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(Received for publication, February 13, 1996, and in revised form, March 12, 1996)
From the Department of Pharmacology, University of Illinois,
Chicago, Illinois 60612
As a consequence of platelet activation and
fibrinogen binding, glycoprotein (GP)IIb-IIIa (integrin
Volume 271, Number 27,
Issue of July 5, 1996
pp. 16416-16421
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
IIb
3 (GPIIb-IIIa) to Talin
EVIDENCE THAT INTERACTION IS MEDIATED THROUGH THE
CYTOPLASMIC DOMAINS OF BOTH 
IIb AND
3
IIb
3) becomes associated with the
cytoskeleton. Although talin has been suggested to act as a linkage
protein mediating the attachment of GPIIb-IIIa to actin filaments,
direct binding of GPIIb-IIIa to this cytoskeletal protein has not been
demonstrated. In the present study, we examined the interaction of
GPIIb-IIIa with purified talin using a solid-phase binding assay.
Soluble GPIIb-IIIa bound in a time- and dose-dependent
manner to microtiter wells coated with talin but not with BSA. Time
course studies demonstrated that steady-state binding was achieved
after 4-5 h incubation at 37 °C. Binding isotherms with varying
concentrations of GPIIb-IIIa showed that half-saturation binding was
achieved at approximately 15 nM GPIIb-IIIa. At saturation,
there was 211 ± 8 fmol of GPIIb-IIIa bound per well containing 117 ± 10 fmol of immobilized talin. Besides binding to immobilized talin,
GPIIb-IIIa also bound to talin captured by the anti-talin monoclonal
antibody 8d4. Moreover, the interaction of GPIIb-IIIa to 8d4-captured
talin was blocked by mAb10B2, a monoclonal antibody raised against a
synthetic peptide encompassing the entire cytoplasmic sequence of
GPIIb. The interaction of talin with the cytoplasmic domain of
GPIIb-IIIa was further investigated using peptide-coated wells.
Purified talin was found to bind to both synthetic peptides
corresponding to the cytoplasmic sequences of GPIIb (P2b) and GPIIIa
(P3a). As expected, the binding of talin to P2b-coated wells was
specifically blocked by mAb10B2. Thus, these results demonstrate direct
binding of GPIIb-IIIa to talin and suggest a role of the cytoplasmic
sequences of both GPIIb and GPIIIa in mediating this interaction.
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