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CD11/CD18-independent neutrophil adherence to laminin is mediated by the
integrin VLA-6
JF Bohnsack
Department of Pediatrics, University of Utah School of Medicine, Salt Lake
City 84132.
Regulated adherence of polymorphonuclear leukocytes (PMNs) to endothelium
and subendothelial matrix is a critical event for PMN localization at and
migration into inflammatory sites. We previously reported that human PMNs
stimulated in vitro adhere to laminin, the major glycoprotein of mammalian
basement membrane, by both CD11/CD18 (beta 2 integrin)-dependent and
CD11/CD18-independent mechanisms. This CD11/CD18-independent adherence is
inhibited by monoclonal antibodies (MoAbs) directed against the beta 1
subunit of integrins (very late antigens [VLA]). The specific PMN VLA
receptor responsible for stimulated CD11/CD18-independent PMN adherence to
laminin was not elucidated. We show here that this CD11/CD18-independent
adherence is mediated by a member of the beta 1 integrins, VLA-6. MoAbs
GoH3 and 450- 30, which bind the alpha 6 subunit of VLA-6, significantly
reduced adherence of phorbol myristate acetate-stimulated PMNs to laminin-
coated surfaces when CD11/CD18-independent adherence was blocked with
anti-CD11/CD18 MoAbs. Furthermore, GoH3 completely inhibited stimulated
adherence of CD11/CD18-deficient PMNs to laminin. Analysis by flow
cytometry showed that human PMNs express VLA-6. The PMN alpha 6 is
identical in size and pl to the platelet alpha 6, but the PMN beta 1
exhibits considerable heterogeneity in molecular weight compared with the
platelet beta 1. This activation-dependent adherence receptor for laminin
may play a role in PMN interaction with basement membrane laminin during
PMN movement through vascular walls.
Volume 79,
Issue 6,
pp. 1545-1552,
03/15/1992
Copyright © 1992 by The American Society of Hematology
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