title: Size of the transmembrane channels produced by complement proteins C5b-8.
abstract: It has been shown previously that erythrocytes can be lysed by complement proteins C5b-8, albeit at a much lower rate than C5b-9. We have now performed kinetic sieving experiments with resealed erythrocyte ghosts using sucrose (0.9 nm molecular diameter) and inulin (3.0 nm molecular diameter) as markers. We found that treatment of the ghosts with C5b-8 released sucrose, but not inulin. Addition of C9 to ghosts carrying C5b-8 dramatically increased the rate of sucrose flux and, in addition, caused release of inulin. Hence, unlike C5b-9 channels, those formed by C5b-8 measure less than 3 nm in diameter. Formation of C5b-8 channels was very slow compared with that of C5b-9 channels. Also, we found that about two-thirds of the C5b-8 ghosts did not have sucrose-releasing channels, but such channels were formed on reaction with C9.
mesh_terms: D002463:Cell Membrane Permeability; D003182:Complement C5; D003183:Complement C6; D003184:Complement C7; D003185:Complement C8; D003165:Complement System Proteins / Q000502:physiology*; D004910:Erythrocyte Membrane; D007444:Inulin; D007473:Ion Channels / Q000648:ultrastructure*; D013329:Structure-Activity Relationship; D013395:Sucrose
chemical_list: D003182:Complement C5; D003183:Complement C6; D003184:Complement C7; D003185:Complement C8; D007473:Ion Channels; D013395:Sucrose; D007444:Inulin; D003165:Complement System Proteins