title: Molecular Model of Plasma PAF Acetylhydrolase-Lipoprotein Association: Insights from the Structure.
abstract: Plasma platelet-activating factor acetylhydrolase (PAF-AH), also called lipoprotein-associated phospholipase A₂ (Lp-PLA₂), is a group VIIA PLA₂ 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.
authors.affiliation: Department of Chemistry & Biochemistry, University of Delaware, Newark, DE, 19716, USA.
authors.forename: Prabhavathi
authors.initials: P
authors.lastname: Srinivasan
authors.affiliation: Department of Chemistry & Biochemistry, University of Delaware, Newark, DE, 19716, USA. bahnson@udel.edu.
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Bahnson
keywords: Lp-PLA2; PAF-AH; group VIIA PLA2; i-face; lipoprotein