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J Biol Chem, Vol. 274, Issue 36, 25301-25307, September 3, 1999
IIb
3 for Fibrinogen
,,
, and
From the Departments of Agonist-generated inside-out signals enable the
platelet integrin Medicine and ¶ Biology,
University of Pennsylvania, Philadelphia, Pennsylvania 19104 and the
Department of Pharmacology, Merck Research Laboratories,
West Point, Pennsylvania 19486
IIb
3 to bind
soluble ligands such as fibrinogen. We found that inhibiting actin
polymerization in unstimulated platelets with cytochalasin D or
latrunculin A mimics the effects of platelet agonists by inducing
fibrinogen binding to IIb3. By contrast, stabilizing actin filaments with jasplakinolide prevented
cytochalasin D-, latrunculin A-, and ADP-induced fibrinogen
binding. Cytochalasin D- and latrunculin A-induced fibrinogen was
inhibited by ADP scavengers, suggesting that subthreshold
concentrations of ADP provided the stimulus for the actin filament
turnover required to see cytochalasin D and latrunculin A effects.
Gelsolin, which severs actin filaments, is activated by calcium,
whereas the actin disassembly factor cofilin is inhibited by serine
phosphorylation. Consistent with a role for these factors in regulating
IIb3 function, cytochalasin D- and
latrunculin A-induced fibrinogen binding was inhibited by the
intracellular calcium chelators
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl ester and EGTA acetoxymethyl ester and the Ser/Thr phosphatase inhibitors okadaic acid and calyculin A. Our results suggest that the actin cytoskeleton in unstimulated platelets constrains IIb3 in a low affinity state.
We propose that agonist-stimulated increases in platelet cytosolic
calcium initiate actin filament turnover. Increased actin filament
turnover then relieves cytoskeletal constraints on
IIb3, allowing it to assume the high
affinity conformation required for soluble ligand binding.
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