Inhibition of β2 Integrin–mediated Leukocyte Cell Adhesion

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http://hdl.handle.net/1975/550

Citation

Journal of cell biology. 2001. 153(5): 905-915.

Title: Inhibition of β2 Integrin–mediated Leukocyte Cell Adhesion
Author: Koivunen, Erkki; Ranta, Tanja-Maria; Annila, Arto; Taube, Seija; van Willigen, Gijsbert; Ihanus, Eveliina; Gahmberg, Carl G.
Publisher: Rockefeller University Press
Date: 2001
Language: en
Number of pages: 358101 bytes
ISSN: 0021-9525
URI: http://hdl.handle.net/1975/550
Abstract: Many integrins mediate cell attachment to the extracellular matrix by recognizing short tripeptide sequences such as arginine–glycine–aspartic acid and leucine–aspartate–valine. Using phage display, we have now found that the leukocyte-specific b2 integrins bind sequences containing a leucine–leucine–glycine (LLG) tripeptide motif. An LLG motif is present on intercellular adhesion molecule (ICAM)-1, the major b2 integrin ligand, but also on several matrix proteins, including von Willebrand factor. We developed a novel b2 integrin antagonist peptide CPCFLLGCC (called LLG-C4), the structure of which was determined by nuclear magnetic resonance. The LLG-C4 peptide inhibited leukocyte adhesion to ICAM-1, and, interestingly, also to von Willebrand factor. When immobilized on plastic, the LLG-C4 sequence supported the b2 integrin–mediated leukocyte adhesion, but not b1 or b3 integrin–mediated cell adhesion. These results suggest that LLG sequences exposed on ICAM-1 and on von Willebrand factor at sites of vascular injury play a role in the binding of leukocytes, and LLG-C4 and peptidomimetics derived from it could provide a therapeutic approach to inflammatory reactions.
Subject: cell adhesion
extracellular matrix
leukocyte
phage display
peptides


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