Measurement of outward translocation of phospholipids across human erythrocyte membrane.
Spin-labeled phospholipids have been used to study the outside----inside and inside----outside transport of phospholipids across the human erythrocyte membrane at 37 degrees C. As already shown, inward transport is much faster for aminophospholipids than for phosphatidylcholine. In addition, we show here that outward transport of the phosphatidylserine and phosphatidylethanolamine analogues is three to four times faster than that of phosphatidylcholine. Magnesium depletion of the erythrocytes considerably decreases the outward rate of both aminophospholipids to values close to that of phosphatidylcholine. These results suggest that the outward aminophospholipid translocation is, at least partly, protein mediated. The protein involved could be identical to the inward Mg-ATP-dependent aminophospholipid carrier.
D000465:Algorithms; D000001:Calcimycin / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000097:blood; D010743:Phospholipids / Q000097:blood*; D013113:Spin Labels / Q000378:metabolism
D010743:Phospholipids; D013113:Spin Labels; D000001:Calcimycin; D008274:Magnesium