[Effects of induced deletion of repeats in binding domain of the VLDL receptor on its ligand-binding capacity].

The ligand-binding domain of the very low-density lipoprotein receptor (VLDL-R) contains eight cysteine-rich repeat sequences that have been postulated as ligand-binding sites. This is obviously different from that of low-density lipoprotein receptor (LDL-R) that includes seven similar repeats. To make clear the contribution of these repeats to ligand-binding and to explore the reason of both receptors' ligand-binding characteristic, the VLDL-R recombinants lacking different repeat(s) were constructed by oligonucleotide-directed mutagenesis and transfected into ldl-A7 cell.

Oxidative Modification of Very Low Density Lipoprotein by Arterial Wall Cells.

Modification of VLDL by arterial wall cells was observed. After incubating VLDL (200 &mgr;g protein/ml) with bovine aortic endothelial cells (EC), rabbit aortic smooth muscle cells (SMC) or mouse peritoneal macrophages (Mpsi)for 24 hours, the TBARS in VLDL increased strikingly to 7.80+/-O.