Complement activation by liposome-encapsulated hemoglobin in vitro: the role of endotoxin contamination.
Incubation of liposome-encapsulated Hb (LEH) with rat serum at 37 degrees C led to accelerated decay of serum hemolytic complement (C) activity (CH50/ml). Empty liposomes (L) caused less decrease of CH50/ml, whereas free Hb had no effect on C activity. The LEH- and L-induced increases in C consumption were unlikely a consequence of endotoxin (LPS) contamination, as spiking of rat serum with LPS caused reduction in C only at levels significantly higher than those detectable in LEH or L. LPS-induced C consumption was not potentiated by free hemoglobin.
D000818:Animals; D003165:Complement System Proteins / Q000187:drug effects*; D004339:Drug Compounding; D004731:Endotoxins / Q000494:pharmacology*; D006454:Hemoglobins / Q000008:administration & dosage*; D008070:Lipopolysaccharides; D008081:Liposomes; D051381:Rats
D004731:Endotoxins; D006454:Hemoglobins; D008070:Lipopolysaccharides; D008081:Liposomes; D003165:Complement System Proteins