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J Biol Chem, Vol. 274, Issue 39, 27385-27391, September 24, 1999
,
,,,
From the Gelsolin, an actin-binding protein, shows a
strong ability to bind to phosphatidylinositol 4,5-bisphosphate
(PIP2). Here we showed in in vitro
experiments that gelsolin inhibited recombinant phospholipase D1 (PLD1)
and PLD2 activities but not the oleate-dependent PLD and
that this inhibition was not reversed by increasing PIP2 concentration. To investigate the role of gelsolin in agonist-mediated PLD activation, we used NIH 3T3 fibroblasts stably transfected with the
cDNA for human cytosolic gelsolin. Gelsolin overexpression suppressed bradykinin-induced activation of phospholipase C (PLC) and
PLD. On the other hand, sphingosine 1-phosphate (S1P)-induced PLD
activation could not be modified by gelsolin overexpression, whereas
PLC activation was suppressed. PLD activation by phorbol myristate
acetate or Ca2+ ionophore A23187 was not affected by
gelsolin overexpression. Stimulation of control cells with either
bradykinin or S1P caused translocation of protein kinase C (PKC) to the
membranes. Translocation of PKC- Department of Biochemistry, Department of Biology,
and PKC-
1 but not PKC-
was
reduced in gelsolin-overexpressed cells, whereas phosphorylation of
mitogen-activated protein kinase was not changed. S1P-induced PLC
activation and mitogen-activated protein kinase phosphorylation were
sensitive to pertussis toxin, but PLD response was insensitive to such
treatment, suggesting that S1P induced PLD activation via certain G
protein distinct from Gi for PLC and mitogen-activated
protein kinase pathway. Our results suggest that gelsolin modulates
bradykinin-mediated PLD activation via suppression of PLC and PKC
activities but did not affect S1P-mediated PLD activation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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