Application of 2-hydroxypropyl-β-cyclodextrin in the assay of acyl-CoA: cholesterol acyltransferase and neutral and acid cholesterol ester hydrolases

Lipids ◽  
1996 ◽  
Vol 31 (3) ◽  
pp. 323-329 ◽  
Author(s):  
Mariana Liza ◽  
José R. Romero ◽  
Yolanda Chico ◽  
Olatz Fresnedo ◽  
Begoña Ochoa
Keyword(s):  
Cholesterol Ester ◽  
Cholesterol Acyltransferase ◽  
Ester Hydrolases

Two cholesterol ester hydrolases

1977 ◽  
Vol 488 (3) ◽  
pp. 359-369 ◽  
Author(s):  
Matthew C. Riddle ◽  
Fujimoto Wilfred ◽  
Russell Ross
Keyword(s):  
Cholesterol Ester ◽  
Ester Hydrolases

scholarly journals Maturation of high-density lipoproteins

2009 ◽  
Vol 6 (39) ◽  
pp. 863-871 ◽  
Author(s):  
Amy Y. Shih ◽  
Stephen G. Sligar ◽  
Klaus Schulten
Keyword(s):  
Central Region ◽  
Cholesterol Ester ◽  
Structural Information ◽  
Level Structure ◽  
Cholesterol Acyltransferase ◽  
High Density ◽  
Coarse Grained ◽  
High Density Lipoproteins ◽  
Hydrophobic Core ◽  
Salt Bridges

Human high-density lipoproteins (HDLs) are involved in the transport of cholesterol. The mechanism by which HDL assembles and functions is not well understood owing to a lack of structural information on circulating spherical HDL. Here, we report a series of molecular dynamics simulations that describe the maturation of discoidal HDL into spherical HDL upon incorporation of cholesterol ester as well as the resulting atomic level structure of a mature circulating spherical HDL particle. Sixty cholesterol ester molecules were added in a stepwise fashion to a discoidal HDL particle containing two apolipoproteins wrapped around a 160 dipalmitoylphosphatidylcholine lipid bilayer. The resulting matured particle, captured in a coarse-grained description, was then described in a consistent all-atom representation and analysed in chemical detail. The simulations show that maturation results from the formation of a highly dynamic hydrophobic core comprised of cholesterol ester surrounded by phospholipid and protein; the two apolipoprotein strands remain in a belt-like conformation as seen in the discoidal HDL particle, but with flexible N- and C-terminal helices and a central region stabilized by salt bridges. In the otherwise flexible lipoproteins, a less mobile central region provides an ideal location to bind lecithin cholesterol acyltransferase, the key enzyme that converts cholesterol to cholesterol ester during HDL maturation.

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