ATP-dependent translocation of amino phospholipids across the human erythrocyte membrane.
Trace amounts of radiolabeled phospholipids were inserted into the outer membrane leaflet of intact human erythrocytes, using a non-specific lipid transfer protein. Phosphatidylcholine, phosphatidylserine and phosphatidylethanolamine were transferred from the donor lipid vesicles to the membrane of the intact red cell with equal ease, whilst sphingomyelin was transferred 6-times less efficiently. The transbilayer mobility and equilibrium distribution of the labeled phospholipids were assessed by treatment of the intact cells with phospholipases. In fresh erythrocytes, the labeled amino phospholipids appeared to move rapidly towards the inner leaflet. The choline phospholipids, on the other hand, approached an equilibrium distribution which strongly favoured the outer leaflet. In ATP-depleted erythrocytes, the relocation of the amino phospholipids was markedly retarded.
D000255:Adenosine Triphosphate / Q000502:physiology*; D002352:Carrier Proteins / Q000502:physiology*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D010713:Phosphatidylcholines / Q000097:blood; D010714:Phosphatidylethanolamines / Q000097:blood; D010718:Phosphatidylserines / Q000097:blood; D010740:Phospholipases; D010743:Phospholipids / Q000097:blood*; D013109:Sphingomyelins / Q000097:blood
D002352:Carrier Proteins; C511922:GLTP protein, human; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010718:Phosphatidylserines; D010743:Phospholipids; D013109:Sphingomyelins; C030363:lipid transfer protein; D000255:Adenosine Triphosphate; D010740:Phospholipases