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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles. / Palmgren, Michael Gjedde; Sommarin, Marianne.

In: Plant Physiology, Vol. 90, No. 3, 07.1989, p. 1009-1014.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Palmgren, MG & Sommarin, M 1989, 'Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles', Plant Physiology, vol. 90, no. 3, pp. 1009-1014. https://doi.org/10.1104/pp.90.3.1009

APA

Palmgren, M. G., & Sommarin, M. (1989). Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles. Plant Physiology, 90(3), 1009-1014. https://doi.org/10.1104/pp.90.3.1009

Vancouver

Palmgren MG, Sommarin M. Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles. Plant Physiology. 1989 Jul;90(3):1009-1014. https://doi.org/10.1104/pp.90.3.1009

Author

Palmgren, Michael Gjedde ; Sommarin, Marianne. / Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles. In: Plant Physiology. 1989 ; Vol. 90, No. 3. pp. 1009-1014.

Bibtex

@article{817e8a8a0d3f4d3d86df6414e96bb3e9,
title = "Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles",
abstract = "Lysophosphatidylcholine at concentrations of 30 micromolar stimulated the rate of MgATP-dependent H+-accumulation in oat (Avena sativa L. cv Rhiannon) root plasma membrane vesicles about 85% while the passive permeability of H+ was unchanged. Activation was dependent on chain length, degree of saturation, and head group of the lysophospholipid. A H+-ATPase assay was developed that allowed the simultaneous measurement of proton pumping and ATPase activity in the same sample. ATP hydrolysis was also stimulated by lysophospholipids and showed the same lipid specificity, but stimulation was only about 25% at 30 micromolar. At higher concentrations of lysophosphatidylcholine the ATPase activity in a latency-free system could be stimulated about 150%. The enzymic properties of proton pumping and ATP hydrolysis were otherwise identical with respect to vanadate sensitivity, Km for ATP and pH optimum. 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.",
author = "Palmgren, {Michael Gjedde} and Marianne Sommarin",
year = "1989",
month = jul,
doi = "10.1104/pp.90.3.1009",
language = "English",
volume = "90",
pages = "1009--1014",
journal = "Plant Physiology",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "3",

}

RIS

TY - JOUR

T1 - Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles

AU - Palmgren, Michael Gjedde

AU - Sommarin, Marianne

PY - 1989/7

Y1 - 1989/7

N2 - Lysophosphatidylcholine at concentrations of 30 micromolar stimulated the rate of MgATP-dependent H+-accumulation in oat (Avena sativa L. cv Rhiannon) root plasma membrane vesicles about 85% while the passive permeability of H+ was unchanged. Activation was dependent on chain length, degree of saturation, and head group of the lysophospholipid. A H+-ATPase assay was developed that allowed the simultaneous measurement of proton pumping and ATPase activity in the same sample. ATP hydrolysis was also stimulated by lysophospholipids and showed the same lipid specificity, but stimulation was only about 25% at 30 micromolar. At higher concentrations of lysophosphatidylcholine the ATPase activity in a latency-free system could be stimulated about 150%. The enzymic properties of proton pumping and ATP hydrolysis were otherwise identical with respect to vanadate sensitivity, Km for ATP and pH optimum. 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.

AB - Lysophosphatidylcholine at concentrations of 30 micromolar stimulated the rate of MgATP-dependent H+-accumulation in oat (Avena sativa L. cv Rhiannon) root plasma membrane vesicles about 85% while the passive permeability of H+ was unchanged. Activation was dependent on chain length, degree of saturation, and head group of the lysophospholipid. A H+-ATPase assay was developed that allowed the simultaneous measurement of proton pumping and ATPase activity in the same sample. ATP hydrolysis was also stimulated by lysophospholipids and showed the same lipid specificity, but stimulation was only about 25% at 30 micromolar. At higher concentrations of lysophosphatidylcholine the ATPase activity in a latency-free system could be stimulated about 150%. The enzymic properties of proton pumping and ATP hydrolysis were otherwise identical with respect to vanadate sensitivity, Km for ATP and pH optimum. 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.

UR - http://www.scopus.com/inward/record.url?scp=84969785201&partnerID=8YFLogxK

U2 - 10.1104/pp.90.3.1009

DO - 10.1104/pp.90.3.1009

M3 - Journal article

AN - SCOPUS:84969785201

VL - 90

SP - 1009

EP - 1014

JO - Plant Physiology

JF - Plant Physiology

SN - 0032-0889

IS - 3

ER -

ID: 245001765