Triggering of L-selectin (gp90MEL-14) induces homotypic lymphocyte adhesion by a mechanism independent of LFA-1.
The L-selectin adhesion receptor plays a central role in regulating leukocyte adhesion to endothelial 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 divalent cations. Analysis of adhesion receptor expression and antibody inhibition experiments indicated that cluster formation did not involve LFA-1, alpha 4 integrins, beta 1 integrins, beta 7 integrins, or CD44.
Strauch
U G
UG
Institute for Medical Microbiology and Hygiene, Technical University of Munich, Germany.
Holzmann
B
B
D000818:Animals; D000911:Antibodies, Monoclonal; D002448:Cell Adhesion / Q000276:immunology* / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000276:immunology*; D002460:Cell Line; D019041:L-Selectin; D016169:Lymphocyte Function-Associated Antigen-1 / Q000276:immunology; D008214:Lymphocytes / Q000276:immunology* / Q000502:physiology; D051379:Mice
D000911:Antibodies, Monoclonal; D015815:Cell Adhesion Molecules; D016169:Lymphocyte Function-Associated Antigen-1; D019041:L-Selectin