Polyphosphoinositides are present in plant tissue culture cells

Boss, Wendy F.; Massel, Mara

doi:10.1016/0006-291x(85)91908-4

Cited by 118 publications

(50 citation statements)

References 16 publications

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“…This compound migrates between the outlined PIP and PIP2 markers and possibly represents the phosphorylation of lysoP1 to form 1ysoPIP [ 121. A lysophosphatidylinositol kinase has been identified in human platelet microsomes [13], and a similar unidentified inositol lipid was observed by Boss and Masse1 [3]. Upon the addition of exogenous PI to the phosphorylation mixture the production of PIP is observed ( fig.2B).…”

Section: Resultssupporting

confidence: 70%

“…The major spots migrating close to the origin are, as yet, unidentified. However, they may represent inositol phosphates produced by breakdown of the phosphorylated lipids [3].…”

Section: Resultsmentioning

confidence: 99%

“…Boss and Masse1 [3] first identified the presence of polyphosphoinositides (PIP and PIP2) in plant membranes and Melin et al [4] demonstrated the presence of a polyphosphoinositide specific phospholipase C. Additionally, the presence of PI kinase and PIP kinase activities in plant plasma membranes has PIP, phosphatidylinositol monophosphate; PIP& phosphatidylinositol bisphosphate been demonstrated [5,6]. However, none of the above enzymes have been purified from plants.…”

Section: Introductionmentioning

confidence: 99%

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Phosphatidylinositol kinase activity of a plasma membrane‐associated calcium‐activated protein kinase from pea

Blowers

Trewavas

1988

FEBS Letters

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A purified protein kinase preparation from pea is shown to contain phosphatidylinositol kinase activity. The preparation, produced by membrane solubilisation and ATP‐agarose affinity chromatography, contains proteins of 18 kDa (ppl8, a calcium activated autophosphorylating protein‐serine kinase), 67 kDa and 48 kDa and exhibits the phosphorylation of an endogenous lipid when supplied with [γ‐32P]ATP. This product is tentatively identified as lysophosphatidylinositol phosphate. When supplied with [γ‐32P]ATP and exogenous phosphatidylinositol, the production of phosphatidylinositol phosphate is observed.

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Section: Resultssupporting

confidence: 70%

“…The major spots migrating close to the origin are, as yet, unidentified. However, they may represent inositol phosphates produced by breakdown of the phosphorylated lipids [3].…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Phosphatidylinositol kinase activity of a plasma membrane‐associated calcium‐activated protein kinase from pea

Blowers

Trewavas

1988

FEBS Letters

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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: 88%

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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“…The cycle has been well characterized in animal systems where it has been implicated in the transduction of hormonal and light stimuli (1). Boss and Massel (2) have presented evidence for the substrates of the PI cycle in a plant system. Evidence for the occurrence of the enzymes of the PI cycle in plants has also been reported (16,17,27), and there is evidence for hormone-stimulated metabolism of the cycle (6,8).…”

mentioning

confidence: 99%

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

Coté

DePass²,

Quarmby³

et al. 1989

Plant Physiol.

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To supplement current thin-layer chromatographic methods for separation and quantitation of plant phospholipids, an altemative method, high-performance liquid chromatography was developed. The major inositol-containing lipids from the pulvini of Samanea saman Merr. were identified as phosphatidylinositol, phosphatidylinositol phosphate, and phosphafidylinositol bisphosphate based on comigration with authentic standards on high-performance liquid chromatography and on thin-layer chromatography. The patterns of incorporation of radioactivity into the putative phosphatidylinositol and phosphatidylinositol phosphate were consistent with these identifications when pulvini were labeled with [3H]

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Polyphosphoinositides are present in plant tissue culture cells

Cited by 118 publications

References 16 publications

Phosphatidylinositol kinase activity of a plasma membrane‐associated calcium‐activated protein kinase from pea

Phosphatidylinositol kinase activity of a plasma membrane‐associated calcium‐activated protein kinase from pea

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

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

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