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PLANT PHYSIOLOGY , Vol 107, Issue 3 845-856, Copyright © 1995 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
The Effects of Mastoparan on the Carrot Cell Plasma Membrane Polyphosphoinositide Phospholipase C
M. H. Cho, Z. Tan, C. Erneux, S. B. Shears and W. F. Boss
Department of Botany, North Carolina State University, Raleigh, North Carolina 27695-7612 (M.H.C., W.F.B.)
When [3H]inositol-labeled carrot (Daucus carota L.) cells were treated with
10 or 25 [mu]M wasp venom peptide mastoparan or the active analog Mas-7
there was a rapid loss of more than 70% of
[3H]phosphatidylinositol-4-monophosphate (PIP) and
[3H]phosphatidylinositol-4,5-bisphosphate (PIP2) and a 3- and 4-fold
increase in [3H]inositol-1,4-P2 and [3H]inositol-1,4,5-P3, respectively.
The identity of [3H]inositol-1,4-P3 was confirmed by phosphorylation with
inositol-1,4,5-P3 3-kinase and co-migration with inositol-1,3,4,5-P4. The
changes in phosphoinositides were evident within 1 min. The loss of [3H]PIP
was evident only when cells were treated with the higher concentrations (10
and 25 [mu]M) of mastoparan or Mas-7. At 1 [mu]M Mas-7, [3H]PIP increased.
The inactive mastoparan analog Mas-17 had little or no effect on [3H]PIP or
[3H]PIP2 hydrolysis in vivo. Neomycin (100 [mu]M) inhibited the uptake of
Mas-7 and thereby inhibited the Mas-7-stimulated hydrolysis of [3H]PIP and
[3H]PIP2. Plasma membranes isolated from mastoparan-treated cells had
increased PIP-phospholipase C (PLC) activity. However, when Mas-7 was added
to isolated plasma membranes from control cells, it had no effect on
PIP-PLC activity at low concentrations and inhibited PIP-PLC at
concentrations greater than 10 [mu]M. In addition,
guanosine-5[prime]-O-(3-thiotriphosphate) had no effect on the PIP-PLC
activity when added to plasma membranes isolated from either the
Mas-7-treated or control cells. The fact that Mas-7 did not stimulate
PIP-PLC activity in vitro indicated that the Mas-7 induced increase in
PIP-PLC in vivo required a factor that was lost from the membrane during
isolation.
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