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Phorbol ester enhances integrin alpha IIb beta 3-dependent adhesion of
human erythroleukemic cells to activation-dependent monoclonal antibodies
C Boudignon-Proudhon, PM Patel and LV Parise
Department of Pharmacology, University of North Carolina at Chapel Hill
27599-7365, USA.
Following platelet stimulation by agonists, integrin-alpha IIb beta 3 (or
glycoprotein IIb-IIIa) is converted to an activated state that can bind
soluble fibrinogen and mediate platelet aggregation. However, little is
known about modulation of alpha IIb beta 3 in cell lines. In the present
study, we show that agonist stimulation modulates alpha IIb beta
3-dependent adhesive properties of a human erythroleukemic (HEL) cell line.
Brief treatment with phorbol 12-myristate 13-acetate (PMA) caused a
significant increase in HEL cell adhesion to monoclonal antibodies (MoAbs)
specific for activated alpha IIb beta 3 (PAC1 or pl- 55). This adhesion was
inhibited by blocking MoAbs or peptides specific for alpha IIb beta 3, but
not by anti-Fc gamma receptor-specific MoAb. Similarly, PMA enhanced HEL
cell adhesion to immobilized fibrinogen by 10-fold. However, the
activation-dependent ligands in solution (ie, PAC1, pl-55, or fibrinogen)
did not inhibit the enhanced HEL cell adhesion to immobilized MoAbs PAC1 or
pl-55 after PMA treatment. Thus, PMA may increase alpha IIb beta
3-dependent adhesion to immobilized activation-dependent antibodies and
fibrinogen by increasing the local concentration of alpha IIb beta 3 to
participate in low-affinity interactions, resulting in an increased
avidity, changing the affinity state of alpha IIb beta 3, or both.
Volume 87,
Issue 3,
pp. 968-976,
02/01/1996
Copyright © 1996 by The American Society of Hematology
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