High affinity binding of immunoglobulin G fragments to human polymorphonuclear leukocytes.
Human neutrophil elastase splits IgG into Fc, Fabc, and Fab fragments. The Fc and Fabc fragments bind with high affinity (KD 2.1 and 2.5 nM respectively) to a small number of binding sites (1175 and 1370 sites/cell respectively) on untreated human polymorphonuclear leukocytes. Molecular mass determination of the binding site by crosslinking of Fc fragments to the neutrophils followed by SDS electrophoresis yields one band corresponding to a molecular mass of 67 kDa for the binding site. Incubation of neutrophils with rIFN-gamma (50 ng/ml, 18 h, 37 degrees C) enhances the expression of binding sites by about 6 fold to about 14,500 sites/cell, while the binding affinity and the molecular mass of the ligand receptor complex remain constant. By comparison with known affinities of leukocyte Fc receptors it is concluded that IgG fragments bind to the high affinity FcRI receptor of human neutrophils.
Eckle
I
I
Zentrum für Innere Medizin, Phillipps-Universität, Marburg.
Reifer
R
R
Hoferichter
A
A
Kolb
G
G
Havemann
K
K
D002478:Cells, Cultured; D003432:Cross-Linking Reagents / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007371:Interferon-gamma / Q000378:metabolism*; D008970:Molecular Weight; D009504:Neutrophils / Q000276:immunology*; D011961:Receptors, Fc / Q000276:immunology / Q000378:metabolism*
D003432:Cross-Linking Reagents; D007074:Immunoglobulin G; D011961:Receptors, Fc; D007371:Interferon-gamma