Key result
Lipoprotein lipase increased cellular degradation of Lp(a) and LDL by 277% and 32.5%, respectively, and cell association by 509% and 83.9%, promoting binding to heparan sulfate proteoglycans.
Population
Mutant Chinese hamster ovary cells and HepG2 cells
Design
Preclinical
Authors
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Animal data implicate LpL in Lp(a) clearance via HSPGs; leaves open relevance to human atherosclerosis.
LpL promotes binding of apolipoprotein B-100-rich lipoproteins to cell surface heparan sulfate proteoglycans, representing a novel catabolic mechanism for cellular accumulation of cholesteryl ester-rich lipoproteins.
Williams et al. (1992) studied Cellular metabolism of lipoproteins. Lipoprotein lipase (LpL) was evaluated on Cellular degradation and cell association of Lp(a) and LDL. Lipoprotein lipase increased cellular degradation of Lp(a) and LDL by 277% and 32.5%, respectively, and cell association by 509% and 83.9%, promoting binding to heparan sulfate proteoglycans.
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