Sammanfattning
| Originalspråk | engelska |
|---|---|
| Tidskrift | Blood |
| Volym | 109 |
| Utgåva | 2 |
| Sidor (från-till) | 802-810 |
| Antal sidor | 9 |
| ISSN | 0006-4971 |
| DOI | |
| Status | Publicerad - 2007 |
| MoE-publikationstyp | A1 Tidskriftsartikel-refererad |
Vetenskapsgrenar
- 1182 Biokemi, cell- och molekylärbiologi
- 3111 Biomedicinska vetenskaper
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Red-cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: characterization of the binding sites on ICAM-4. / Ihanus, Eveliina; Uotila, Liisa M; Toivanen, Anne; Varis, Minna; Gahmberg, Carl G.
I: Blood, Vol. 109, Nr. 2, 2007, s. 802-810.Forskningsoutput: Tidskriftsbidrag › Artikel › Vetenskaplig › Peer review
TY - JOUR
T1 - Red-cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: characterization of the binding sites on ICAM-4
AU - Ihanus, Eveliina
AU - Uotila, Liisa M
AU - Toivanen, Anne
AU - Varis, Minna
AU - Gahmberg, Carl G
PY - 2007
Y1 - 2007
N2 - Intercellular adhesion molecule 4 (ICAM-4) is a unique member of the ICAM family because of its specific expression on erythroid cells and ability to interact with several types of integrins expressed on blood and endothelial cells. The first reported receptors for ICAM-4 were CD11a/CD18 and CD11b/CD18. In contrast to these 2, the cellular ligands and the functional role of the third 02 integrin, CD11c/CD18, have not been well defined. Here, we show that ICAM-4 functions as a ligand for the monocyte/macrophage-specific CD11c/CD18. Deletion of the individual immunoglobulin domains of ICAM-4 demonstrated that both its domains contain binding sites for CD11c/CD18. Analysis of a panel of ICAM-4 point mutants identified residues that affected binding to the integrin. By molecular modeling the important residues were predicted to cluster in 2 distinct but spatially close regions of the first domain with an extension to the second domain spatially distant from the other residues. We also identified 2 peptides derived from sequences of ICAM-4 that are capable of modulating the binding to CD11c/CD18. CD11c/CD18 is expressed on macrophages in spleen and bone marrow. Inhibition of erythrophagocytosis by anti-ICAM-4 and antiintegrin antibodies suggests a role for these interactions in removal of senescent red cells. (c) 2007 by The American Society of Hematology
AB - Intercellular adhesion molecule 4 (ICAM-4) is a unique member of the ICAM family because of its specific expression on erythroid cells and ability to interact with several types of integrins expressed on blood and endothelial cells. The first reported receptors for ICAM-4 were CD11a/CD18 and CD11b/CD18. In contrast to these 2, the cellular ligands and the functional role of the third 02 integrin, CD11c/CD18, have not been well defined. Here, we show that ICAM-4 functions as a ligand for the monocyte/macrophage-specific CD11c/CD18. Deletion of the individual immunoglobulin domains of ICAM-4 demonstrated that both its domains contain binding sites for CD11c/CD18. Analysis of a panel of ICAM-4 point mutants identified residues that affected binding to the integrin. By molecular modeling the important residues were predicted to cluster in 2 distinct but spatially close regions of the first domain with an extension to the second domain spatially distant from the other residues. We also identified 2 peptides derived from sequences of ICAM-4 that are capable of modulating the binding to CD11c/CD18. CD11c/CD18 is expressed on macrophages in spleen and bone marrow. Inhibition of erythrophagocytosis by anti-ICAM-4 and antiintegrin antibodies suggests a role for these interactions in removal of senescent red cells. (c) 2007 by The American Society of Hematology
KW - 1182 Biochemistry, cell and molecular biology
KW - 3111 Biomedicine
U2 - 10.1182/blood-2006-04-014878
DO - 10.1182/blood-2006-04-014878
M3 - Article
VL - 109
SP - 802
EP - 810
JO - Blood
JF - Blood
SN - 0006-4971
IS - 2
ER -