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Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on
circulating reticulocytes in sickle cell anemia
CC Joneckis, RL Ackley, EP Orringer, EA Wayner and LV Parise
Department of Pharmacology, University of North Carolina at Chapel Hill
27599-7365.
The abnormal adherence of red blood cells, especially circulating
reticulocytes (erythrocyte precursors), to the endothelium is believed to
contribute to vascular occlusion observed in patients with sickle cell
disease. Although several plasma proteins including von Willebrand factor
and fibronectin have been proposed to mediate this adhesion, the mechanism
of sickle cell adhesion to the endothelium remains unknown. Using flow
cytometry, we screened sickle red blood cells with monoclonal antibodies
(MoAbs) against known adhesion receptors and detected integrin subunits
alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but
not on erythrocytes. No reactivity was detected against integrin subunits
alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha
IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of
reticulocytes with either alpha 4- or beta 1-specific antibodies identified
the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor
for fibronectin and vascular cell adhesion molecule-1. An antibody against
glycoprotein IV, a receptor reported to bind thrombospondin and collagen,
immunoprecipitated an 88-kD protein consistent with its reported M(r).
MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and
17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta
1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and
independent mechanisms of reticulocyte adhesion to endothelium and exposed
extracellular matrix.
Volume 82,
Issue 12,
pp. 3548-3555,
12/15/1993
Copyright © 1993 by The American Society of Hematology
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