Intermembrane cholesterol transfer: role of sterol carrier proteins and phosphatidylserine.

Abstract:

:The effect of phosphatidylserine and sterol carrier proteins on cholesterol exchange was determined using an assay not requiring separation of donor and acceptor membrane vesicles. Sterol carrier protein-2 (SCP2, also called nonspecific lipid transfer protein), but not fatty acid binding protein (FABP, also called sterol carrier protein), enhanced the initial rate of sterol exchange between neutral zwitterionic phosphatidylcholine small unilamellar vesicles (SUV) 2.3-fold. Phosphatidylserine at 10 mol% increased the initial rate of spontaneous and of SCP2-mediated (but not FABP-mediated) sterol exchange by 22% and 44-fold, respectively. The SCP2 potentiation of sterol transfer was dependent on SCP2 concentration and on phosphatidylserine concentration. The SCP2-mediated sterol transfer was inhibited by a variety of cations including KCl, divalent metal ions, and neomycin. The data suggest that SCP2 increase in activity for sterol transfer may be partly ascribed to charge on the phospholipid.

journal_name

Lipids

journal_title

Lipids

authors

Schroeder F,Butko P,Hapala I,Scallen TJ

doi

10.1007/BF02544032

subject

Has Abstract

pub_date

1990-11-01 00:00:00

pages

669-74

issue

11

eissn

0024-4201

issn

1558-9307

journal_volume

25

pub_type

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