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J. Biol. Chem., Vol. 264, Issue 9, 4818-4824, 03, 1989
A Jonas, KE Kezdy and JH Wald
We prepared and isolated defined, reconstituted high density lipoprotein
(r-HDL) particles containing apolipoprotein A-I (apoA-I),
palmitoyloleoylphosphatidylcholine, and cholesterol. The initial r-HDL were
prepared by the sodium cholate method, then part of the preparation was
depleted of phospholipid by exposure to LDL, and the resulting, stable
r-HDL species were isolated by gel filtration. The isolated r-HDL were
characterized in terms of their size, alpha-helix content, and the
conformation of apoA-I as reported by the fluorescence properties of the
tryptophan residues. Then the relative reactivity of the r-HDL with
lecithin cholesterol acyltransferase was assessed. The isolated, discoidal
r-HDL contained 2 and 3 apoA-I molecules/particle, and had 77 and 109 A
diameters, respectively. Their spectral properties were essentially
identical and were distinct from the larger particles in the class of r-HDL
with 2 apoA-I molecules/particle (particles with diameters of 86 and 96 A).
In addition, the reactivity of the 77 and 109 A particles with pure
lecithin cholesterol acyltransferase was similar and about 10-fold lower
than for the 86 and 96 A particles. We conclude that the stable, limiting
r-HDL particles in each class (77 and 109 A) can arise from the larger
particles of the same class by depletion of phospholipids. These limiting
particles have very similar apoA-I conformations, with decreased
alpha-helix contents and compact protein regions, that are very poor in
activating lecithin cholesterol acyltransferase. Based on these results, we
propose a model to explain the origin of the different classes and
subclasses of the discoidal r- HDL particles.
Defined apolipoprotein A-I conformations in reconstituted high density lipoprotein discs
Department of Biochemistry, College of Medicine at Urbana-Champaign, Illinois 61801.
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K. L. Gillotte, W. S. Davidson, S. Lund-Katz, G. H. Rothblat, and M. C. Phillips Apolipoprotein A-I Structural Modification and the Functionality of Reconstituted High Density Lipoprotein Particles in Cellular Cholesterol Efflux J. Biol. Chem., September 27, 1996; 271(39): 23792 - 23798. [Abstract] [Full Text] [PDF]
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D. J. Bolin and A. Jonas Sphingomyelin Inhibits the Lecithin-Cholesterol Acyltransferase Reaction with Reconstituted High Density Lipoproteins by Decreasing Enzyme Binding J. Biol. Chem., August 9, 1996; 271(32): 19152 - 19158. [Abstract] [Full Text] [PDF]
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K.-A. Rye, N. J. Hime, and P. J. Barter The Influence of Sphingomyelin on the Structure and Function of Reconstituted High Density Lipoproteins J. Biol. Chem., February 23, 1996; 271(8): 4243 - 4250. [Abstract] [Full Text] [PDF]
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J. Bergeron, P. G. Frank, D. Scales, Q.-H. Meng, G. Castro, and Y. L. Marcel Apolipoprotein A-I Conformation in Reconstituted Discoidal Lipoproteins Varying in Phospholipid and Cholesterol Content J. Biol. Chem., November 17, 1995; 270(46): 27429 - 27438. [Abstract] [Full Text] [PDF]
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D. L. Sparks, W. S. Davidson, S. Lund-Katz, and M. C. Phillips Effects of the Neutral Lipid Content of High Density Lipoprotein on Apolipoprotein A-I Structure and Particle Stability J. Biol. Chem., November 10, 1995; 270(45): 26910 - 26917. [Abstract] [Full Text] [PDF]
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W. S. Davidson, W. V. Rodrigueza, S. Lund-Katz, W. J. Johnson, G. H. Rothblat, and M. C. Phillips Effects of Acceptor Particle Size on the Efflux of Cellular Free Cholesterol J. Biol. Chem., July 21, 1995; 270(29): 17106 - 17113. [Abstract] [Full Text] [PDF]
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W. S. Davidson, K. L. Gillotte, S. Lund-Katz, W. J. Johnson, G. H. Rothblat, and M. C. Phillips The Effect of High Density Lipoprotein Phospholipid Acyl Chain Composition on the Efflux of Cellular Free Cholesterol J. Biol. Chem., March 17, 1995; 270(11): 5882 - 5890. [Abstract] [Full Text] [PDF]
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D. L. Sparks, G. M. Anantharamaiah, J. P. Segrest, and M. C. Phillips Effect of the Cholesterol Content of Reconstituted LpA-I on Lecithin:Cholesterol Acyltransferase Activity J. Biol. Chem., March 10, 1995; 270(10): 5151 - 5157. [Abstract] [Full Text] [PDF]
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Q.-H. Meng, D. L. Sparks, and Y. L. Marcel Effect of LpA-I Composition and Structure on Cholesterol Transfer between Lipoproteins J. Biol. Chem., March 3, 1995; 270(9): 4280 - 4287. [Abstract] [Full Text] [PDF]
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J. N. Maiorano and W. S. Davidson The Orientation of Helix 4 in Apolipoprotein A-I-containing Reconstituted High Density Lipoproteins J. Biol. Chem., June 2, 2000; 275(23): 17374 - 17380. [Abstract] [Full Text] [PDF]
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D. Sviridov, A. Hoang, W. H. Sawyer, and N. H. Fidge Identification of a Sequence of Apolipoprotein A-I Associated with the Activation of Lecithin:Cholesterol Acyltransferase J. Biol. Chem., June 23, 2000; 275(26): 19707 - 19712. [Abstract] [Full Text] [PDF]
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K. N. Liadaki, T. Liu, S. Xu, B. Y. Ishida, P. N. Duchateaux, J. P. Krieger, J. Kane, M. Krieger, and V. I. Zannis Binding of High Density Lipoprotein (HDL) and Discoidal Reconstituted HDL to the HDL Receptor Scavenger Receptor Class B Type I. EFFECT OF LIPID ASSOCIATION AND APOA-I MUTATIONS ON RECEPTOR BINDING J. Biol. Chem., July 7, 2000; 275(28): 21262 - 21271. [Abstract] [Full Text] [PDF]
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K.-H. Cho and A. Jonas A Key Point Mutation (V156E) Affects the Structure and Functions of Human Apolipoprotein A-I J. Biol. Chem., August 25, 2000; 275(35): 26821 - 26827. [Abstract] [Full Text] [PDF]
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B. Corsico, J. D. Toledo, and H. A. Garda Evidence for a Central Apolipoprotein A-I Domain Loosely Bound to Lipids in Discoidal Lipoproteins That Is Capable of Penetrating the Bilayer of Phospholipid Vesicles J. Biol. Chem., May 11, 2001; 276(20): 16978 - 16985. [Abstract] [Full Text] [PDF]
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