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Blood, Vol. 92 No. 8 (October 15), 1998:
pp. 2951-2958
Sickle Cell Adhesion to Laminin: Potential Role for the  5 Chain
Sheritha P. Lee,
Michelle L. Cunningham,
Patrick C. Hines,
Christopher C. Joneckis,
Eugene P. Orringer, and
Leslie V. Parise
From the Department of Biology, North Carolina Central University,
Durham, NC; and the Departments of Pharmacology and Medicine, and The
Center for Thrombosis and Hemostasis, The University of North Carolina
at Chapel Hill, Chapel Hill, NC.
Sickle red blood cell (RBC) adhesion to the endothelium and to
exposed, underlying subendothelial proteins is believed to contribute
to vascular occlusion in sickle cell disease. Laminin, a major
component of the subendothelium, supports significant adhesion of
sickle, but not normal RBCs. The purpose of this study was to define
the adhesive region for sickle RBCs within a human laminin preparation
using a flow adhesion assay designed to mimic physiologic flow through
postcapillary venules. Because sickle RBCs did not adhere to the common
laminin contaminants entactin or collagen type IV, neither of these
proteins are likely to contribute to the observed adhesion to laminin.
Known adhesive regions of laminin neither supported nor inhibited
sickle RBC adhesion to laminin, suggesting a mechanism of adhesion
previously uncharacterized in other laminin adhesion studies. Moreover,
sickle RBCs did not adhere to mouse EHS laminin or to human laminin-2
(merosin), eliminating the  1, 2,  1, and  1 chains as
mediators of sickle cell adhesion. The monoclonal antibody 4C7, which
binds at or near the G-domain of the laminin 5 chain, significantly
inhibited sickle RBC adhesion. These results suggest that an adhesive
region for sickle RBCs is contained within the laminin 5 chain.
© 1998 by The American Society of Hematology.
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