Secreted Phospholipase A2-VII (sPLA2-VII), also known as Platelet-Activating Factor Acetylhydrolase (PAF-AH), is an enzyme encoded by the PLA2G7 gene in humans. This enzyme is part of the secreted phospholipases A2 (sPLA2) family, which plays a crucial role in lipid metabolism and inflammatory processes.
sPLA2-VII is a secreted enzyme that hydrolyzes the sn-2 ester bond of phospholipids, releasing free fatty acids and lysophospholipids. This hydrolytic activity is essential for the degradation of platelet-activating factor (PAF) and oxidized phospholipids in low-density lipoproteins (LDL), converting them into biologically inactive products . The enzyme is primarily produced by inflammatory cells and circulates in the blood, predominantly associated with LDL and to a lesser extent with high-density lipoproteins (HDL) .
The primary biological function of sPLA2-VII is to modulate inflammatory responses. By degrading PAF, a potent inflammatory mediator, sPLA2-VII helps regulate inflammation and immune responses. Additionally, the enzyme’s ability to hydrolyze oxidized phospholipids in LDL is crucial for preventing the formation of atherosclerotic plaques, thereby playing a protective role against cardiovascular diseases .
The recombinant form of sPLA2-VII, produced in Human Embryonic Kidney (HEK) cells, is widely used in research to study its structure, function, and role in various diseases. The recombinant enzyme retains the same biological activity as the native enzyme, making it a valuable tool for biochemical and pharmacological studies .
Given its role in modulating inflammation and preventing atherosclerosis, sPLA2-VII is a potential therapeutic target for treating inflammatory diseases and cardiovascular disorders. Inhibitors of sPLA2-VII are being explored as potential therapeutic agents to reduce inflammation and prevent the progression of atherosclerosis .