Influence of phospholipid structure on sterol efflux induced by albumin-phospholipid complexes.
Sterol release from strain L fibroblasts was measured in serum-free medium supplemented with delipidated human serum albumin and various phospholipids. The sterol molecule appears to preferentially interact with the sn-2-acyl chain of the phospholipid. The carbonyl oxygen of the phospholipid acyl ester linkage is not required for sterol-phospholipid interactions, while the phosphate and choline groups are required. In the presence of the human serum albumin-phospholipid complex, phospholipids containing trans-acyl groups are significantly more effective at removing cellular sterol than the corresponding cis-acyl group.
D000215:Acylation; D000818:Animals; D005347:Fibroblasts / Q000378:metabolism; D006736:Horses; D006801:Humans; D007739:L Cells; D008563:Membrane Lipids / Q000378:metabolism*; D051379:Mice; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013261:Sterols / Q000378:metabolism*; D013329:Structure-Activity Relationship
D008563:Membrane Lipids; D010743:Phospholipids; D012709:Serum Albumin; D013261:Sterols