Speciated Human High-Density Lipoprotein Protein Proximity Profiles

Gauthamadasa, Kekulawalage; Rosales, Corina; Pownall, Henry J.; Macha, Stephen F.; Jerome, W. Gray; Huang, Rong; Silva, R. A. Gangani D.

doi:10.1021/bi1015452

Cited by 26 publications

(67 citation statements)

References 58 publications

(126 reference statements)

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“…On the other hand, the entire population of LpA-I:A-II demonstrates the presence of only two apoA-I molecules per particle, while the number of apoA-II molecules varies from one dimeric apoA-II to two and then to three. Upon compositional analyses of individual subpopulations, LpA-I:A-II exhibits comparable proportions for major lipid classes across subfractions, while LpA-I components show significant variability (Gauthamadasa et al 2010).…”

Section: Heterogeneity In Hdl Proteinsmentioning

confidence: 99%

“…LpA-I particles can be further subfractionated according to size. The number of apoA-I molecules in such subpopulations is increased from two to three to four with an increase in the particle size (Gauthamadasa et al 2010). On the other hand, the entire population of LpA-I:A-II demonstrates the presence of only two apoA-I molecules per particle, while the number of apoA-II molecules varies from one dimeric apoA-II to two and then to three.…”

Section: Heterogeneity In Hdl Proteinsmentioning

confidence: 99%

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Structure of HDL: Particle Subclasses and Molecular Components

Kontush

Lindahl

Lhomme

et al. 2014

Handbook of Experimental Pharmacology

216

226

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Section: Heterogeneity In Hdl Proteinsmentioning

confidence: 99%

Section: Heterogeneity In Hdl Proteinsmentioning

confidence: 99%

Structure of HDL: Particle Subclasses and Molecular Components

Kontush

Lindahl

Lhomme

et al. 2014

Handbook of Experimental Pharmacology

216

226

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“…In addition, there is production of ‫ف‬ 7 nm diameter lipid-poor apoA-I (pre-␤ 1-HDL) that comprises an apoA-I monomer associated with three to nine PL molecules and one or two FC molecules ( 114,117 ). The population of nascent HDL particles is heterogeneous regardless of the cell type in which the ABCA1 is located, and the particles of different sizes are apolipoprotein cross-linking shows contain up to four proximal apoA-I molecules, LpA-I+A-II particles contain only two proximal apoA-I molecules and up to three proximal dimeric apoA-II molecules ( 6 ).…”

Section: Apoa-i Organization In Spherical Hdlmentioning

confidence: 99%

New insights into the determination of HDL structure by apolipoproteins

Phillips

2013

Journal of Lipid Research

149

106

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This article is available online at http://www.jlr.orgThe purpose of this review is to summarize current understanding of how apolipoproteins (apoA-I in particular) determine the structures of HDL particles. The focus is on recent advances in the fi eld, so the coverage of the literature on HDL structure is not comprehensive. Knowledge of HDL structure at the molecular level is critical for understanding how this lipoprotein achieves the multiple functions elaborated in other reviews in this thematic series.In human plasma, HDL is a heterogeneous collection of particles ranging 7-12 nm in diameter and 1.063-1.21 g/ml in density ( 1-4 ). The predominant species of HDL are spherical microemulsion particles, in which a core of neutral cholesteryl ester (CE) and triacylglycerol (TG) is encapsulated by a monolayer of phospholipid (PL), unesterifi ed (free) cholesterol (FC), and protein ( 5 ). The protein and PL constituents comprise approximately 50 and 25%, respectively, of the mass of such particles, with the CE, FC, and TG components making up the remainder. Larger, less dense HDL particles have a higher lipidto-protein mass ratio. Approximately 70% of total plasma HDL protein is apoA-I (which is present in normolipidemic human plasma at ‫ف‬ 130 mg/dl), and it is located in essentially every HDL particle. The second most abundant protein is apoA-II, which comprises 15-20% of total plasma HDL protein, but this component is not present in all HDL particles. In human plasma, about 25% of apoA-I is present in HDL particles containing only apoA-I (LpA-I); the remaining HDL particles contain both apoA-I and apoA-II (LpA-I+A-II), typically in a molar ratio of 1-2/1 ( 6 ). ApoA-I and apoA-II are the "scaffold" proteins that primarily determine HDL particle structure. Other members of the exchangeable apolipoprotein gene family that are Abstract Apolipoprotein (apo)A-I is the principal protein component of HDL, and because of its conformational adaptability, it can stabilize all HDL subclasses. The amphipathic ␣ -helix is the structural motif that enables apoA-I to achieve this functionality. In the lipid-free state, the helical segments unfold and refold in seconds and are located in the N-terminal two thirds of the molecule where they are loosely packed as a dynamic, four-helix bundle. The C-terminal third of the protein forms an intrinsically disordered domain that mediates initial binding to phospholipid surfaces, which occurs with coupled ␣ -helix formation. The lipid affi nity of apoA-I confers detergent-like properties; it can solubilize vesicular phospholipids to create discoidal HDL particles with diameters of approximately 10 nm. Such particles contain a segment of phospholipid bilayer and are stabilized by two apoA-I molecules that are arranged in an anti-parallel, double-belt conformation around the edge of the disc, shielding the hydrophobic phospholipid acyl chains from exposure to water. The apoA-I molecules are in a highly dynamic state, and they stabilize discoidal particles of different sizes by certain s...

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“…Individual NDGGE subspecies bands, particularly those containing apoA-I but no apoA-II, are generally broad, suggesting a mixture of minor protein components. We included the effects of one molecule of apoC-III, the longest and most abundant of the apoCs, on calculated diameter of the 4:0 stoichiometry for the double-shell model; the resulting value stays well within the broad size distribution of HDL [7]. We also included the effects of one molecule of apoE on the calculated diameter of the 4:0 stoichiometry for the double-shell model; the resulting value falls just outside the broad size distribution of HDL [7].…”

Section: Calculations Of the Stoichiometry And Dimensions Of Reconstimentioning

confidence: 99%