Two populations of complement factor H differ in their ability to bind to cell surfaces.
Using hydrophobic affinity chromatography on phenyl-Sepharose, human complement factor H can be separated into two subpopulations, phi 1 and phi 2. Although phi 1 and phi 2 are known to differ in their aggregation properties under non-physiological low ionic strength conditions, no difference in aggregation state was detected under the conditions used for cell-binding experiments. We have investigated these two subpopulations further to determine whether functional differences exist between them. The subpopulation phi 2 was found to bind specifically and saturably to the surface of Raji cells. The binding of the other subpopulation, phi 1, was low, and essentially non-specific. A monoclonal anti-factor H antibody, BGH-1, was raised which recognizes preferentially the phi 2 subpopulation and inhibits the binding of factor H to cell surfaces.
Ripoche
J
J
INSERM U78 543, Chemin de la Breteque, Bois-Guillaume, France.
Erdei
A
A
Gilbert
D
D
Al Salihi
A
A
Sim
R B
RB
Fontaine
M
M
D000911:Antibodies, Monoclonal; D002460:Cell Line; D003180:Complement C3b Inactivator Proteins / Q000378:metabolism*; D017242:Complement Factor H; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D046911:Macromolecular Substances; D011485:Protein Binding
D000911:Antibodies, Monoclonal; C493495:CFH protein, human; D003180:Complement C3b Inactivator Proteins; D046911:Macromolecular Substances; D017242:Complement Factor H