Monocytic cell adhesion to intact and plasmin-modified fibrinogen: Possible involvement of Mac-1 (CD11b/CD18) and ICAM-1 (CD54)

β2‐integrin Mac‐1 and immunoglobulin‐like ICAM‐1 adhesion molecules are expressed by monocytes and both known to bind fibrinogen and its degradation products. Here, we investigated whether fibrinogen cleavage with plasmin modulates the adherence of monocytic cells and what types of adhesion molecule...

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Bibliographic Details
Published in:Journal of cellular physiology 2001-09, Vol.188 (3), p.403-409
Main Authors: Arefieva, T.L., Krasnikova, Tatiana L.
Format: Article
Language:English
Subjects:
Cell Adhesion - drug effects
Cell Adhesion - physiology
Cell Line
Fibrin Fibrinogen Degradation Products - metabolism
Fibrinogen - metabolism
Fibrinolysin - metabolism
Fibrinolysin - pharmacology
Humans
Intercellular Adhesion Molecule-1 - biosynthesis
Macrophage-1 Antigen - biosynthesis
Monocytes - cytology
Monocytes - metabolism
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Summary:β2‐integrin Mac‐1 and immunoglobulin‐like ICAM‐1 adhesion molecules are expressed by monocytes and both known to bind fibrinogen and its degradation products. Here, we investigated whether fibrinogen cleavage with plasmin modulates the adherence of monocytic cells and what types of adhesion molecules are involved. Using several cell types, characterized by different patterns of Mac‐1 and ICAM‐1 expression, and monoclonal antibodies against β2‐integrins and ICAM‐1 we demonstrate, that fibrinogen cleavage evokes gradual decrease in β2‐integrin‐dependent cell adhesion. Furthermore, generation of the early degradation products, fragments X and Y, by minimum cleavage of fibrinogen stimulates cell adhesion, mediated by ICAM‐1. © 2001 Wiley‐Liss, Inc.
ISSN:0021-9541
1097-4652
DOI:10.1002/jcp.1127