Journal of Experimental Botany, Vol 50, 1735-1742, Copyright © 1999 by Oxford University Press
J van Himbergen, B ter Riet, H Meijer, H van den Ende, A Musgrave and T Munnik
The G-protein activator mastoparan and its analogues are becoming popular
tools for studying signalling in plants. Therefore the abilities of
mastoparan, mas7, mas8, and mas17 to activate phospholipase C (PLC), PLD
and to induce the deflagellation response in Chlamydomonas
moewusii Gerloff were compared. The aim was to test whether
their relative potencies in a plant system resemble those reported for
bovine brain Go and Gi, as is generally assumed, and to determine at which
concentrations cells become permeabilized, a known effect of higher
concentrations. The concentrations at which 50% deflagellation was induced,
were 2.0
ARTICLES
Mastoparan analogues stimulate phospholipase C- and phospholipase D-activity in Chlamydomonas: a comparative study
Institute for Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, Kruislaan 318, 1098 SM, Amsterdam, The Netherlands; Corresponding author; Fax: +31 20 525 7934; E-mail: himbergen@bio.uva.nl
M mastoparan, 3.0 M mas8, 3.6 
M mas7, and 5.8 M
mas17. Similar activities were found for the production of phosphatidic
acid, which is the result of the combined activities of PLD and PLC
(together with diacylglycerol kinase). PLD activity alone was measured
in vivo by its ability to phosphatidylate
n-butanol. Surprisingly, the concentrations that
stimulated maximum activity were about 10-fold lower (
1
M) than those that stimulated maximum PLC activity (10
M). Mas17 was an exception with both maxima above 10 M.
All the compounds except mas17 permeabilized C.
moewusii cells. The concentrations at which 50% of the cells
were permeabilized to Evan's blue were 7.4 M mas8, 16.0 M
mas7 and 22.4 M mastoparan. In conclusion, only mastoparan itself
and the least active analogue mas17 induced maximum deflagellation, PLC and
PLD activities without permeabilizing the cells.Keywords:
Chlamydomonas, deflagellation, mastoparan,
phospholipases C and D, phospholipid metabolism
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  P. Poutrain, C. Mazars, M. Thiersault, M. Rideau, and O. Pichon Two distinct intracellular Ca2+-release components act in opposite ways in the regulation of the auxin-dependent MIA biosynthesis in Catharanthus roseus cells J. Exp. Bot., March 1, 2009; 60(4): 1387 - 1398. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y.-Y. Pan, X. Wang, L.-G. Ma, and D.-Y. Sun Characterization of Phosphatidylinositol-Specific Phospholipase C (PI-PLC) from Lilium daviddi Pollen Plant Cell Physiol., October 1, 2005; 46(10): 1657 - 1665. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Dhonukshe, A. M. Laxalt, J. Goedhart, T. W. J. Gadella, and T. Munnik Phospholipase D Activation Correlates with Microtubule Reorganization in Living Plant Cells PLANT CELL, November 1, 2003; 15(11): 2666 - 2679. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Mueller-Roeber and C. Pical Inositol Phospholipid Metabolism in Arabidopsis. Characterized and Putative Isoforms of Inositol Phospholipid Kinase and Phosphoinositide-Specific Phospholipase C Plant Physiology, September 1, 2002; 130(1): 22 - 46. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Baluska, M. von Witsch, M. Peters, A. Hlavacka, and D. Volkmann Mastoparan Alters Subcellular Distribution of Profilin and Remodels F-Actin Cytoskeleton in Cells of Maize Root Apices Plant Cell Physiol., September 1, 2001; 42(9): 912 - 922. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Reggiani and P. Laoreti Evidence for the Involvement of Phospholipase C in the Anaerobic Signal Transduction Plant Cell Physiol., December 1, 2000; 41(12): 1392 - 1396. [Abstract] [Full Text] [PDF]
|
|