Lipoprotein lipase facilitates very low density lipoprotein binding to the subendothelial cell matrix.
The effect of bovine lipoprotein lipase (LPL) on very low density lipoprotein (VLDL) binding to subendothelial matrix was studied. Without LPL, VLDL bound poorly to the matrix. However, decreasing NaCl or elevating Ca++ concentration increased matrix VLDL binding. With LPL, VLDL binding was markedly increased. Since LPL is a normal constituent of the artery wall and is elevated in atherosclerotic lesions, we postulate two potential mechanisms for the involvement of VLDL and LPL in atherogenesis. First, VLDL acquisition is attenuated by the increased matrix LPL content in the developing atheroma. Secondly, elevated plasma levels of VLDL (and VLDL remnants) such as in Type II or III dyslipidemia could enhance such interactions. These events likely accelerate the rate of atherosclerosis lesion development.
Saxena
U
U
Department of Pharmacology, Parke-Davis Pharmaceutical Research, Warner-Lambert Company, Ann Arbor, MI 48105.
Ferguson
E
E
Auerbach
B J
BJ
Bisgaier
C L
CL
D000818:Animals; D001011:Aorta / Q000187:drug effects / Q000378:metabolism*; D002417:Cattle; D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000187:drug effects / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000302:isolation & purification / Q000494:pharmacology*; D008079:Lipoproteins, VLDL / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D008892:Milk / Q000201:enzymology; D011485:Protein Binding; D013552:Swine
D008079:Lipoproteins, VLDL; D008071:Lipoprotein Lipase