LIPG encodes endothelial lipase, a secreted enzyme with dual enzymatic activity toward lipid substrates. It exerts both phospholipase and triglyceride lipase activities, functioning predominantly as a phospholipase [UniProt]. The enzyme hydrolyzes high-density lipoproteins (HDL) more efficiently than other lipoprotein fractions 12, and mediates HDL binding and selective cholesterol ester uptake independently of its catalytic activity 3. Beyond canonical lipid metabolism, LIPG has emerged as a multifunctional regulator in cancer biology. In triple-negative breast cancer, LIPG promotes tumorigenicity and metastasis through both lipase-dependent proliferation and lipase-independent functions affecting invasiveness and stemness via DTX3L-ISG15 signaling 4. In cervical squamous cell carcinoma, LIPG facilitates tumor progression by hydrolyzing phosphatidylcholine and activating MAPK-p38 signaling 5. In colorectal cancer, LIPG expression is negatively regulated by ZDHHC1, and elevated LIPG promotes cancer cell growth through altered lipid storage 6. Genetic variation in LIPG associates with plasma lipid levels and cardiovascular risk across populations. The rs9958947 promoter variant increases ischemic stroke risk in Asian populations 7, while the Thr111Ile polymorphism modulates HDL cholesterol associations in hyperlipidemic patients 8. These findings position LIPG as both a metabolic regulator and a potential therapeutic target in lipid-driven cancers.