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Protein phosphatase inhibitors okadaic acid and calyculin A alter cell
shape and F-actin distribution and inhibit stimulus-dependent increases in
cytoskeletal actin of human neutrophils
P Kreienbuhl, H Keller and V Niggli
Department of Pathology, University of Bern, Switzerland.
The phosphatase inhibitors okadaic acid and calyculin A were found to
elicit or to modify several neutrophil responses, suggesting that
dephosphorylation plays a regulatory role. The concentrations of okadaic
acid (> or = 1 mumol/L) that were effective on neutrophil functions
(shape changes and marginal stimulation of pinocytosis) were shown to
stimulate the incorporation of 32PO4 into many neutrophil proteins
several-fold. Calyculin A was effective at 50-fold lower concentrations. In
the presence of the inhibitors, the cells exhibited a nonpolar shape and
the polarization response induced by chemotactic peptide was inhibited.
Both phosphatase inhibitors also induced the association of F-actin with
the cell membrane. A steady-state phosphatase activity is thus involved in
maintaining shape and F-actin localization of resting cells. Inhibitors
alone had no significant effect on the amount of cytoskeleton-associated
actin. The increase in cytoskeletal actin observed at 30 minutes of
stimulation with phorbol ester or 5 to 30 minutes of stimulation with
chemotactic peptide, however, was abolished by okadaic acid or calyculin A,
suggesting an important role of a phosphatase. In contrast, the early
increase in cytoskeleton-associated actin observed at 1 minute of
stimulation with peptide was not affected. This finding indicates that the
increased association of actin with the cytoskeleton in the early and the
later stages of neutrophil activation may be mediated by different
signalling pathways.
Volume 80,
Issue 11,
pp. 2911-2919,
12/01/1992
Copyright © 1992 by The American Society of Hematology
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