Hepatic triacylglycerol lipase (LIPC, and lipoprotein lipase...

created [InstanceEdit:6785192] Jassal, Bijay, 2015-06-25
dbId 6785176
displayName Hepatic triacylglycerol lipase (LIPC, and lipoprotein lipase...
modified [InstanceEdit:9863299] May, Bruce, 2024-02-28
schemaClass Summation
text Hepatic triacylglycerol lipase (LIPC, and lipoprotein lipase, LPL) are dimeric lipases (Hill et al. 1997) that hydrolyse triglycerides from circulating lipoproteins thereby playing important roles in lipoprotein remodeling and uptake. LIPC dimer (as well as LPL dimer) binds to an ER membrane protein known as lipase maturation factor 1 (LMF1) which can mediate secretion and enzymatic maturation of these lipases. Human LMF1 contain five TM segments that divide the protein into six separate domains with cytoplasmic and ER lumenal orientation thereby transporting LIPC dimer from ER lumen to the cytosol. The mechanism of LIPC dimer translocation from cytosol to secretion is unknown (Babilonia-Rosa & Neher 2014). Another family member, LMF2, may function as LMF1 based on similarity. Defects in LMF1 can cause combined lipase deficiency (CLD; MIM:246650), characterised by hypertriglyceridemia caused by ER retention of both LIPC dimer and LPL dimer (Peterfy et al. 2007).
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