Preferential binding of [3H]cholesteryl linoleyl ether-HDL3 by bovine adrenal membranes.
Membranes isolated from bovine adrenal cortex, incubated with human high-density lipoproteins (HDL3), labeled with 125I and [3H]cholesteryl linoleyl ether, showed preferential binding of [3H]cholesteryl linoleyl ether. The preferential binding was Ca2+ independent, temperature sensitive and was slightly increased after phospholipase C or pronase treatment. Reduction of membrane phosphatidylcholine by phospholipase A2 resulted in a marked increase in the binding of the entire HDL3 particle and a relative decrease in preferential binding of [3H]cholesteryl linoleyl ether. These findings suggest that the presence of intact phospholipid in the membrane plays an important role in the magnitude of the preferential binding.
D000302:Adrenal Cortex / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D002784:Cholesterol / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008075:Lipoproteins, HDL / Q000378:metabolism*; D053440:Lipoproteins, HDL3; D010713:Phosphatidylcholines / Q000378:metabolism; D010741:Phospholipases A / Q000494:pharmacology; D054467:Phospholipases A2; D011402:Pronase / Q000494:pharmacology; D013696:Temperature; D010738:Type C Phospholipases / Q000494:pharmacology
D008075:Lipoproteins, HDL; D053440:Lipoproteins, HDL3; D010713:Phosphatidylcholines; C027575:cholesteryl linoleyl ether; D002784:Cholesterol; D010741:Phospholipases A; D054467:Phospholipases A2; D010738:Type C Phospholipases; D011402:Pronase