Separation and Characterization of Inositol Phospholipids from the Pulvini of <i>Samanea saman</i>

Coté, Gary G.; DePass, Anthony L.; Quarmby, Lynne M.; Tate, Bonnie F.; Morse, M. J.; Satter, Ruth L.; Crain, Richard C.

doi:10.1104/pp.90.4.1422

Cited by 36 publications

(19 citation statements)

References 26 publications

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“…inositol was incorporated into PtdInsP but the level was very low, limiting our ability to detect its incorporation into PtdInsP 2. Much of the problem lay in the poor uptake together with metabolism of that which was taken up, and judging from our own observations (data not shown) and previous reports, this is typical of plant cells (Cot~ et al 1987;Drebak et al 1988;Cot6 et al 1989;Rinc6n et al 1989;Rinc6n and Boss 1990). The 32p-labelling kinetics of PtdInsP and PtdlnsP 2 during incorporation and pulse-chase experiments were obviously different from those of the structural lipids and were characteristic of lipids expressing a high turnover rate.…”

Section: Discussionsupporting

confidence: 62%

“…Analysis of PtdInsP in carnation petals showed the presence of both PtdIns(3)P and PtdIns(4)P. Since PtdIns(3)P has also been found in Chlamydomonas (Irvine et al 1992) and in the aquatic monocotylodon Spirodella polyrhiza (Brearley and Hanke 1992) its presence in carnation suggests that this signalling system, which is still being elucidated for animal cells (Downes and Carter 1991;Irvine 1992;Panayotou and Waterfield 1992), is also common in plants. The low level of PtdInsP 2 in carnation petals prevented us from analyzing this lipid for the presence of 3-isomers, but since the most prevalent isomer PtdIns(3,4)P 2 constitutes less than 1% of the PtdInsP 2 pool in animal and lower-plant cells (Downes and Carter 1991 ;Irvine et al 1992), we presume that the PtdInsP2 found in carnation is predominantly PtdIns(4,5)P2, as has been demonstrated earlier for other plants (Cot6 et al 1989;Irvine et al 1989).…”

Section: Discussionmentioning

confidence: 84%

“…Polyphosphoinositides have been identified in several plants, in various tissues (Sandelius and Sommarin 1990), and have been demonstrated to be identical to those found in animals, namely PtdIns(4)P and PtdIns(4,5)P 2 (Cot6 et al 1989;Irvine et al 1989). In addition, several enzymes involved in their metabolism, such as PtdIns kinase, PtdInsP kinase, DAG kinase, phospholipase C, and PtdInsP 2 monoesterase have been reported (Sandelius and Sommarin 1986;Heim and Wagner 1987;Pfaffmann et al 1987;McMurray and Irvine 1988;Sommarin and Sandelius 1988;Einspahr et al 1989;Tate et al 1989;Sandelius and Sommarin 1990;Kamada and Muto 1991;Lundberg and Sommarin 1992;Wissing et al 1989).…”

Section: Introductionmentioning

confidence: 99%

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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: Discussionsupporting

confidence: 62%

Section: Discussionmentioning

confidence: 84%

Section: Introductionmentioning

confidence: 99%

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Rapid turnover of polyphosphoinositides in carnation flower petals

Munnik¹,

Musgrave

Vrije³

1994

Planta

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“…The mechanism of IAA action might involve second messenger molecules derived from PI phosphate hydrolysis, such as diacylglycerol and IP3 and/or Ca2" ions. The presence of IP3 in plant tissues has been confirmed (4,6,12) and it has been shown that IP3 is able to promote calcium release from intracellular sources in plants, as well (8,21,22).…”

Section: Resultsmentioning

confidence: 85%

Comparison of the Effect of Indoleacetic Acid and Fusicoccin on the Breakdown of Phosphatidylinositol in Maize Coleoptiles

Zocchi¹

1990

Plant Physiol.

