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J. Biol. Chem., Vol. 266, Issue 12, 7345-7352, Apr, 1991
PJ Sims, MH Ginsberg, EF Plow and SJ Shattil
Platelet activation converts the membrane GP IIb-IIIa complex into a
functional receptor for fibrinogen, but the mechanism is poorly understood.
We asked whether induction of receptor competency coincides with a
conformational change affecting the spatial arrangement of exoplasmic
domains of the IIb and IIIa subunits. Epitopes on these subunits were
labeled with monoclonal antibodies conjugated to either a donor fluorescein
(FITC) or an acceptor tetramethylrhodamine (TR) chromophore. Then,
fluorescence resonance energy transfer (RET) between platelet-bound FITC
and TR was measured by flow cytometry. In unstimulated platelets, 6-8% RET
efficiency was detected between antibody B1B5, bound to GP IIb, and
antibody SSA6, bound to GP IIIa, regardless of which antibody served as RET
donor. RET was also observed between these antibodies and A2A9, an antibody
specific for the GP IIb- IIIa complex. Cell stimulation by thrombin, ADP
plus epinephrine or phorbol-ester caused up to a 2-fold increase in RET
between chromophore- labeled, platelet-bound B1B5, SSA6, and A2A9 (p less
than or equal to 0.05), suggesting a change in the separation or
orientation of these epitopes within the GP IIb-IIIa complex. The
activation-related conformational change detected by the increase in RET
between antibody B1B5 and SSA6 was independent of receptor occupancy since
it was unaffected by the addition of fibrinogen or by the inhibition of
fibrinogen binding by the antibody, A2A9, or the peptide, RGDS. In contrast
to these results with antibodies bound to different epitopes within GP
IIb-IIIa, no RET was observed between FITC-A2A9 and TR-A2A9 bound to
different GP IIb-IIIa complexes or between a TR-labeled GP Ib antibody and
FITC-labeled GP IIb-IIIa antibodies. These studies demonstrate that
platelet activation causes a change in the spatial separation or
orientation of exoplasmic domains within GP IIb and IIIa, which may serve
to convert this integrin into a functional adhesion receptor.
Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex
Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
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E. Loh, K. Beaverson, G. Vilaire, W. Qi, M. Poncz, and J. S. Bennett Agonist-stimulated Ligand Binding by the Platelet Integrin alphaIIbbeta3 in a Lymphocyte Expression System J. Biol. Chem., August 4, 1995; 270(31): 18631 - 18636. [Abstract] [Full Text] [PDF]
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P. E. Hughes, T. E. O'Toole, J. Ylänne, S. J. Shattil, and M. H. Ginsberg The Conserved Membrane-proximal Region of an Integrin Cytoplasmic Domain Specifies Ligand Binding Affinity J. Biol. Chem., May 26, 1995; 270(21): 12411 - 12417. [Abstract] [Full Text] [PDF]
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S. Honda, Y. Tomiyama, A. J. Pelletier, D. Annis, Y. Honda, R. Orchekowski, Z. Ruggeri, and T. J. Kunicki Topography of Ligand-induced Binding Sites, Including a Novel Cation-sensitive Epitope (AP5) at the Amino Terminus, of the Human Integrin [IMAGE][IMAGE] Subunit J. Biol. Chem., May 19, 1995; 270(20): 11947 - 11954. [Abstract] [Full Text] [PDF]
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