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Effects of apolipoprotein structure on the kinetics of apolipoprotein transfer between phospholipid vesicles
Journal article   Peer reviewed

Effects of apolipoprotein structure on the kinetics of apolipoprotein transfer between phospholipid vesicles

Jamal A. Ibdah, Constance Smith, Sissel Lund-Katz, Michael C. Phillips and Cecilia M Smith
Biochimica et biophysica acta. Lipids and lipid metabolism, v 1081(2)
1991
DOI: https://doi.org/10.1016/0005-2760(91)90029-H
PMID: 1998741
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Apolipoprotein transfer Kinetic mechanism Phospholipid vesicle Unilamellar vesicle
The kinetics and mechanism of transfer of 14C-labeled human apolipoproteins A-I, A-II and C-III 1 between small unilamellar vesicles (SUV) have been investigated. Ion exchange chromatography was used for rapid separation of negatively charged egg phosphatidylcholine (PC)/dicetyl phosphate donor SUV containing bound 14C-labeled apoprotein from neutral egg PC acceptor SUV present in 10-fold molar excess. The transfer kinetics of these apolipoproteins at 37°C are consistent with the existence of fast, slow and apparently ‘nontransferrable’ pools of SUV-associated lipoprotein; the transfers from these pools occur on timescales of seconds (or less), minutes/hours and days/weeks, respectively. For donor SUV containing about 15 apoprotein molecules per vesicle and at a donor SUV concentration of 0.15 mg phospholipid/ml incubation mixture, the sizes of the fast kinetic pools for apolipoproteins A-I, A-II and C-III 1 associated with donor SUV are 2, 10 and 11%, respectively. The sizes of the slow kinetic pools for these apolipoproteins are 16, 71 and 50%, respectively. The transfer of the various apolipoproteins from the slow kinetic pool follows first order kinetics and the half-time ( t 1 2 ) values are in the order: apo C-III 1 < apo A-II < apo A-I. Increasing the number of apoprotein molecules per donor SUV enlarges the size of the fast pool and increases the t 1 2 of slow transfer. The differences in the kinetics of apolipoprotein transfer between SUV are consequences of the variations in the primary and secondary structures of the apolipoprotein molecules. The slow transfer of apoprotein molecules is mediated by collisions between donor and acceptor SUV; the rate is dependent on the apoprotein molecular weight with larger molecules transferring more slowly from donor SUV containing the same lipid/protein molar ratio. The hydrophobicity of the apoprotein molecule is also significant with less hydrophobic molecules transferring more rapidly. Further understanding of the differences in the kinetics of transfer of these apolipoproteins will require more knowledge of their secondary and tertiary structures.

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Collaboration types
Domestic collaboration
International collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
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