| | |  | | | | Record from Web of Science® | | | | | | |
| Mac-1 (CDllb/CD18) is an oligodeoxynucleotide-binding protein |
|
|
| Author(s): Benimetskaya L, Loike JD, Khaled Z, Loike G, Silverstein SC, Cao L, Khoury JE, Cai TQ, Stein CA |
| Source: NATURE MEDICINE Volume: 3 Issue: 4 Pages: 414-420 Published: APR 1997 |
| Times Cited: 159 References: 42 |
| Abstract: We have studied the interactions of phosphodiester and phosphorothioate oligodeoxynucleotides with Mac-1 (CD11b/CD18; alpha M beta 2), a heparin-binding integrin found predominately on the surface of polymorphonuclear leukocytes (PMNs), macrophages and natural killer cells. Binding of a homopolymer of thymidine occurred on both the alpha M and beta 2 subunits. Soluble fibrinogen, a natural ligand for Mac-1, was an excellent competitor of the binding of a phosphorothioate oligodeoxynucleotide to both TNF-alpha-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 beta 2-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 mediate their internalization and that this binding may have important functional consequences. |
| Document Type: Article |
| Language: English |
Addresses:
1. COLUMBIA UNIV COLL PHYS & SURG, NEW YORK, NY 10032 USA
2. ROCKEFELLER UNIV, CELLULAR PHYSIOL & IMMUNOL LAB, NEW YORK, NY 10021 USA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology; Medicine, Research & Experimental |
| IDS Number: WQ825 |
| ISSN: 1078-8956 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |