The nature of the receptor for complement (C3b) in the human renal glomerulus.
The physicochemical nature of the human glomerular complement receptor was studied. Receptor activity was measured by determining the avidity of glomeruli of normal human renal tissue for fluorescein-labeled bacteria (S.typhi) coated with C3b. Maximal binding of C3b-coated bacteria to normal human glomeruli took place in phosphate-saline buffers of pH 6.5 and 0.08 to 0.15 mu ionic strength. Pretreatment of renal tissue with neuraminidase enhanced receptor activity. On the other hand, binding of C3b-coated bacteria to the glomeruli was diminished by pretreatment of the tissue with proteolytic enzymes, phospholipase C and certain lipid solvents. The binding of C3b-coated bacteria to the glomeruli was also diminished by pretreatment of the tissue with fluid-phase C3b, or by pretreatment of the bacteria with C3b inactivator. Normal human serum and purified fluid-phase C3 or the absence of magnesium and calcium ions had little effect on glomerular complement receptor activity.
D001666:Binding Sites, Antibody / Q000187:drug effects; D002648:Child; D003179:Complement C3b; D003180:Complement C3b Inactivator Proteins / Q000494:pharmacology; D046508:Culture Techniques; D006801:Humans; D007678:Kidney Glomerulus / Q000276:immunology*; D009439:Neuraminidase / Q000494:pharmacology; D010206:Papain / Q000494:pharmacology; D010740:Phospholipases / Q000494:pharmacology; D012485:Salmonella typhi / Q000276:immunology; D012997:Solvents / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
D003180:Complement C3b Inactivator Proteins; D012997:Solvents; D003179:Complement C3b; D010740:Phospholipases; D009439:Neuraminidase; D014357:Trypsin; D010206:Papain