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Cholesterol esterase: a cholesterol transfer protein

S C Myers-Payne1, D Y Hui, H L Brockman

  • 1Department of Physiology and Pharmacology, Texas A&M University, TVMC, College Station 77843-4466.

Biochemistry
|March 28, 1995
PubMed
Summary
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Rat pancreatic cholesterol esterase enhances sterol transfer between lipid vesicles containing negatively charged phospholipids. This activity is independent of the enzyme's catalytic function, highlighting a novel mechanism for lipid interactions.

Area of Science:

  • Biochemistry
  • Lipid Metabolism
  • Enzymology

Background:

  • Cholesterol esterase plays a role in lipid metabolism.
  • Understanding its mechanism in sterol transfer is crucial.
  • The role of phospholipids in enzyme-mediated sterol exchange is not fully elucidated.

Purpose of the Study:

  • To investigate the role of rat pancreatic cholesterol esterase in sterol transfer between small unilamellar vesicles (SUVs).
  • To determine the influence of negatively charged phospholipids on cholesterol esterase-mediated sterol exchange.
  • To assess whether esterasic activity is required for cholesterol esterase's effect on sterol transfer.

Main Methods:

  • Utilized a novel assay to measure sterol exchange between SUVs without vesicle separation.

Related Experiment Videos

  • Employed SUVs composed of phosphatidylcholine with or without phosphatidylserine or phosphatidic acid.
  • Investigated enzyme adsorption to lipid monolayers and used a catalytically inactive mutant enzyme.

    • Main Results:

    • Cholesterol esterase significantly enhanced sterol transfer in SUVs containing phosphatidylserine and phosphatidic acid.
    • The enzyme increased the initial rate of sterol transfer by approximately 80% in phosphatidic acid-containing SUVs.
    • Cholesterol esterase's sterol transfer activity was ineffective in the absence of negatively charged phospholipids and independent of its esterasic function.

    Conclusions:

    • Rat pancreatic cholesterol esterase enhances sterol transfer in SUVs containing negatively charged phospholipids.
    • Negatively charged phospholipids are essential for enzyme adsorption to lipid interfaces and subsequent sterol transfer.
    • The sterol transfer-promoting activity of cholesterol esterase is independent of its catalytic esterasic activity.