scholarly journals Conformation of apolipoprotein B after lipid extraction of low density lipoproteins attached to an electron microscope grid.

1989 ◽  
Vol 30 (3) ◽  
pp. 415-422
Author(s):  
M L Phillips ◽  
V N Schumaker
Keyword(s):  
Electron Microscope ◽  
Apolipoprotein B ◽  
Lipid Extraction ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Electron Microscope Grid ◽  
Microscope Grid

scholarly journals Limited proteolysis selectively destroys epitopes on apolipoprotein B in low density lipoproteins.

1983 ◽  
Vol 24 (7) ◽  
pp. 877-885
Author(s):  
K S Hahm ◽  
M J Tikkanen ◽  
R Dargar ◽  
T G Cole ◽  
J M Davie ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Limited Proteolysis ◽  
Low Density Lipoproteins ◽  
Low Density

Adsorption of Lipoprotein Containing Apolipoprotein-B through Plasma Separation for Treatment of Familial Hypercholesterolemia

1986 ◽  
Vol 9 (5) ◽  
pp. 343-348 ◽  
Author(s):  
M. Odaka ◽  
H. Kobayashi ◽  
K. Soeda ◽  
N. Murotani ◽  
Y. Saito ◽  
...  
Keyword(s):  
Total Cholesterol ◽  
Adsorption Capacity ◽  
Familial Hypercholesterolemia ◽  
Apolipoprotein B ◽  
Clinical Results ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Affinity Adsorbent ◽  
Excellent Selectivity

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.

scholarly journals The Assembly and Secretion of Apolipoprotein B-48-containing Very Low Density Lipoproteins in McA-RH7777 Cells

2000 ◽  
Vol 275 (14) ◽  
pp. 10506-10513 ◽  
Author(s):  
Pia Stillemark ◽  
Jan Borén ◽  
Maria Andersson ◽  
Thomas Larsson ◽  
Sabina Rustaeus ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins

scholarly journals Palmitoylation of Apolipoprotein B Is Required for Proper Intracellular Sorting and Transport of Cholesteroyl Esters and Triglycerides

2000 ◽  
Vol 11 (2) ◽  
pp. 721-734 ◽  
Author(s):  
Yang Zhao ◽  
James B. McCabe ◽  
Jean Vance ◽  
Luc G. Berthiaume
Keyword(s):  
Apolipoprotein B ◽  
Neutral Lipids ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Hydrophobic Core ◽  
Wild Type ◽  
Very Low Density Lipoproteins ◽  
Structural Requirement ◽  
Lipoprotein Particles ◽  
Intracellular Sorting

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.

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