Key result
Inhibition of endothelial lipase by intravenous infusion of a specific polyclonal antibody increased HDL cholesterol levels by 25–60% in wild-type, hepatic lipase knockout, and human apoA-I transgenic mice.
Why the study?
Does inhibition of endothelial lipase increase HDL cholesterol levels in mice?
Does inhibition of endothelial lipase increase HDL cholesterol levels in mice?
Effect estimate: 25-60% increase across models
Absolute Event Rate: 92.8% vs 70.7%
p-value: p=<0.001
Inhibition of endothelial lipase in vivo significantly increases HDL cholesterol levels and slows HDL phospholipid turnover, demonstrating that endothelial lipase is a key physiological regulator of HDL metabolism.
Supports endothelial lipase inhibition for HDL elevation in mice; leaves open translation to humans or clinical outcomes.
Endothelial lipase (EL) is a recently discovered member of the triglyceride lipase gene family (1, 2). EL is highly homologous to lipoprotein lipase (LPL) and hepatic lipase (HL), both of which are known to hydrolyze lipids within lipoproteins and thereby influence their metabolism. EL has been shown to effectively hydrolyze HDL phospholipids in vitro (3), and overexpression of human EL in mouse liver markedly reduced plasma HDL cholesterol (HDL-C) levels in vivo (1). These data suggested that EL might play a physiological role in modulating HDL metabolism. However, proof of that concept requires an assessing the effect of reduction of EL activity in vivo.
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Jin et al. (2003) studied HDL metabolism (n=42). Anti-murine endothelial lipase (mEL) polyclonal antibody vs. Control rabbit IgG (1 mg) was evaluated on Plasma HDL cholesterol (HDL-C) levels at 48 hours (wild-type mice) (25-60% increase across models, p=<0.001). Inhibition of endothelial lipase by intravenous infusion of a specific polyclonal antibody increased HDL cholesterol levels by 25–60% in wild-type, hepatic lipase knockout, and human apoA-I transgenic mice.
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