Lipid Apheresis by Hemoperfusion: In Vitro Efficacy and Ex Vivo Biocompatibility of a New Low-Density Lipoprotein Adsorber Compatible with Human Whole Blood

2008 ◽  
Vol 17 (7) ◽  
pp. 640-652 ◽  
Author(s):  
T. Bosch ◽  
B. Schmidt ◽  
M. Blumenstein ◽  
H.-J. Gurland
2000 ◽  
Vol 46 (4) ◽  
pp. 199-204 ◽  
Author(s):  
Reiko HIRANO ◽  
Naomi OSAKABE ◽  
Tamami IWAMOTO ◽  
Akiyo MATSUMOTO ◽  
Midori NATSUME ◽  
...  

1992 ◽  
Vol 20 (3) ◽  
pp. 340-347 ◽  
Author(s):  
Christine Breugnot ◽  
Jean Pierre Iliou ◽  
Sylvie Privat ◽  
Frédéric Robin ◽  
Jean Paul Vilaine ◽  
...  

Platelets ◽  
1993 ◽  
Vol 4 (1) ◽  
pp. 11-15 ◽  
Author(s):  
A. Bröijersén ◽  
N. H. Wallén ◽  
S. Vitols ◽  
P. T. Larsson ◽  
P. Hjemdahl

1999 ◽  
Vol 58 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Ingeborg R Brude ◽  
Christian A Drevon ◽  
Kjersti Viken ◽  
Jon E Arnstad ◽  
Kolbjørn N Valnes ◽  
...  

2003 ◽  
Vol 71 (6) ◽  
pp. 3280-3284 ◽  
Author(s):  
Johannes H. M. Levels ◽  
Philip R. Abraham ◽  
Erik P. van Barreveld ◽  
Joost C. M. Meijers ◽  
Sander J. H. van Deventer

ABSTRACT Lipoteichoic acid (LTA), a major cell wall component of gram-positive bacteria, is an amphipathic anionic glycolipid with structural similarities to lipopolysaccharide (LPS) from gram-negative bacteria. LTA has been implicated as one of the primary immunostimulatory components that may trigger the systemic inflammatory response syndrome. Plasma lipoproteins have been shown to sequester LPS, which results in attenuation of the host response to infection, but little is known about the LTA binding characteristics of plasma lipid particles. In this study, we have examined the LTA binding capacities and association kinetics of the major lipoprotein classes under simulated physiological conditions in human whole blood (ex vivo) by using biologically active, fluorescently labeled LTA and high-performance gel permeation chromatography. The average distribution of an LTA preparation from Staphylococcus aureus in whole blood from 10 human volunteers revealed that >95% of the LTA was associated with total plasma lipoproteins in the following proportions: high-density lipoprotein (HDL), 68% ± 10%; low-density lipoprotein (LDL), 28% ± 8%; and very low density lipoprotein (VLDL), 4% ± 5%. The saturation capacity of lipoproteins for LTA was in excess of 150 μg/ml. The LTA distribution was temperature dependent, with an optimal binding between 22 and 37°C. The binding of LTA by lipoproteins was essentially complete within 10 min and was followed by a subsequent redistribution from HDL and VLDL to LDL. We conclude that HDL has the highest binding capacity for LTA and propose that the loading and redistribution of LTA among plasma lipoproteins is a specific process that closely resembles that previously described for LPS (J. H. M. Levels, P. R. Abraham, A. van den Ende, and S. J. H. van Deventer, Infect. Immun. 68:2821-2828, 2001).


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