Title : Heparan sulfate-dependent and low density lipoprotein receptor-related protein-dependent catabolic pathways for lipoprotein lipase in mouse embryonic fibroblasts.

Pub. Date : 1996 Jun

PMID : 8682650






6 Functional Relationships(s)
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1 Heparan sulfate-dependent and low density lipoprotein receptor-related protein-dependent catabolic pathways for lipoprotein lipase in mouse embryonic fibroblasts. Heparitin Sulfate lipoprotein lipase Mus musculus
2 Heparan sulfate and low density lipoprotein receptor related protein (LRP) have been shown to participate in the uptake and degradation of the enzyme lipoprotein lipase (LPL). Heparitin Sulfate lipoprotein lipase Mus musculus
3 Heparan sulfate and low density lipoprotein receptor related protein (LRP) have been shown to participate in the uptake and degradation of the enzyme lipoprotein lipase (LPL). Heparitin Sulfate lipoprotein lipase Mus musculus
4 Assuming that a) heparinase treatment abolished the heparan-sulfate pathway, and that b) the degradation remaining in heparin-treated cultures represents nonspecific values, it appears that heparan sulfate contributes about 61%, 83% and 95% of total LPL degradation, whereas the LRP pathway contributes 39%, 17% and less than 5% of LPL degradation in MEF, PEA-10 and PEA-13 cells, respectively. Heparitin Sulfate lipoprotein lipase Mus musculus
5 Assuming that a) heparinase treatment abolished the heparan-sulfate pathway, and that b) the degradation remaining in heparin-treated cultures represents nonspecific values, it appears that heparan sulfate contributes about 61%, 83% and 95% of total LPL degradation, whereas the LRP pathway contributes 39%, 17% and less than 5% of LPL degradation in MEF, PEA-10 and PEA-13 cells, respectively. Heparitin Sulfate lipoprotein lipase Mus musculus
6 In addition, the data indicate that LPL interaction with heparan sulfate and the LRP pathways is independent of each other. Heparitin Sulfate lipoprotein lipase Mus musculus