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Regulatory role of CD43 leukosialin on integrin-mediated T-cell adhesion to
endothelial and extracellular matrix ligands and its polar redistribution
to a cellular uropod
P Sanchez-Mateos, MR Campanero, MA del Pozo and F Sanchez-Madrid
Servicio de Inmunologia, Hospital de la Princesa, Universidad Autonoma de
Madrid, Spain.
CD43 is a cell surface-associated mucin that is abundantly expressed by
most leukocytes, and that appears to function as a negative regulator of
cell surface interactions, providing a repulsive barrier around cells. We
have analyzed herein the ability of anti-CD43 monoclonal antibody (MoAb) to
upregulate both beta 1 and beta 2 integrin-mediated cell adhesion and to
promote redistribution of the CD43 molecule into a cellular uropod.
Engagement of CD43 with specific antibodies enhanced the cell adhesion to
both 80- and 38-kD fibronectin fragments as well as to the endothelial cell
ligands vascular cell adhesion molecule-1 and intercellular adhesion
molecule-1, an effect that was mediated through the alpha 5 beta 1, alpha 4
beta 1, and alpha L beta 2 integrins, respectively. This effect on cell
adhesion was achieved in Jurkat leukemic T cells by anti-CD43 MoAb alone;
however, in T lymphoblasts, the activation of cell adhesion required the
concomitant ligation of CD3 with suboptimal doses of anti-CD3 MoAb.
Immunofluorescence analysis showed that the engagement of CD43 was
accompanied by a differential redistribution of CD43 into a well- defined
cytoplasmic projection or uropod, whereas the beta 1 or beta 2 integrins
remained uniformly located on the contact area with substrata. This change
in the localization of CD43 did not require costimulation and was induced
directly by engagement of CD43 in T lymphoblasts. Other stimuli of cell
adhesion in the form of cross- linked anti-CD3 MoAb or phorbol esters did
not induce uropod formation or CD43 redistribution. In addition, we
observed that prolonged co- culture of resting peripheral blood T
lymphocytes with endothelial cells, in the absence of anti-CD43 MoAb,
induced uropod formation and redistribution of CD43 in T cells.
Interestingly, the myosin-disrupting drug butanedione monoxime inhibited
the redistribution of CD43 induced by the specific MoAb, whereas the
stimulation of cell adhesion induced by engagement of CD43 was preserved in
the presence of this drug. These observations indicate that the signaling
inducing integrin-mediated cell adhesion by CD43 takes place independently
from the receptor redistribution. Altogether, these results indicate that
CD43 has a regulatory role on both integrin-mediated T-cell adhesion and
cellular morphology.
Volume 86,
Issue 6,
pp. 2228-2239,
09/15/1995
Copyright © 1995 by The American Society of Hematology
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