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={Michael Palmgren and Marianne Sommarin and Peter Ulvlskov and Peter Leth 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… 
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125 Citations

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 roots using an aqueous polymer two-phase system and the curve for the stability of soluble H+, ATPase as a function of pH closely resembles the pH Curve for the activity of the H+, which suggests that binding of protons to transport sites may stabilize the soluble H-atPase in an enzymatically active form.

Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles.

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.

Rapid purification of the plasma membrane H+-ATPase in its non-activated form using FPLC

The plasma membrane H-ATPase purified in the presence of glycerol and ATP showed no loss in activity during 8 h on ice nor upon freezing at -80°C and thawing, and the recovery was up to 75%.

Effect of lysophosphatidylcholine on the NADH-ferricyanide reductase activity associated with the plasma membranes of corn roots

Fusicoccin Activates the Plasma Membrane H+-ATPase by a Mechanism Involving the C-Terminal Inhibitory Domain.

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.

Kinetics of the purified plasma membrane H+‐ATPase from red beet (Beta vulgaris)

The plasma membrane H+-ATPase was purified by washing red beet plasma membranes with sodium deoxycholate and separating the ATPase, solubilized with lysophosphatidylcholine, by centrifugation in a glycerol gradient, and presented a higher affinity for adenosine 5′-triphosphate (ATP) and a lower sensitivity to the inhibitors vanadate and inorganic phosphate.

Selective Delipidation of the Plasma Membrane by

It is suggested that surfactants activate the ATPase by altering the hydrophobic environment around the enzyme, and proposed that sterols, through their interaction with the ATP enzyme, may be essential for ATPase activity.

Selective delipidation of the plasma membrane by surfactants : enrichment of sterols and activation of ATPase.

It is suggested that surfactants activate the ATPase by altering the hydrophobic environment around the enzyme, and proposed that sterols, through their interaction with the ATP enzyme, may be essential for ATPase activity.

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)

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.

Plasma Membrane H+-ATPase in Maize Roots Induced for NO3- Uptake

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.
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