%0 Journal Article
%T Molecular Model of Plasma PAF Acetylhydrolase-Lipoprotein Association: Insights from the Structure
%A Prabhavathi Srinivasan
%A Brian J. Bahnson
%J Pharmaceuticals
%D 2010
%I MDPI AG
%R 10.3390/ph3030541
%X Plasma platelet-activating factor acetylhydrolase (PAF-AH), also called lipoprotein-associated phospholipase A 2 (Lp-PLA 2), is a group VIIA PLA 2 enzyme that catalyzes the hydrolysis of PAF and certain oxidized phospholipids. Although the role of PAF-AH as a pro- or anti-atherosclerotic enzyme is highly debated, several studies have shown it to be an independent marker of cardiovascular diseases. In humans the majority of plasma PAF-AH is bound to LDL and a smaller portion to HDL; the majority of the enzyme being associated with small dense LDL and VHDL-1 subclasses. Several studies suggest that the anti- or pro-atherosclerotic tendency of PAF-AH might be dependent on the type of lipoprotein it is associated with. Amino acid residues in PAF-AH necessary for binding to LDL and HDL have been identified. However our understanding of the interaction of PAF-AH with LDL and HDL is still incomplete. In this review we present an overview of what is already known about the interaction of PAF-AH with lipoprotein particles, and we pose questions that are yet to be answered. The recently solved crystal structure of PAF-AH, along with functional work done by others is used as a guide to develop a model of interaction of PAF-AH with lipoprotein particles.
%K PAF-AH
%K Lp-PLA2
%K group VIIA PLA2
%K lipoprotein
%K i-face
%U http://www.mdpi.com/1424-8247/3/3/541