Endothelial lipase

Endothelial Lipase
Identifiers
SymbolLIPG
Alt. symbolsEL
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Endothelial lipase (LIPG) is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and vascularization, such as the liver, lung, kidney, and thyroid gland.[1] The LIPG enzyme is a vital component to many biological processes. These processes include lipoprotein metabolism, cytokine expression, and lipid composition in cells.[1] Unlike the lipases that hydrolyze Triglycerides, endothelial lipase primarily hydrolyzes phospholipids.[1] Due to the hydrolysis specificity, endothelial lipase contributes to multiple vital systems within the body. On the contrary to the beneficial roles that LIPG plays within the body, endothelial lipase is thought to play a potential role in cancer and inflammation.[1] Knowledge obtained in vitro and in vivo suggest the relations to these conditions, but human interaction knowledge lacks due to the recent discovery of endothelial lipase.[2] Endothelial lipase was first characterized in 1999.[3] The two independent research groups which are notable for this discovery cloned the endothelial lipase gene and identified the novel lipase secreted from endothelial cells.[2] The anti-Atherosclerosis opportunity through alleviating plaque blockage and prospective ability to raise High-density lipoprotein (HDL) have gained endothelial lipase recognition.[4]

  1. ^ a b c d Yu JE, Han SY, Wolfson B, Zhou Q (January 2018). "The role of endothelial lipase in lipid metabolism, inflammation, and cancer". Histology and Histopathology. 33 (1): 1–10. doi:10.14670/HH-11-905. PMC 5858721. PMID 28540715.
  2. ^ a b Paradis ME, Lamarche B (February 2006). "Endothelial lipase: its role in cardiovascular disease". The Canadian Journal of Cardiology. 22 Suppl B (Suppl B): 31B–34B. doi:10.1016/S0828-282X(06)70984-9. PMC 2780840. PMID 16498510.
  3. ^ Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ (April 1999). "A novel endothelial-derived lipase that modulates HDL metabolism". Nature Genetics. 21 (4): 424–8. doi:10.1038/7766. PMID 10192396. S2CID 20658953.
  4. ^ Darrow AL, Olson MW, Xin H, Burke SL, Smith C, Schalk-Hihi C, Williams R, Bayoumy SS, Deckman IC, Todd MJ, Damiano BP, Connelly MA (February 2011). "A novel fluorogenic substrate for the measurement of endothelial lipase activity". Journal of Lipid Research. 52 (2): 374–82. doi:10.1194/jlr.D007971. PMC 3023558. PMID 21062953.