Romero, I.A.; Amos, C.L.; Greenwood, J. and Adamson, P.
|DOI (Digital Object Identifier) Link:||http://dx.doi.org/10.1016/S0169-328X(02)00392-3|
|Google Scholar:||Look up in Google Scholar|
The precise mechanism by which ICAM-1 transduces signals from adherent lymphocytes remains elusive. The ERM proteins ezrin and moesin were found to strongly co-localise with both ICAM-1 and F-actin in brain microvascular endothelial cells suggesting a potential role in mediating ICAM-1 signalling. Such strong co-localisation was maintained following treatment of cells with cytochalasin D, which inhibits actin polymerization and which is capable of inhibiting ICAM-1-induced signalling. Cross-linking of ICAM-1 demonstrated ICAM-1 clustering which no longer associated with ezrin or moesin. In addition immunoprecipitation analysis revealed that ICAM-1 was incapable of precipitating ERM proteins under conditions where ezrin was efficiently precipitated with anti-ICAM-2 antibodies. Fractionation of cell lysates on sucrose density gradients shows ICAM-1 and ezrin to sediment at different densities, whereas ICAM-2 co-sediments with ezrin. Together these data suggest that ICAM-1 is not directly associated with ezrin and moesin in brain microvascular endothelial cells.
|Item Type:||Journal Article|
|Keywords:||CNS endothelium; ICAM-1; Cytoskeleton; ERM proteins; GP8 cells|
|Academic Unit/Department:||Science > Life, Health and Chemical Sciences
|Interdisciplinary Research Centre:||Biomedical Research Network (BRN)|
|Depositing User:||Ignacio A Romero|
|Date Deposited:||23 Aug 2007|
|Last Modified:||14 Jan 2016 16:41|
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