Modulation of plasma membrane H+-ATPase from oat roots by lysophosphatidylcholine, free fatty acids and phospholipase A2

@article{Palmgren1988ModulationOP,
  title={Modulation of plasma membrane H+-ATPase from oat roots by lysophosphatidylcholine, free fatty acids and phospholipase A2},
  author={M. Palmgren and M. Sommarin and Peter Ulvlskov and P. L. J{\o}rgensen},
  journal={Physiologia Plantarum},
  year={1988},
  volume={74},
  pages={11-19}
}
Plasma membrane vesicles were purified from 8-day-old oat (Avena sativa L. cv. Brighton) roots in an aqueous polymer two-phase system. The plasma membranes possessed high specific ATPase activity [ca 4 μmol P1 (mg protein)−1 min−1 at 37°C]. Addition of lysophosphatidylcholine (lyso-PC) produced a 2–3 fold activation of the plasma membrane ATPase, an effect due both to exposure of latent ATP binding sites and to a true activation of the enzyme. Lipid activation increased the affinity for ATP and… Expand
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Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots
Plasma membrane vesicles with H+-ATPase activity were purified from 8-day-old oat (Avena sativa L. cv. Brighton) roots using an aqueous polymer two-phase system. Of several detergents tested, only… Expand
Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles.
TLDR
The stimulatory effect of lysophospholipids suggests that these compounds could be part of the regulatory system for plant plasma membrane H(+)-ATPase activity in vivo. Expand
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The plasma membrane H-ATPase (EC 3.1.6.35) was solubilized from isolated spinach (Spinacia oleracea) leaf plasma membranes using the detergent dodecyl-β-d-maltoside and subsequently purified to near… Expand
Effect of lysophosphatidylcholine on the NADH-ferricyanide reductase activity associated with the plasma membranes of corn roots
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From these experiments, it is postulated that the reductase, which exhibits an optimum pH at 7.0 and is slightly stimulated by LPC, could be located on the external side of the plasmalemma, such as the catalytic site of ATPase. Expand
Fusicoccin Activates the Plasma Membrane H+-ATPase by a Mechanism Involving the C-Terminal Inhibitory Domain.
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The data suggest that in vivo activation of the H+-ATPase by fusicoccin proceeds by a mechanism involving a displacement of the C-terminal inhibitory domain. Expand
Kinetics of the purified plasma membrane H+‐ATPase from red beet (Beta vulgaris)
The plasma membrane H+-ATPase (EC 3.6.1.35) was purified by washing red beet (Beta vulgaris L.) plasma membranes with sodium deoxycholate and separating the ATPase, solubilized with… Expand
Selective Delipidation of the Plasma Membrane by
The influence of plasma membrane lipid components on the activity of the H+-ATPase has been studied by determining the effect of surfactants on membrane lipids and ATPase activity of oat (Avena… Expand
Modulation of H+-ATPase Activity by Fusicoccin in Plasma Membrane Vesicles from Oat (Avena sativa L.) Roots (A Comparison of Modulation by Fusicoccin, Trypsin, and Lysophosphatidylcholine)
TLDR
Kinetic analysis of the pH dependency curves revealed different mechanisms for activation by fusicoccin and by lyso-PC, and the involvement of the C-terminal inhibitory domain in the fusICoccin signal transduction chain seemed to increase dephosphorylation independently of pH. Expand
Plasma Membrane H+-ATPase in Maize Roots Induced for NO3- Uptake
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Results are consistent with the idea of an involvement of plasma membrane H+-ATPase in the overall response of roots to NO3- and kinetics of NO3-- or Cl--stimulated ATP-dependent intravesicular H+ accumulation were modified in plasma membrane vesicles isolated from NO3)-- induced roots. Expand
Multiple Effects of Lysophosphatidylcholine on the Activity of the Plasma Membrane H+‐ATPase of Radish Seedlings*
: We analyzed the effect of lysophosphatidylcholine (lysoPC) on the activity of the plasma membrane (PM) H+-AT-Pase measured at pH 6.3 or 7.5 in inside-out PM vesicles isolated from germinating… Expand
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