PMID: 9555948Apr 29, 1998Paper

Chylomicron remnant uptake is regulated by the expression and function of heparan sulfate proteoglycan in hepatocytes.

Journal of Lipid Research
B J ZengT G Redgrave

Abstract

Chylomicron remnants transport cholesterol from the intestine, and are removed from the circulation principally by the liver. While hepatic receptors, including the low density lipoprotein (LDL) receptor account for endocytosis, heparan sulfate proteoglycans (HSPG) participate in the initial binding of remnants to liver cells. To explore the interactions between HSPG and endocytosis of remnants, in the present study the expression of HSPG was inhibited in HepG2 cells transfected by a synthetic antisense oligodeoxynucleotide SYN5. Immunofluorescent staining by a monoclonal anti-syndecan antibody showed significant reduction in the expression of syndecan in SYN5-treated cells compared with control cells. Remnant binding decreased by about 50-70% in SYN5-transfected cells. Monoclonal antibodies to either heparan sulphate or the LDL receptor decreased binding by about 60-65%. The glycosylation inhibitor beta-nitrophenylxylopyranoside inhibited remnant uptake by 25%, whereas 4-nitrophenyl-beta-D-galactopyranoside had no effect on remnant binding. Heparinase completely abolished binding at appropriate concentrations. Heparitinase was less effective than hep arinase in inhibiting remnant binding. Suramin completely abolished the remna...Continue Reading

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