Ethanol stimulates phospholipid turnover and inositol 1,4,5-trisphosphate production in Chlamydomonas eugametos gametes

Musgrave, A.; Kuin, H.M.A.; Jongen, Marjan; Wildt, Piet de; Schuring, F.; Klerk, H. C. De; Ende, H. van den

doi:10.1007/bf00195326

Cited by 30 publications

(30 citation statements)

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“…In animal systems, the hydrolysis of PtdInsP 2 by phospholipase C is reflected in a rapidly 32P-labelled PtdOH pool due to subsequent phosphorylation of the resulting DAG by DAG kinase (Berridge 1992). Similar claims have been made for the green algae Chlamydomonas and Dunaliella (Einspahr et al 1988;Brederoo et al 1991 ;Ha and Thompson1991 ;Musgrave et al 1992) and the same process is presumed to occur in higher plants (Heim and Wagner 1990). In carnation, the rapid incorporation and loss of 32p-label from PtdOH resembles the labelling kinetics of PtdInsP and PtdInsP2, suggesting that the two are again causally related.…”

Section: Discussionmentioning

confidence: 68%

Rapid turnover of polyphosphoinositides in carnation flower petals

Munnik¹,

Musgrave

Vrije³

1994

Planta

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Abstract. Carnation (Dianthus caryophyllus L. cv. White Sim) petal discs were radiolabelled with [32p]orthophosphate and the lipids were extracted and analysed by thin-layer chromatography and autoradiography. Phospholipids were identified by co-migration with standards using thin-layer chromatography with different solvent systems. Results showed that [32p]orthophosphate was rapidly incorporated into the minor lipids phosphatidic acid (PtdOH), phosphatidylinositol monophosphate (PtdInsP) and phosphatidylinositol bisphosphate (PtdInsP2), and relatively slowly into the structural lipids phosphatidylcholine, -ethanolamine, -glycerol and -inositol. Pulse-chase experiments revealed that the label was rapidly lost from PtdOH, PtdInsP and PtdInsP2 while the structural lipids remained radiolabelled. The amount of PtdInsP and PtdInsP2 was found to constitute 0.45% and 0.013%, respectively, of the total phospholipids, on a molar basis. Together these results show that the turnover of the chemically low-abundant polyphosphoinositides is relatively high compared with the major structural phospholipids. Phosphatidylinositol monophosphate was further characterized by showing that it incorporates myo-[3H]inositol and that its major fatty-acid constituents are palmitic acid and linoleic acid. Furthermore, we present evidence for the presence of both phosphatidylinositol 3-phosphate and phosphatidylinositol 4-phosphate isomers. The significance of these results is discussed with respect to plant phosphoinositide signal transduction.

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Section: Discussionmentioning

confidence: 68%

Rapid turnover of polyphosphoinositides in carnation flower petals

Munnik¹,

Musgrave

Vrije³

1994

Planta

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“…From animal systems, we know that extracellular information received by cell surface receptors often activates heterotrimeric G proteins, which in turn activate intracellular effector enzymes that catalyze the formation of second messengers (Gilman, 1987;Birnbaumer et al, 1990;Berridge, 1993;Neer, 1995;Nishizuka, 1995). In recent years, biochemical and molecular analyses have demonstrated that heterotrimeric G proteins are present in plants (reviewed in Ma, 1994), and because their activation has been shown to stimulate effector enzymes and induce physiological responses (Bolwell et al, 1991;Warpeha et al, 1991;Legendre et ai., 1992Legendre et ai., , 1993Musgrave et al, 1992;Quarmby et al, 1992;Neuhaus et al, 1993;Romero and Lam, 1993;White et al, 1993;Yueh and Crain, 1993;Bowler et al, 1994;Cote and Crain, 1994;Elich and Chory, 1994;Ma, 1994;Quarmby and Hartzell, 1994), we assume they play a role in plant cell signaling similar to that described for animals.…”

Section: Introductionmentioning

confidence: 69%

“…A good plant system for studying its possible involvement is the biflagellate green alga Chlamydomonas spp, because there is already convincing evidence for the presence of PLC signaling activity (Irvine et al, 1989Schuring et al, 1990;Brederoo et al, 1991;Dr$bak, 1992Dr$bak, , 1993Musgrave et al, 1992Musgrave et al, ,1993Quarmby et al, 1992;Yueh and Crain, 1993;Cote and Crain, 1994;Munnik et al, 1994aMunnik et al, , 1994bQuarmby and Hartzell, 1994). What is more, this pathway is activated by G protein activators with dramatic effects for gametes; for example, they deflagellate and activate their mating structures, which are two well-established Ca2+ responses (Schuring et al, 1990;Musgrave et al, 1992;Quarmby et al, 1992;Quarmby, 1994;Quarmby and Hartzell, 1994;Sanders and Salisbury, 1994). Using phosphorus-32 to monitor phospholipid turnover, these effects were shown to be correlated with the increased turnover of PtdlnsP2 and a dramatic rise in PtdOH, thought to reflect the phosphorylation of DAG by DAG kinase Quarmby et al, 1992); in retrospect, this rise in PtdOH could be due partially to PLD activity.…”

