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

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.

authors

• Schroeder, Friedhelm

published proceedings

• Lipids

author list (cited authors)

• Schroeder, F., Butko, P., Hapala, I., & Scallen, T. J.

citation count

• 33

complete list of authors

• Schroeder, F||Butko, P||Hapala, I||Scallen, TJ

publication date

• November 1990

publisher

• Wiley  Publisher

published in

• Lipids  Journal

keywords

• Biological Transport
• Carrier Proteins
• Cholesterol
• Ergosterol
• Fatty Acid-binding Proteins
• Fluorescence Polarization
• Membranes, Artificial
• Models, Chemical
• Neoplasm Proteins
• Nephelometry And Turbidimetry
• Phosphatidylserines
• Plant Proteins

Digital Object Identifier (DOI)

• 10.1007/BF02544032

start page

• 669

end page

• 674

volume

• 25

issue

• 11

URL

• http://dx.doi.org/10.1007/bf02544032