Stimulation by target cell membrane lipid of actin polymerization and phagocytosis by Entamoeba histolytica.
The identity of molecules of mammalian target cells that stimulate contact-dependent attack by Entamoeba histolytica was sought using human erythrocytes (RBC) as a model. Protein-free liposomes prepared from RBC membrane lipids stimulated the same rapid E. histolytica actin polymerization and phagocytosis as did whole target cells. Liposomes constructed from the major phospholipids of RBC stimulated these responses but only if a negatively charged phospholipid was included. The addition to these liposomes of digalactosyl diglyceride significantly enhanced their stimulatory activity. The results demonstrate that ligands that trigger attack-related responses by E. histolytica reside in the target cell membrane lipid fraction and suggest roles for both glycolipid and phospholipid components.
D008841:Actin Cytoskeleton / Q000502:physiology; D000199:Actins / Q000502:physiology*; D004705:Endocytosis; D004748:Entamoeba histolytica / Q000502:physiology*; D004912:Erythrocytes / Q000502:physiology*; D006017:Glycolipids / Q000502:physiology; D008081:Liposomes; D008563:Membrane Lipids / Q000502:physiology*; D010587:Phagocytosis; D010743:Phospholipids / Q000502:physiology; D011956:Receptors, Cell Surface / Q000502:physiology
D000199:Actins; D006017:Glycolipids; D008081:Liposomes; D008563:Membrane Lipids; D010743:Phospholipids; D011956:Receptors, Cell Surface