Evidence for an interaction of lipoprotein lipase with artery wall proteoglycans.
1. Artery wall proteoglycans-lipoprotein lipase binding characteristics were studied using bovine milk 125I-labelled lipoprotein lipase (LPL) and chondroitin sulphate-dermatan sulphate proteoglycans (PGs) purified from pig aorta. 2. The binding process was studied either by a soluble assay (gel filtration) or by an immobilized proteoglycan assay (ELISA). 3. The binding process was reversible, saturable and occurred at a stoichiometry 1:1. 4. The binding process involved ionic interactions between the positively charged groups of LPL and the negatively charged groups of PG carbohydrate chains. 5. The complex PG-LPL may lead to the production of remnant lipoproteins and, thereby, contribute to cholesteryl ester accumulation in the arterial wall.
Laboratoire de Biochimie, INSERM U 181, Faculté de Médecine Saint-Antoine, Paris, France.
D
D
Margelin
A M
AM
Pigier
J
J
Gardette
J
J
Bertrand
N
N
Vu-Dac
J
J
Picard
D000818:Animals; D001011:Aorta / Q000378:metabolism*; D001667:Binding, Competitive; D002412:Cations / Q000494:pharmacology; D002850:Chromatography, Gel; D004797:Enzyme-Linked Immunosorbent Assay; D066298:In Vitro Techniques; D008071:Lipoprotein Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008892:Milk / Q000201:enzymology; D011485:Protein Binding; D011509:Proteoglycans / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
D002412:Cations; D011509:Proteoglycans; D008071:Lipoprotein Lipase