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Departments of
*
Immunology and
Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, NY 14263; and
Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, IL 60611
L-selectin mediates lymphocyte extravasation into lymphoid tissues
through binding to sialomucin-like receptors on the surface of high
endothelial venules (HEV). This study examines the biochemical basis
and regulation of interactions between L-selectin, an integral
transmembrane protein, and the lymphocyte cytoskeleton. Using a
detergent-based extraction procedure, constitutive associations between
L-selectin and the insoluble cytoskeletal matrix could not be detected.
However, engagement of the L-selectin lectin domain by Abs or by
glycosylation-dependent cell adhesion molecule-1, an HEV-derived ligand
for L-selectin, rapidly triggered redistribution of L-selectin to the
detergent-insoluble cytoskeleton. L-selectin attachment to the
cytoskeleton was not prevented by inhibitors of actin/microtubule
polymerization (cytochalasin B, colchicine, or nocodozole) or
serine/threonine and tyrosine kinase activity (staurosporine,
calphostin C, or genistein), although L-selectin-mediated adhesion of
human PBL was markedly suppressed by these agents. Exposure of human
PBL or murine pre-B transfectants expressing full-length human
L-selectin to fever-range hyperthermia also markedly increased
L-selectin association with the cytoskeleton, directly correlating with
enhanced L-selectin-mediated adhesion. In contrast, a deletion mutant
of L-selectin lacking the COOH-terminal 11 amino acids failed to
associate with the cytoskeletal matrix in response to Ab cross-linking
or hyperthermia stimulation and did not support adhesion to HEV. These
studies, when taken together with the previously demonstrated
interaction between the L-selectin cytoplasmic domain and the
cytoskeletal linker protein 
-actinin, strongly implicate the
actin-based cytoskeleton in dynamically controlling L-selectin
adhesion.
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