An interaction between CD16 and CR3 enhances iC3b binding to CR3 but is lost during differentiation of monocytes into dendritic cells.

@article{PreynatSeauve2004AnIB,
  title={An interaction between CD16 and CR3 enhances iC3b binding to CR3 but is lost during differentiation of monocytes into dendritic cells.},
  author={Olivier Preynat-Seauve and Christian L. Villiers and Guillaume Jourdan and M. -F. Richard and Jo{\"e}l Plumas and Alain Favier and Patrice N Marche and M. Favrot},
  journal={European journal of immunology},
  year={2004},
  volume={34 1},
  pages={147-55}
}
The receptor for the iC3b fragment of complement, CR3, is involved in monocytes/macrophages and neutrophils phagocytosis. CR3 is known to interact with the low affinity receptor for Ig (CD16) and previous studies have suggested that this cooperation modulates CR3 functions. Herein we have studied the effect of CD16 on the ability of human monocytes CR3 to bind to iC3b. We show that iC3b binding to CR3 is inhibited by several reagents that are known to dissociate the CD16/CR3 complex. In… CONTINUE READING

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