title: LDL receptor-independent and -dependent uptake of lipoproteins.
abstract: The liver plays a decisive role in the regulation of the plasma levels of atherogenic lipoproteins. The primary liver interaction site for chylomicron-remnants and VLDL remnants (beta-VLDL) is still unidentified, while the subsequent cellular uptake is likely to be mediated in concert by the LDL receptor related protein (LRP) and the LDL receptor. The nature of the primary interaction site of remnants (remnant-receptor) might be a liver-specific proteoglycan or a liver-specific protein. Atherogenic modified LDL can be recognized by a family of scavenger-receptors. A newly identified 95-kDa protein forms the most likely candidate for mediating the in vivo uptake of oxidized LDL from the circulation and might thus protect the body against the presence of oxidized LDL in the blood compartment.
authors.affiliation: Division of Biopharmaceutics, University of Leiden, Netherlands.
authors.forename: T J
authors.initials: TJ
authors.lastname: van Berkel
authors.forename: K
authors.initials: K
authors.lastname: Fluiter
authors.forename: A G
authors.initials: AG
authors.lastname: van Velzen
authors.forename: C J
authors.initials: CJ
authors.lastname: Vogelezang
authors.forename: G J
authors.initials: GJ
authors.lastname: Ziere
mesh_terms: D000818:Animals; D001161:Arteriosclerosis / Q000097:blood* / Q000209:etiology / Q000473:pathology; D008074:Lipoproteins / Q000097:blood*; D008099:Liver / Q000378:metabolism; D011973:Receptors, LDL / Q000378:metabolism*
chemical_list: D008074:Lipoproteins; D011973:Receptors, LDL