The recognition events and receptor rearrangements that lead to signaling through Lselectin were studied using antibodies and sialyl lewis-x (sLex) carbohydrate ligands. These were bound to neutrophils in solution or following attachment via their Fc domains to protein-A microspheres, and then activation was quantitated as upregulation of surface CD11b/CD18 (Mac-1) using fluorescence flow cytometry. In general, relatively high affinity binding and receptor clustering appeared to be a requirement for signal transduction through L-selectin.
|Original language||English (US)|
|Journal||Annals of Biomedical Engineering|
|Issue number||SUPPL. 1|
|State||Published - 2000|
ASJC Scopus subject areas
- Biomedical Engineering