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The effect of indoleacetic acid (IAA) and fusicoccin (FC) on the breakdown of phosphatidylinositol in maize (Zea mays L.) coleoptiles has been studied. Coleoptiles were able to incorporate [3H] myo-inositol into the phospholipid fraction almost linearly for 8 hours. Thin layer chromatography analysis of total phospholipids showed that [3H]myo-inositol was incorporated only into phosphatidylinositol. Prelabeled coleoptiles treated with IAA showed a loss of the radioactivity incorporated in the phospholipid fraction, whose level decreased by 34% after 1 hour. Treatment with FC, on the contrary, did not modify the content of labelled phosphatidylinositol with respect to the control. The different effects of IAA and FC and a possible mechanism of IAA action on growth are discussed.IAA and FC treatment on the breakdown of phosphatidylinositol in maize coleoptiles is reported. MATERIALS AND METHODS Plant MaterialTwo millimeter coleoptile segments from 3-d-old etiolated maize seedlings (Zea mays L., cv DeKalb XL85) were used. Seeds were germinated at 26°C in the dark as already reported (24). The 2 mm segments were obtained by cutting the coleoptile cylinder with a multiblade device and then deblading the segments with a needle. TreatmentsTransducing mechanisms are very important to signal intraand extracellular stimuli to the cell. In animal cells the mechanisms involved in the translation of these signals (hormones, neurotransmitters, and growth factors) are linked to the hydrolysis of the phospholipidic fraction of the membrane. In particular, the hydrolysis of PI2 phosphates plays a major role in the flux ofthese signals through the release ofcalcium from internal stores induced by IP3 (1,3,15) The cylindrical segments so obtained, 1 g per test, were washed in distilled water and preincubated for 1 h in 10 mL of a buffer containing 5 mM sucrose and 2 mm Tris-Mes (pH 6.2). The preincubation buffer was then substituted with 10 mL of the same fresh buffer containing 0.37 kBq/mL of [3H] myo-inositol (Amersham) and the coleoptiles incubated for the desired time. After 2 h incubation, coleoptiles were carefully rinsed with fresh buffer and allowed to exchange free [3H]myo-inositol in 10 mL of the same buffer supplemented with 5 mm unlabeled myo-inositol for 15 min. After a new rinsing, 10 mL of fresh buffer containing l0-' M IAA or I0-' M FC were added and the coleoptiles allowed to incubate for the further desired time. All the incubations were carried out at 26°C in a thermoregulated and agitated water bath.

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“…Inositol phospholipids (2,4,13,21) and inositol phosphates (3) have been identified in plant tissues. Furthermore, IP3-stimulated release of calcium from plant microsomal vesicles (7) and from plant vacuolar vesicles (18) has been demonstrated.…”

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confidence: 99%

Characterization of a Polyphosphoinositide Phospholipase C from the Plasma Membrane of Avena sativa

Tate¹,

Schäller²,

Sussman³

et al. 1989

Plant Physiol.

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A phosphoinositide-specific phospholipase C activity was identified in oat root (Avena sativa, cv Victory) plasma membranes purified by separation in an aqueous two-phase polymer system. The enzyme is highly active toward inositol phospholipids but only minimally active toward phosphatidylethanolamine and phosphatidylcholine. Activity approaches maximal levels at 200 micromolar phosphatidylinositol 4-phosphate (PIP) and is highly dependent on calcium; it is inhibited by I millimolar EGTA and is activated by calcium with an apparent activation constant of 2 micromolar. At 10 micromolar calcium and 200 micromolar inositol phospholipid, the enzyme is specific for phosphatidylinositol 4,5-bisphosphate (PIP2) and PIP, which are hydrolyzed at 10 and 4 times, respectively, the rate of phosphatidylinositol (PI) We here report the presence of a phospholipase C activity in oat root plasma membranes purified by separation with an aqueous two-phase polymer system. Our findings show a phospholipase C activity that is calcium activated and is most active with the polyphosphoinositide substrate, PIP2. MATERIALS AND METHODS Plant MaterialSeeds of oats (Avena sativa, cv Victory) were planted in moist, fine vermiculite and grown at 25°C in constant darkness. Plants were harvested after 6 d and the roots were removed for isolation of membranes. Plasma Membrane IsolationAll membrane isolation procedures were performed at 4°C. Oat roots were homogenized with a Waring blender in a 0.25 M Tris-HCl buffer (pH 6.5) containing 1.15 M sucrose, 25 mM EDTA, 2 mm PMSF, and 70 mM 2-mercaptoethanol. The homogenate was then subjected to centrifugation at 8,000g for 15 min followed by centrifugation of the supernatant at 33,500g for 90 min. The resulting crude membrane pellet was resuspended in a 5 mm potassium phosphate buffer (pH 7.8) with 0.33 M sucrose and 4 mM KCI and the suspension was applied to a two-phase system containing 6.5% (w/w) dextran T500 and 6.5% (w/w) polyethylene glycol 3350 in the same buffer (9). After mixing by repeated inversions (30-35 times), the two phases were separated by a 5 min centrifugation at 1,500g. The upper phase, containing the plasma membrane vesicles, was then washed twice with fresh lower phase and diluted with an equal volume of Tris-HCl buffer (10 mM, pH 7.5) containing 0.33 M sucrose. After a 60 min centrifugation at 100,000g, the resulting pellet, which contained the purified plasma membranes, was resuspended in 1 mL of the above Tris-HCl buffer and stored in 100 1L aliquots at -70°C until use. Protein concentration of the purified membrane preparations was determined by the method of Lowry et al. (10

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Separation and Characterization of Inositol Phospholipids from the Pulvini of Samanea saman

Cited by 36 publications

References 26 publications

Rapid turnover of polyphosphoinositides in carnation flower petals

Rapid turnover of polyphosphoinositides in carnation flower petals

Comparison of the Effect of Indoleacetic Acid and Fusicoccin on the Breakdown of Phosphatidylinositol in Maize Coleoptiles

Characterization of a Polyphosphoinositide Phospholipase C from the Plasma Membrane of Avena sativa

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