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Cholesterol Binding and Cholesterol Transport Proteins: pp 183–227Cite as

High Density Lipoprotein Structure–Function and Role in Reverse Cholesterol Transport

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Part of the book series: Subcellular Biochemistry ((SCBI,volume 51))

Abstract

High density lipoprotein (HDL) possesses important anti-atherogenic properties and this review addresses the molecular mechanisms underlying these functions. The structures and cholesterol transport abilities of HDL particles are determined by the properties of their exchangeable apolipoprotein (apo) components. ApoA-I and apoE, which are the best characterized in structural terms, contain a series of amphipathic α-helical repeats. The helices located in the amino-terminal two-thirds of the molecule adopt a helix bundle structure while the carboxy-terminal segment forms a separately folded, relatively disorganized, domain. The latter domain initiates lipid binding and this interaction induces changes in conformation; the α-helix content increases and the amino-terminal helix bundle can open subsequently. These conformational changes alter the abilities of apoA-I and apoE to function as ligands for their receptors. The apoA-I and apoE molecules possess detergent-like properties and they can solubilize vesicular phospholipid to create discoidal HDL particles with hydrodynamic diameters of ~10 nm. In the case of apoA-I, such a particle is stabilized by two protein molecules arranged in an anti-parallel, double-belt, conformation around the edge of the disc. The abilities of apoA-I and apoE to solubilize phospholipid and stabilize HDL particles enable these proteins to be partners with ABCA1 in mediating efflux of cellular phospholipid and cholesterol, and the biogenesis of HDL particles. ApoA-I-containing nascent HDL particles play a critical role in cholesterol transport in the circulation whereas apoE-containing HDL particles mediate cholesterol transport in the brain. The mechanisms by which HDL particles are remodeled by lipases and lipid transfer proteins, and interact with SR-BI to deliver cholesterol to cells, are reviewed.

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Abbreviations

ANS:

8-anilino-1-napthalenesulfonic acid

AP:

acute phase

apo:

apolipoprotein

CE:

cholesterol ester

CETP:

cholesteryl ester transfer protein

DMPC:

dimyristoyl PC

EL:

endothelial lipase

FC:

free (unesterified) cholesterol

HDL:

high density lipoprotein

HL:

hepatic lipase

LCAT:

lecithin-cholesterol acyltransferase

LDL:

low density lipoprotein

LUV:

large unilamellar vesicle

MLV:

multilamellar vesicle

PC:

phosphatidylcholine

PL:

phospholipid

PLTP:

phospholipid transfer protein

RCT:

reverse cholesterol transport

SAA:

serum amyloid A

SUV:

small unilamellar vesicle

TAG:

triacylglycerol

VLDL:

very low density lipoprotein

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Acknowledgements

We are indebted to all our colleagues for their valuable contributions to the studies from our laboratory described here. Our research reported here was supported by NIH Grants HL22633 and HL 56083.

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  1. Division of Gastroenterology/Hepatology/Nutrition, Children’s Hospital of Philadelphia, University of Pennsylvania School of Medicine, 3615 Civic Center Blvd, Suite 1102, Philadelphia, PA, 19104-4318, USA

    Sissel Lund-Katz

  2. The Children’s Hospital of Philadelphia, Philadelphia, PA, 19104-4318, USA

    Michael C. Phillips

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  1. Sissel Lund-Katz
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    J. Robin Harris

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Lund-Katz, S., Phillips, M.C. (2010). High Density Lipoprotein Structure–Function and Role in Reverse Cholesterol Transport. In: Harris, J. (eds) Cholesterol Binding and Cholesterol Transport Proteins:. Subcellular Biochemistry, vol 51. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-8622-8_7

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