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Papers In Press, published online ahead of print February 16, 2004
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University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7
Corresponding Author: dsparks{at}ottawaheart.ca
The effects of apolipoprotein (apo)A-II on the structure and stability of HDL has been investigated in reconstituted HDL particles (LpA-I). Purified human apoA-II was incorporated into sonicated, spherical LpA-I particles containing apoA-I, phospholipids (PC) and various amounts of triacylglycerol (TG), diacylglycerol (DG) and/or free cholesterol (FC). While addition of PC to apoA-I reduces the thermodynamic stability of its alpha-helices, PC has the opposite effect on apoA-II and significantly increases its helical stability. Similarly, substitution of apoA-I with various amounts of apoA-II significantly increases the thermodynamic stability of the particle alpha-helical structure. ApoA-II also increases the size and net negative charge of the lipoprotein particles. ApoA-II directly affects apoA-I conformation and increases the immunoreactivity of epitopes in the N- and C-terminus of apoA-I, but decreases the exposure of central domains in the molecule (residues 98-186). ApoA-II appears to increase hepatic lipase (HL) association with HDL and inhibits lipid hydrolysis. ApoA-II mildly inhibited PC hydrolysis in TG-enriched particles, but significantly inhibited DG hydrolysis in DG-rich LpA-I. In addition, apoA-II enhances the ability of reconstituted LpA-I particles to inhibit VLDL-TG hydrolysis by HL. ApoA-II therefore affects both the structure and dynamic behavior of HDL particles and selectively modifies lipid metabolism.
Revised on January 21, 2004
Accepted on February 2, 2004
Apolipoprotein A-II regulates HDL stability and affects hepatic lipase association and activity
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