absorption. Annu Rev Physiol.. 1983;45:651-677.[Medline] [Order article via Infotrieve]
78. Mansbach CM II, Arnold A, Cox M. Factors influencing triacylglycerol delivery into mesenteric lymph. Am J Physiol.. 1985;249:642-648.
79. Glickman RM, Kirsch K, Isselbacehr KJ. Fat absorption during the inhibition of protein synthesis. Studies of chylomicron apoproteins. J Clin Invest.. 1973;52:2910-2920.
80. Peacock RE, Karpe F, Talmud PJ, Hamsten A, Humphries SE. Common variation in the gene for apolipoprotein B modulates postprandial lipoprotein metabolism: A hypothesis generating study. Atherosclerosis.. 1995;116:135-145.[Medline] [Order article via Infotrieve]
81.
Kane JP, Hardman DA, Paulus HE.
Heterogeneity of apolipoprotein B: isolation of
a new species from human chylomicrons. Proc Natl Acad Sci
U S A.. 1980;77:2465-2469.
82. Powell LM, Wallis SC, Pease RJ, Edwards YH, Knott TJ, Scott J. A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine. Cell.. 1987;50:831-840.[Medline] [Order article via Infotrieve]
83.
Chen SH, Habib G, Yang CY, Gu ZW, Lee BR, Weng SA,
Silberman SR, Cai SJ, Deslypere JP, Rosseneu M, Gotto AM Jr, Li WH,
Chan L. Apolipoprotein B-48 is the product of a messenger
RNA with an organ-specific in-frame stop codon.
Science.. 1987;238:363-366.
84. Driscoll DM, Wynne JK, Wallis SC, Scott J. An in vitro system for the editing of apolipoprotein B mRNA. Cell.. 1989;58:519-525.[Medline] [Order article via Infotrieve]
85.
Chen SH, Li XX, Liao WS, Wu JH, Chan L. RNA
editing of apolipoprotein B mRNA. Sequence specificity determined by in
vitro coupled transcription editing. J Biol
Chem.. 1990;265:6811-6816.
86.
Smith HC, Kuo SR, Backus JW, Harris SG, Sparks CE,
Sparks JD. In vitro apolipoprotein B mRNA editing:
identification of a 27S editing complex. Proc Natl Acad
Sci U S A.. 1991;88:1489-1493.
87. Hegele RA, Huang LS, Herbert PN. Apolipoprotein B gene DNA polymorphisms associated with myocardial infarction. N Engl J Med.. 1986;315:1509-1515.[Abstract]
88. Monsalve MV, Young R, Jobsis J, Wiseman SA, Dhamu S, Powell JT, Greenhalgh RM, Humphries SE. DNA polymorphism of the gene for apolipoprotein B in patients with peripheral arterial disease. Atherosclerosis.. 1988;70:123-129.[Medline] [Order article via Infotrieve]
89. Bohn M, Berg K. The XbaI polymorphism at the apolipoprotein B locus and risk of atherosclerotic disease. Clin Genet.. 1994;46:77-79.[Medline] [Order article via Infotrieve]
90. Hansen PS, Klausen IC, Lemming L, Gerdes LU, Gregersen N, Faergeman O. Apolipoprotein B gene polymorphisms in ischemic heart disease and hypercholesterolemia: effects of age and sex. Clin Genet.. 1994;45:78-83.[Medline] [Order article via Infotrieve]
91. Brown SA, Goldstein JL. Lipoprotein metabolism in the macrophage: implications for cholesterol deposition in atherosclerosis. Annu Rev Biochem.. 1983;52:223-261.[Medline] [Order article via Infotrieve]
92. Daugherty A, Lange LG, Sobel BE, Schonfeld G. Aortic accumulation and plasma clearance of beta-VLDL and HDL: effects of diet-induced hypercholesterolemia in rabbits. J Lipid Res.. 1985;26:955-963.[Abstract]
93. Tall AR. Plasma high density lipoproteins. Metabolism and relationship to atherogenesis. J Clin Invest.. 1990;86:379-384.
94. Fainaru M, Mahley RW, Hamilton RL, Innerarity TL. Structural and metabolic heterogeneity of beta-very low density lipoproteins from cholesterol-fed dogs and from humans with type III hyperlipoproteinemia. J Lipid Res.. 1982;23:701-714.
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