Effector-target interactions: saturability, affinity and binding isotherms. A study of such interactions in the human NK cell-K562 tumour cell system.
Effector-target interactions at the cell-to-cell level have been studied. This has revealed that saturability, i.e., the existence of a finite number of specific receptor sites, applies to both the effector and target cell populations and plays a key role in the formation of conjugates. As a result, two maximum conjugate frequencies, alpha max and beta max, are recognised for the effector and target cell populations, respectively. The dissociation constant of the conjugates formed, KD, characterizes effector-target affinity. This constant, together with the maximum conjugate frequencies, are the three parameters which make it possible to describe the binding process quantitatively. The existence of binding isotherms for effector-target interactions has been demonstrated. These isotherms contain all the relevant information necessary to interpret quantitatively the formation of conjugates. Quantitative procedures to determine the three binding parameters are described together with the modifications necessary to use Scatchard plots in the analysis of conjugate frequencies in these kinds of cell-to-cell interactions. A quantitative study of these interactions in the NK-K562 tumour cell system has been performed. For this purpose, nine different cell source donors were used to test the model proposed. Relationships with related phenomena--CMC and the adhesion process--are also discussed.
Garcia-Peñarrubia
P
P
Department of Biochemistry and Molecular Biology, School of Medicine, Murcia, Spain.
Cabrera
L
L
Alvarez
R
R
Galvez
J
J
D000328:Adult; D000911:Antibodies, Monoclonal; D001665:Binding Sites / Q000276:immunology; D002448:Cell Adhesion / Q000276:immunology; D003602:Cytotoxicity, Immunologic / Q000276:immunology*; D006801:Humans; D007694:Killer Cells, Natural / Q000276:immunology*; D007700:Kinetics; D008433:Mathematics; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal