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- W2052534903 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." @default.
- W2052534903 created "2016-06-24" @default.
- W2052534903 creator A5088960519 @default.
- W2052534903 creator A5089162499 @default.
- W2052534903 date "2010-03-08" @default.
- W2052534903 modified "2023-10-14" @default.
- W2052534903 title "Molecular Model of Plasma PAF Acetylhydrolase-Lipoprotein Association: Insights from the Structure" @default.
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- W2052534903 doi "https://doi.org/10.3390/ph3030541" @default.
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