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Expression of a functional laminin receptor (alpha 6 beta 1, very late
activation antigen-6) on human eosinophils
SN Georas, BW McIntyre, M Ebisawa, JL Bednarczyk, SA Sterbinsky, RP Schleimer and BS Bochner
Department of Medicine, Johns Hopkins University School of Medicine, Johns
Hopkins Asthma and Allergy Center, Baltimore, MD 21224-6801.
The mechanisms responsible for the accumulation of eosinophils at sites of
allergic and other inflammatory reactions are unknown, but recent studies
have implicated both eosinophil and endothelial adhesion molecules in this
process. However, less well studied have been the adhesive interactions
between eosinophils and the subendothelial basement membrane and
interstitial connective tissues. To test the hypothesis that eosinophils
might interact with extracellular matrix proteins, we analyzed purified
human eosinophils for the expression and function of various beta 1
integrins. Using indirect immunofluorescence and flow cytometry, purified
eosinophils from mildly allergic donors were found to consistently express
the integrin subunits beta 1 (CD29), alpha 4 (CD49d, very late activation
antigen [VLA]-4 alpha), and alpha 6 (CD49f, VLA-6 alpha). No significant
expression of the alpha 1, alpha 2, alpha 3, alpha 5, or beta 4 subunits
was detected. Platelet contamination of the eosinophil preparations was
excluded by light microscopy and by the inability to detect expression of
platelet glycoproteins alpha v, CD41b, and CD42b. Immunoprecipitation and
sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of
eosinophils confirmed the expression of cell-surface beta 1, alpha 4, and
alpha 6. Furthermore, eosinophils purified from allergic donors were shown
to adhere to plate-bound laminin, but not to type 1 or type 4 collagen.
Adhesion to laminin was concentration-dependent, required divalent cations,
and was completely and specifically inhibited by the anti-alpha 6
monoclonal antibody (MoAb) GoH3 and by the anti-beta 1 MoAb 33B6.
Interestingly, the anti-beta 1 MoAb 18D3 (which like 33B6 blocks eosinophil
binding to VCAM-1) did not inhibit eosinophil adhesion to laminin,
suggesting that there are functionally distinct epitopes on the beta 1
subunit. Eosinophils purified from 4 healthy, nonallergic donors also
showed alpha 6-dependent adhesion to laminin, although these cells adhered
less well. These studies establish the expression of alpha 6 beta 1 on
human eosinophils and document its function as a laminin receptor.
Interaction of eosinophil alpha 6 beta 1 with laminin, eg, in basement
membranes, may contribute to the localization of these cells at
inflammatory sites in vivo.
Volume 82,
Issue 9,
pp. 2872-2879,
11/01/1993
Copyright © 1993 by The American Society of Hematology
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