Measurement of (C13)arginine incorporation into apolipoprotein B-100 in very low density lipoproteins and low density lipoproteins in normal subjects using (13C)sodium bicarbonate infusion and isotope ratio mass spectrometry

1990 ◽  
Vol 19 (8) ◽  
pp. 459-464 ◽  
Author(s):  
Michael J. Bennett ◽  
Dennis R. Cryer ◽  
Marc Yudkoff ◽  
Paul M. Coates ◽  
Jean A. Cortner ◽  
...  
1986 ◽  
Vol 9 (5) ◽  
pp. 343-348 ◽  
Author(s):  
M. Odaka ◽  
H. Kobayashi ◽  
K. Soeda ◽  
N. Murotani ◽  
Y. Saito ◽  
...  

For the treatment of familial hypercholesterolemia, Liposorber LA-40 was clinically applied. The Liposorber is a commercially developed affinity adsorbent for plasma perfusion which selectivily adsorbs low density lipoproteins and very low density lipoproteins and is specially designed for plasmapheretic treatment of hypercholesterolemia. The Liposorber column, containing activated cellulose beads having an affinity for liporpotein containing apolipoprotein-B, has an excellent adsorption capacity, excellent selectivity, minimum albumin loss. This new apheresis system was applied to 2 clinical cases. After seven months of trial perfusion every 2 weeks, patient condition was good, with a level of total cholesterol under 300 mg/dl. No replacement fluids were given during or after treatment. In this paper, clinical results of these patients were shown and the mechanism of adsorption of this specific adsorbent was discussed.


1984 ◽  
Vol 30 (3) ◽  
pp. 349-351 ◽  
Author(s):  
M J Bugugnani ◽  
M Koffigan ◽  
I Kora ◽  
D Ouvry ◽  
V Clavey ◽  
...  

Abstract We describe an isoelectric-focusing method for rapidly separating and quantifying apolipoprotein (apo) C-II and C-III subspecies of triglyceride-rich lipoproteins. Concentrated very-low-density lipoproteins (VLDL) or delipidated apo VLDL are focused on dry acrylamide plates, after their rehydration with ampholytes and urea. Apo C-II and apo C-III in VLDL are resolved into four major bands--C-II (pI 5.01), C-III0 (pI 5.10), C-III1 (pl 4.92), and C-III2 (pI 4.84)--at the same pI values as for purified apo C. This precise technique can be used without delipidating VLDL. The relative percentage of C apoproteins found in VLDL from plasma of normal subjects agreed with previously published data. The ratio of apo C-II to apo C-III decreased in patients with chronic renal failure or with coronary artery disease.


2000 ◽  
Vol 275 (14) ◽  
pp. 10506-10513 ◽  
Author(s):  
Pia Stillemark ◽  
Jan Borén ◽  
Maria Andersson ◽  
Thomas Larsson ◽  
Sabina Rustaeus ◽  
...  

2000 ◽  
Vol 11 (2) ◽  
pp. 721-734 ◽  
Author(s):  
Yang Zhao ◽  
James B. McCabe ◽  
Jean Vance ◽  
Luc G. Berthiaume

Apolipoprotein B (apoB) is an essential component of chylomicrons, very low density lipoproteins, and low density lipoproteins. ApoB is a palmitoylated protein. To investigate the role of palmitoylation in lipoprotein function, a palmitoylation site was mapped to Cys-1085 and removed by mutagenesis. Secreted lipoprotein particles formed by nonpalmitoylated apoB were smaller and denser and failed to assemble a proper hydrophobic core. Indeed, the relative concentrations of nonpolar lipids were three to four times lower in lipoprotein particles containing mutant apoB compared with those containing wild-type apoB, whereas levels of polar lipids isolated from wild-type or mutant apoB lipoprotein particles appeared identical. Palmitoylation localized apoB to large vesicular structures corresponding to a subcompartment of the endoplasmic reticulum, where addition of neutral lipids was postulated to occur. In contrast, nonpalmitoylated apoB was concentrated in a dense perinuclear area corresponding to the Golgi compartment. The involvement of palmitoylation as a structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle and its intracellular sorting represent novel roles for this posttranslational modification.


1984 ◽  
Vol 218 (1) ◽  
pp. 101-111 ◽  
Author(s):  
A K Soutar ◽  
B L Knight

Human blood monocyte-derived macrophages that had been cultured in medium containing human serum for 7 days degraded the abnormal very-low-density lipoproteins (VLDL) from the plasma of subjects with type III hyperlipoproteinaemia by two distinct saturable processes. One process was stimulated when cells from normal subjects were preincubated with lipoprotein-free medium, was inhibited by excess unlabelled low-density lipoproteins (LDL) and was absent from cells from subjects with homozygous familial hypercholesterolaemia; on these criteria it was identified as an LDL-receptor-dependent process. Degradation by the second process was of equal magnitude in both cell types and was unaffected by excess unlabelled LDL or acetylated LDL. The activity of this process was reduced when the cells were preincubated in lipoprotein-free medium. The abnormal VLDL from the plasma of cholesterol-fed rabbits were also degraded by this process, which was similar to that in mouse peritoneal macrophages mediated by the receptor for VLDL of beta-electrophoretic mobility [Goldstein, Ho, Brown, Innerarity & Mahley (1980) J. Biol. Chem. 255, 1839-1848].


1979 ◽  
Vol 25 (2) ◽  
pp. 221-226 ◽  
Author(s):  
C C Heuck ◽  
G Schlierf

Abstract We studied the development of light scattering in the reaction between anti-apolipoprotein B and apolipoprotein B in intact very-low-density lipoproteins (I) and low-density lipoproteins (II) as well as in lipoproteins treated with lipases, and found considerable differences in the kinetics of the immunoreaction for the two lipoprotein classes. Pre-incubation with triglyceride lipase and cholesterol esterase caused a decrease of final light scattering in I but only minimal changes in the reaction with II. Non-ionic detergent not only decreased the original light scattering in hyperlipemic serum samples, but also accelerated the immunoreaction. Under standardized conditions, results of quantitative nephelometry correlated highly significantly with quantitative determination of apolipoprotein B by radial immunodiffusion, both for normolipemic and hyperlipoproteinemic serum samples. The nonspecific light scattering caused by neutral lipids in intact lipoproteins could be minimized when samples were pre-incubated with lipolytic enzymes.


Sign in / Sign up

Export Citation Format

Share Document