Sterol release in mammalian cells. The role of a liposomal-free albumin-phospholipid complex.
Human serum albumin, the purity of which was confirmed by two-dimensional gel electrophoresis and high-pressure liquid chromatography, is able to bind dipalmitoyl phosphatidylcholine and the resulting albumin-phospholipid complex can cause marked sterol release from animal and human cells in tissue culture. The complex-induced sterol release was synergistic, exceeding by 4--5-fold the sum of sterol release in the presence of albumin and phospholipid individually. Isolation of the albumin-phospholipid complex by gel permeation chromatography yielded a liposomal-free fraction which caused full sterol release. No synergistic release of sterol occurred when cells were incubated with human serum albumin and dilinoleoyl phosphatidylcholine.
D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007739:L Cells / Q000378:metabolism*; D051379:Mice; D011663:Pulmonary Surfactants / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D013261:Sterols / Q000378:metabolism*
D011663:Pulmonary Surfactants; D012709:Serum Albumin; D013261:Sterols