Phorbol ester and vasopressin activate phospholipase D in Leydig cells

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Phorbol ester and vasopressin activate phospholipase D in Leydig cells. / Vinggaard, Anne Marie; Hansen, Harald S.

In: Molecular and Cellular Endocrinology, Vol. 79, No. 1-3, 01.01.1991, p. 157-165.

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

Harvard

Vinggaard, AM & Hansen, HS 1991, 'Phorbol ester and vasopressin activate phospholipase D in Leydig cells', Molecular and Cellular Endocrinology, vol. 79, no. 1-3, pp. 157-165.

APA

Vinggaard, A. M., & Hansen, H. S. (1991). Phorbol ester and vasopressin activate phospholipase D in Leydig cells. Molecular and Cellular Endocrinology, 79(1-3), 157-165.

Vancouver

Vinggaard AM, Hansen HS. Phorbol ester and vasopressin activate phospholipase D in Leydig cells. Molecular and Cellular Endocrinology. 1991 Jan 1;79(1-3):157-165.

Author

Vinggaard, Anne Marie ; Hansen, Harald S. / Phorbol ester and vasopressin activate phospholipase D in Leydig cells. In: Molecular and Cellular Endocrinology. 1991 ; Vol. 79, No. 1-3. pp. 157-165.

Bibtex

@article{ff0b5e1d78a94be28a76e28cfa56b06a,
title = "Phorbol ester and vasopressin activate phospholipase D in Leydig cells",
abstract = "In the present study evidence is provided for the existence of phospholipase D (PLD) activity in rat Leydig cells. Leydig cells were cultured and labelled with [H]myristic acid. In the presence of ethanol, phorbol 12-myristate 13-acetate (PMA) stimulated the formation of [H]phosphatidylethanol ([H]PEt) in a dose-dependent manner at the expense of [H]phosphatidic acid ([H]PA). In cells prelabelled with [H]choline, PMA caused a rapid increase in intracellular free [H]choline. The time course of [H]PEt formation was similar to the time course of intracellular [H]choline formation. The data taken together support the notion that PMA stimulates phosphatidylcholine (PC) hydrolysis by a mechanism, which principally involves PLD. Activation of PLD by PMA was inhibited by long-term pretreatment of cells with PMA to downregulate protein kinase C (PKC) and by pretreatment with staurosporine. These data support the notion that activation of PLD by PMA is dependent on PKC. Arginine vasopressin (AVP) caused a rapid stimulation of PLD activity in the cells. This activation was inhibited after downregulation of PKC, indicating that the agonist acts by a mechanism similar to that of PMA.",
author = "Vinggaard, {Anne Marie} and Hansen, {Harald S.}",
year = "1991",
month = jan,
day = "1",
language = "English",
volume = "79",
pages = "157--165",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "1-3",

}

RIS

TY - JOUR

T1 - Phorbol ester and vasopressin activate phospholipase D in Leydig cells

AU - Vinggaard, Anne Marie

AU - Hansen, Harald S.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - In the present study evidence is provided for the existence of phospholipase D (PLD) activity in rat Leydig cells. Leydig cells were cultured and labelled with [H]myristic acid. In the presence of ethanol, phorbol 12-myristate 13-acetate (PMA) stimulated the formation of [H]phosphatidylethanol ([H]PEt) in a dose-dependent manner at the expense of [H]phosphatidic acid ([H]PA). In cells prelabelled with [H]choline, PMA caused a rapid increase in intracellular free [H]choline. The time course of [H]PEt formation was similar to the time course of intracellular [H]choline formation. The data taken together support the notion that PMA stimulates phosphatidylcholine (PC) hydrolysis by a mechanism, which principally involves PLD. Activation of PLD by PMA was inhibited by long-term pretreatment of cells with PMA to downregulate protein kinase C (PKC) and by pretreatment with staurosporine. These data support the notion that activation of PLD by PMA is dependent on PKC. Arginine vasopressin (AVP) caused a rapid stimulation of PLD activity in the cells. This activation was inhibited after downregulation of PKC, indicating that the agonist acts by a mechanism similar to that of PMA.

AB - In the present study evidence is provided for the existence of phospholipase D (PLD) activity in rat Leydig cells. Leydig cells were cultured and labelled with [H]myristic acid. In the presence of ethanol, phorbol 12-myristate 13-acetate (PMA) stimulated the formation of [H]phosphatidylethanol ([H]PEt) in a dose-dependent manner at the expense of [H]phosphatidic acid ([H]PA). In cells prelabelled with [H]choline, PMA caused a rapid increase in intracellular free [H]choline. The time course of [H]PEt formation was similar to the time course of intracellular [H]choline formation. The data taken together support the notion that PMA stimulates phosphatidylcholine (PC) hydrolysis by a mechanism, which principally involves PLD. Activation of PLD by PMA was inhibited by long-term pretreatment of cells with PMA to downregulate protein kinase C (PKC) and by pretreatment with staurosporine. These data support the notion that activation of PLD by PMA is dependent on PKC. Arginine vasopressin (AVP) caused a rapid stimulation of PLD activity in the cells. This activation was inhibited after downregulation of PKC, indicating that the agonist acts by a mechanism similar to that of PMA.

UR - http://www.scopus.com/inward/record.url?scp=0025739305&partnerID=8YFLogxK

M3 - Journal article

AN - SCOPUS:0025739305

VL - 79

SP - 157

EP - 165

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 1-3

ER -

ID: 45562187