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Mechanism of tissue factor activation on HL-60 cells
RR Bach and CF Moldow
Veterans Affairs Medical Center, Research Service (151), Minneapolis, MN
55417, USA.
Tissue factor (TF) procoagulant activity (PCA) on the surface of intact
HL-60 cells is encrypted. This latent TF PCA was activated by exposing the
cells to ionomycin, a calcium ionophore. Within seconds an increase in TF
PCA of greater than 100-fold was observed. The ionomycin effect was blocked
by pretreating the cells with calmidazolium, a calmodulin inhibitor.
Changes in TF structure and function, coincident with the ionophore-induced
increase in TF PCA, were identified. TF-factor VIIa complexes formed on
both untreated and ionophore-treated cells, but pseudosubstrate inhibitors
only bound to TF-factor VIIa on the ionophore-treated cells. TF PCA was
inhibited by reacting cells with
sulfosuccinimidyl-6-(biotinamido)hexanoate, and the rate of this reaction
increased twofold after cells were exposed to ionomycin. When proteins on
the surface of untreated cells, expressing minimal TF PCA, were
cross-linked with 3-3'-dithiobis(sulfosuccinimidylpropionate), cross-linked
TF dimers were produced. TF cross-linking was prevented by first treating
the cells with ionomycin. These results suggest a mechanism for the
ionomycin-induced increase in TF PCA. TF activation appears to be a
calmodulin-dependent process, which exposes an essential macromolecular
substrate binding site on TF, possibly as the result of a change in TF
quaternary structure.
Volume 89,
Issue 9,
pp. 3270-3276,
05/01/1997
Copyright © 1997 by The American Society of Hematology
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