Key result
In vitro, lipoprotein lipase induced catabolism of normal human triglyceride-rich lipoproteins via the LDL receptor-related protein, a process requiring cell-surface proteoglycans.
Population
Cultured mutant fibroblasts lacking LDL receptors
Design
Preclinical
Authors
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Hypothesis-generating for LRP-mediated lipoprotein clearance; leaves open in vivo relevance and clinical translation.
This in vitro study establishes that lipoprotein lipase induces the catabolism of triglyceride-rich lipoproteins via the LDL receptor-related protein (LRP), facilitated by cell-surface proteoglycans.
Chappell et al. (1993) studied this question. Lipoprotein lipase was evaluated on Binding, uptake, and degradation of 125I-labeled normal human triglyceride-rich lipoproteins. In vitro, lipoprotein lipase induced catabolism of normal human triglyceride-rich lipoproteins via the LDL receptor-related protein, a process requiring cell-surface proteoglycans.
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