Mac-1 (CD11b/CD18) is an oligodeoxynucleotide-binding protein
Author: ["Lyuba Benimetskaya","John D. Loike","Zahangir Khaled","Gila LoiKe","Samuel C. Silverstein","Long Cao","Joseph E.L. Khoury","Tian-Quan CaI","C.A. Stein"]
Publication: Nature Medicine
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Abstract
We have studied the interactions of phosphodiester and phosphorothioate oligodeoxynucleotides with Mac-1 (CD11b/CD18; αMβ2), a heparin-binding integrin found predominately on the surface of polymorphonuciear leukocytes (PMNs), macrophages and natural killer cells. Binding of a homopolymer of thymidine occurred on both the αM and β2 subunits. Soluble fibrinogen, a natural figand for Mac-1, was an excellent competitor of the binding of a phosphorothioate oligodeoxynucleotide to both TNF-α-activated and nonactivated PMNs. Upregulation of cell-surface Mac-1 expression increased cell-surface binding of oligodeoxynucleotides. Binding was inhibited by anti-Mac-1 monoclonal antibodies, and the increase in cell-surface binding was correlated with a three- to fourfold increase in internalization by PMNs. An oligodeoxynucleotide inhibited β2-dependent migration through Matrigel, but the production of reactive oxygen species in PMNs adherent to fibrinogen dramatically increased. Thus, our data demonstrate that Mac-1 is a cell-surface receptor for oligodeoxynucleotides that can medi ate their internalization and that this binding may have important functional consequences.
Cite this article
Benimetskaya, L., Loike, J., Khaled, Z. et al. Mac-1 (CD11b/CD18) is an oligodeoxynucleotide-binding protein. Nat Med 3, 414–420 (1997). https://doi.org/10.1038/nm0497-414
