Kinetic analysis of histamine release due to covalently linked IgE dimers.
We present a kinetic model of histamine release from human basophils due to covalently linked IgE dimers. Comparison of theory with experiment shows that the model gives a good description of histamine release by IgE dimers and allows a number of the parameters of the model to be determined. Comparison with previous models of release by conventional antigens indicates that despite their covalent structure, IgE dimers are subject to the same laws governing inactivation as are antigen produced crosslinks. In addition, the kinetic equation which relates the rate of histamine release to the number of crosslinked Fc epsilon receptors per cell is the same for crosslinks formed by IgE dimers as for antigen induced crosslinks. Quantitative fitting of histamine release data also yields a value for the rate constant for crosslink formation by IgE dimer on the cell surface (rx approximately 5 x 10(-10) cm2/sec). This rate constant is remarkably high and indicates that the reaction is diffusion controlled.
D001491:Basophils / Q000276:immunology; D003432:Cross-Linking Reagents; D004120:Dimethyl Suberimidate / Q000494:pharmacology; D006636:Histamine Release; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D007700:Kinetics; D008954:Models, Biological; D011961:Receptors, Fc / Q000276:immunology
D003432:Cross-Linking Reagents; D011961:Receptors, Fc; D004120:Dimethyl Suberimidate; D007073:Immunoglobulin E