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rdf:type
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Description
| - Práce se zabývá molekulárním mechanismem toxického působení iontů hlinitých. Jako modelový rostlinný materiál byla použita tabáková buněčná linie BY-2. Práce ukazuje, že ionty hlinité snižují in vivo hladinu kyseliny fosfatidové a inhibují in vitro aktivitu fosfolipasy D závislé na fosfatidyl-4,5-bisfosfátu. Snížení hladiny kys. fosfatidové je závislé na stavu mikrotubulů. (cs)
- Aluminum is a highly cytotoxic metal to plants, but the molecular base and the primary target of Al toxicity are still unknown. The most important physiological consequence of Al toxicity is a cessation of root growth and changes in root morphology suggesting a role of the root cytoskeleton as a target structure. The important role of phospholipid degrading enzyme phospholipase D in regulation of cytoskeleton remodelling in both animal and plant organisms is now evident. Both the phospholipid pathway and the cytoskeleton are influenced by Al3þ, but their relationship with Al stress remains to be explored. Therefore, we tested the possibility that Al stress could be sensed by plants through microtubules in close interaction with phospholipases. We have shown that Al3þ reduced the formation of phosphatidic acid in vivo, inhibited activity of phosphatidylinositol-4,5-bisphosphate-dependent phospholipase D in vitro and that the phosphatidic acid production is modified by microtubule dynamics.
- Aluminum is a highly cytotoxic metal to plants, but the molecular base and the primary target of Al toxicity are still unknown. The most important physiological consequence of Al toxicity is a cessation of root growth and changes in root morphology suggesting a role of the root cytoskeleton as a target structure. The important role of phospholipid degrading enzyme phospholipase D in regulation of cytoskeleton remodelling in both animal and plant organisms is now evident. Both the phospholipid pathway and the cytoskeleton are influenced by Al3þ, but their relationship with Al stress remains to be explored. Therefore, we tested the possibility that Al stress could be sensed by plants through microtubules in close interaction with phospholipases. We have shown that Al3þ reduced the formation of phosphatidic acid in vivo, inhibited activity of phosphatidylinositol-4,5-bisphosphate-dependent phospholipase D in vitro and that the phosphatidic acid production is modified by microtubule dynamics. (en)
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Title
| - Aluminum ions inhibit phospholipase D in a microtubule-dependent manner
- Aluminum ions inhibit phospholipase D in a microtubule-dependent manner (en)
- Ionty hlinité inhibují fosfolipasu D v závislosti na stavu mikrotubulů (cs)
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skos:prefLabel
| - Aluminum ions inhibit phospholipase D in a microtubule-dependent manner
- Aluminum ions inhibit phospholipase D in a microtubule-dependent manner (en)
- Ionty hlinité inhibují fosfolipasu D v závislosti na stavu mikrotubulů (cs)
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skos:notation
| - RIV/61389030:_____/08:00319645!RIV09-AV0-61389030
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - P(GA522/05/0340), Z(AV0Z50380511)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61389030:_____/08:00319645
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - Aluminum toxicity; Phospholipase D; Microtubules (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - GB - Spojené království Velké Británie a Severního Irska
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Cell Biology International
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Martinec, Jan
- Novotná, Z.
- Valentová, O.
- Pejchar, Přemysl
- Schwarzerová, K.
- Pleskot, R.
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http://linked.open...ain/vavai/riv/wos
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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