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Intracellular calcium and calcineurin regulate neutrophil motility on
vitronectin through a receptor identified by antibodies to integrins alphav
and beta3
B Hendey, M Lawson, EE Marcantonio and FR Maxfield
Department of Pharmacology, Rush Medical College, Chicago, IL, USA.
Buffering of intracellular calcium ([Ca2+]i) or inhibition of the
calcium/calmodulin-dependent phosphatase, calcineurin, results in
neutrophils being unable to detach from vitronectin with a consequent loss
of motility. Treatment of [Ca2+]i-buffered or calcineurin- inhibited
neutrophils with monoclonal antibodies (MoAbs) to beta3 or alphav beta3
integrins allowed neutrophils to detach and restored motility. Quantitative
immunofluorescence and flow cytometry showed that MoAbs specific for beta3,
alphav, or alphav beta3 integrins bind to neutrophils. Immunolocalization
studies using antibodies to the highly conserved cytoplasmic domains of
alphav and beta3 also identified the receptor on neutrophils. Whereas
antibodies to alphav, alphav beta3, and beta3 recognized the receptor in
intact cells, only the beta3 MoAb immunoprecipitated the receptor from a
neutrophil cell lysate. The alpha subunit co-immunoprecipitated by the
beta3 antibody reacted with an antibody to alphav by Western blot. Peptide
maps of V8 protease digests showed a strong similarity in alpha and beta
chains precipitated by antibodies to beta3 from neutrophils and endothelial
cells. These results indicate that [Ca2+]i and calcineurin regulate
neutrophil motility on vitronectin through an alphav beta3-like receptor.
Although we cannot rule out the possibility that neutrophils have an
isoform of alphav, such an isoform would have to be similar enough to react
with alphav- and alphav beta3-specific MoAbs in intact cells.
Volume 87,
Issue 5,
pp. 2038-2048,
03/01/1996
Copyright © 1996 by The American Society of Hematology
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