Section: Mastoparan-stimulated Formation Of Ptdohmentioning

confidence: 99%

“…The quantitative relation between these two pathways is currently being studied and will be presented in a later paper. However, PtdOH can be seen as a biologically active second messenger, because the two known responses to G protein activation, namely, deflagellation and mating struc ture activation (Schuring et al, 1990;Musgrave et al, 1992;Quarmby et al, 1992;Quarmby and Hartzell, 1994), are also induced by PtdOH treatment. Figure 5 shows the dose-dependent deflagellation induced by PtdOH.…”

Section: In Vivo Measurement Of Phospholipase D and Activation By Masmentioning

confidence: 99%

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G Protein Activation Stimulates Phospholipase D Signaling in Plants.

et al. 1995

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We provide direct evidence for phospholipase D (PLD) signaling i n plants by showing that this enzyme is stimulated by the G protein activators mastoparan, ethanol, and cholera toxin. An i n vivo assay for PLD activity i n plant cells was developed based on the use of a "reporter alcohol" rather than water as a transphosphatidylation substrate. The product was a phosphatidyl alcohol, which, in contrast to the normal product phosphatidic acid, i s a specific measure of PLD activity.When 32P-labeled cells were treated with 0.1% n-butanol, 3*P-phosphatidyl butanol (32P-PtdBut) was formed in a timedependent manner. In cells treated with any of the three G protein activators, the production of 32P-PtdBut was increased i n a dose-dependent manner. The G protein involved was pertussis toxin insensitive. Ethanol could activate PLD but was itself consumed by PLD as transphosphatidylation substrate. In contrast, secondary alcohols (e.g., sec-butyl alcohol) activated PLD but did not function as substrate, whereas tertiary alcohols did neither. Although most of the experiments were performed with the green alga Chlamydomonas eugametos, the relevance for higher plants was demonstrated by showing that PLD in carnation petals could also be activated by mastoparan. The results indicate that PLD activation must be considered as a potential signal transduction mechanism in plants, just as in animals.

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“…Chlamydomonas cells are able to increase the cytoplasmic concentration of calcium either via rhodopsinactivated channels in the cell body, voltage-gated channels on the¯agella (Hartz and Hegemann 1991;Beck and Uhl 1994) or by activating phospholipase C which hydrolyses phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (InsP 3 ; Musgrave et al 1992Musgrave et al , 1993Quarmby and Hartzell 1994). The InsP 3 can then induce the release of calcium from internal stores by binding to the InsP 3 receptor (Berridge 1993).…”

Section: Introductionmentioning

confidence: 99%

Characterisation and cloning of a calmodulin-like domain protein kinase from Chlamydomonas moewusii (Gerloff )

Siderius

Henskens

Porto-Leblanche

et al. 1997

Planta

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General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018Abstract. Calcium-stimulated protein kinase activity in the¯agella of the green alga Chlamydomonas moewusii (Gerlo ) was characterised. Using SDS-PAGE and an on-blot phosphorylation assay, a 65-kDa protein was identi®ed as the major calcium-stimulated protein kinase. Its activity was directly stimulated by calcium, a characteristic of the calmodulin-like domain protein kinases (CDPKs). Monoclonal antibodies raised against the CDPKa from soybean cross-reacted with the 65-kDa protein in the¯agella, and also with other proteins in thē agellum and cell body. The same monoclonal antibodies were used to screen a C. moewusii cDNA expression library in order to isolate CDPK cDNAs from C. moewusii. The CCK1 cDNA encodes a protein with a kinase and calmodulin-like domain linked by a junction domain typical of CDPKs. From Southern analyses, evidence was obtained for a CDPK gene family in C. moewusii and C. reinhardtii.

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Ethanol stimulates phospholipid turnover and inositol 1,4,5-trisphosphate production in Chlamydomonas eugametos gametes

Cited by 30 publications

References 32 publications

Rapid turnover of polyphosphoinositides in carnation flower petals

Rapid turnover of polyphosphoinositides in carnation flower petals

G Protein Activation Stimulates Phospholipase D Signaling in Plants.

Characterisation and cloning of a calmodulin-like domain protein kinase from Chlamydomonas moewusii (Gerloff )

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