Lpl, or Lipoprotein lipase, is a critical enzyme in humans. It hydrolyzes triglycerides from the cores of circulating plasma lipoproteins, and via its catalytic and non-catalytic functions, interacts with receptors to mediate lipoprotein uptake, thus playing a key role in lipid homeostasis and directing lipid distribution. It is involved in the intravascular processing of triglyceride-rich lipoproteins (TRLs), which is essential for delivering dietary lipids to tissues for energy metabolism or storage [2,4].

In Gpihbp1-deficient mouse models, suckling mice with high hepatic Lpl expression did not develop hypertriglyceridemia (HTG), while those without it developed severe HTG after weaning. AAV-mediated liver-targeted Lpl expression dose-dependently decreased plasma TG levels in Gpihbp1-deficient mice and rats, increased post-heparin plasma Lpl mass and activity, decreased mortality in rat pups, and reduced the susceptibility and severity of HTG-related acute pancreatitis (HTG-AP) [1]. In addition, ANGPTL4 was found to regulate intracapillary Lpl levels in brown adipose tissue in mice at thermoneutral temperatures, affecting TRL margination [3].

In conclusion, Lpl is essential for lipid metabolism and maintaining normal plasma triglyceride levels. Studies using gene-knockout mouse models, such as Gpihbp1-deficient mice, have revealed its role in preventing HTG and HTG-AP. Understanding Lpl's function can potentially provide new therapeutic approaches for lipid-related diseases.