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Details on Person Lipoprotein lipase (LPL) and hepatic triacylglycerol lipase ...

Class:IdSummation:8963895
_displayNameLipoprotein lipase (LPL) and hepatic triacylglycerol lipase ...
_timestamp2024-02-17 18:51:36
created[InstanceEdit:8963894] D'Eustachio, Peter, 2017-02-13
modified[InstanceEdit:8963908] D'Eustachio, Peter, 2017-02-13
[InstanceEdit:9861376] D'Eustachio, Peter, 2024-02-17
textLipoprotein lipase (LPL) and hepatic triacylglycerol lipase (LIPC) enzymes on the lumenal surfaces of capillary endothelia mediate the hydrolysis of triglyceride molecules in circulating lipoprotein particles.
LPL is widely expressed in the body and is especially abundant in adipocytes and skeletal and cardiac myocytes. Activation of the protein requires glycosylation, dimerization, and glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1), which delivers it to heparan sulfate proteoglycan (HSPG) associated with the plasma membrane. It is inactivated by proteolytic cleavage (Berryman & Bensadoun 1995; Sukonina et al. 2006; Young et al. 2011).
Expression of the LPL gene is transcriptionally regulated by Cyclic AMP-responsive element-binding protein 3-like protein 3 (CREB3L3), which also regulates the expression of APOA4, APOA5, APOC2, CIDEC and FGF21 (Lee et al. 2011).
Maturation of LIPC enzyme requires association with LMF1 protein (or possibly, inferred from sequence similarity, LMF2). Heparin binding stabilizes LIPC in its active dimeric form (Babilonia-Rosa & Neher 2014).
(summation)[Pathway:8963889] Assembly of active LPL and LIPC lipase complexes [Homo sapiens]
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