Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type III hyperlipoproteinemia.
ZS Ji, S Fazio, RW Mahley - Journal of Biological Chemistry, 1994 - ASBMB
The initial step in the clearance of apolipoprotein (apo) E-enriched remnant lipoproteins
from the plasma appears to be sequestration within the liver mediated by their binding to
heparan sulfate proteoglycans (HSPG). The surface-bound remnants are believed to be
internalized by their interaction with the low density lipoprotein (LDL) receptor-related
protein or by the LDL receptor. Cholesterol-induced rabbit beta-very low density lipoproteins
(beta-VLDL) enriched in human apoE3 display 4-5-fold enhanced binding to cultured cells …
from the plasma appears to be sequestration within the liver mediated by their binding to
heparan sulfate proteoglycans (HSPG). The surface-bound remnants are believed to be
internalized by their interaction with the low density lipoprotein (LDL) receptor-related
protein or by the LDL receptor. Cholesterol-induced rabbit beta-very low density lipoproteins
(beta-VLDL) enriched in human apoE3 display 4-5-fold enhanced binding to cultured cells …