| Abstrakt: |
The L-selectin adhesion receptor plays a central role in regulating leukocyte adhesion to endothellal cells. The data presented in this report demonstrate that triggering of L-selectin results in a rapid and vigorous homotypic adhesion among normal lymphocytes as well as lymphoblastoid cells, thereby providing evidence for a novel cell-cell adhesion function of L-selectin. The cellular adhesion event induced by mAb MEL-14 was dependent on metabolic energy, an intact cytoskeleton, and the activation of intracellular protein kinases. Cell clustering did not require cross-linking of L-selectin molecules and occurred in the complete absence of divaient cations. Analysis of adhesion receptor expression and antibody inhibition experiments indicated that cluster formation did not involve LFA-1, integrins, integrins, integrins, or CD44. [ABSTRACT FROM PUBLISHER] |
