Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells

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Standard

Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells. / Lauritzen, L.; Hansen, Harald S.

I: Biochemical and Biophysical Research Communications, Bind 217, Nr. 3, 01.01.1995, s. 747-754.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lauritzen, L & Hansen, HS 1995, 'Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells', Biochemical and Biophysical Research Communications, bind 217, nr. 3, s. 747-754. https://doi.org/10.1006/bbrc.1995.2836

APA

Lauritzen, L., & Hansen, H. S. (1995). Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells. Biochemical and Biophysical Research Communications, 217(3), 747-754. https://doi.org/10.1006/bbrc.1995.2836

Vancouver

Lauritzen L, Hansen HS. Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells. Biochemical and Biophysical Research Communications. 1995 jan. 1;217(3):747-754. https://doi.org/10.1006/bbrc.1995.2836

Author

Lauritzen, L. ; Hansen, Harald S. / Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells. I: Biochemical and Biophysical Research Communications. 1995 ; Bind 217, Nr. 3. s. 747-754.

Bibtex

@article{5e726a6ee1324bc18d2acd19a9067720,
title = "Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells",
abstract = "The aim of the present study was to compare the transphosphatidylation activity of phospholipase D (PLD) under different substrate labeling conditions, in order to investigate whether PLD in rat Leydig cells exhibited any substrate preferences for the alkyl- or acyl-form of phosphatidylcholine (PtdCho). The [H] phosphatidylethanol formation in response to 4{\ss}-phorbol 12-myristate 13-acetate (PMA), sphingosine, or Ca-ionophore A23187, was lower when Leydig cells were labeled with 1-O-[H]alkyl lysoPtdCho compared with the responses when [H]myristic acid was employed. In contrast, the results for the receptor agonists (vasopressin, bradykinin, and lysophosphatidic acid), using the two labels, showed mole consistency. Thus, the PLD-activity induced by PMA, sphingosine, or A23187 has a more selective substrate range (i.e. mainly acyl-linked PtdCho) than the PLD-activity stimulated via a receptor. Our data suggests the existence of PLD isozymes that differ with respect to substrate specificity and activation mechanisms.",
author = "L. Lauritzen and Hansen, {Harald S.}",
year = "1995",
month = jan,
day = "1",
doi = "10.1006/bbrc.1995.2836",
language = "English",
volume = "217",
pages = "747--754",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Differential phospholipid-labeling suggests two subtypes of phospholipase D in rat Leydig cells

AU - Lauritzen, L.

AU - Hansen, Harald S.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - The aim of the present study was to compare the transphosphatidylation activity of phospholipase D (PLD) under different substrate labeling conditions, in order to investigate whether PLD in rat Leydig cells exhibited any substrate preferences for the alkyl- or acyl-form of phosphatidylcholine (PtdCho). The [H] phosphatidylethanol formation in response to 4ß-phorbol 12-myristate 13-acetate (PMA), sphingosine, or Ca-ionophore A23187, was lower when Leydig cells were labeled with 1-O-[H]alkyl lysoPtdCho compared with the responses when [H]myristic acid was employed. In contrast, the results for the receptor agonists (vasopressin, bradykinin, and lysophosphatidic acid), using the two labels, showed mole consistency. Thus, the PLD-activity induced by PMA, sphingosine, or A23187 has a more selective substrate range (i.e. mainly acyl-linked PtdCho) than the PLD-activity stimulated via a receptor. Our data suggests the existence of PLD isozymes that differ with respect to substrate specificity and activation mechanisms.

AB - The aim of the present study was to compare the transphosphatidylation activity of phospholipase D (PLD) under different substrate labeling conditions, in order to investigate whether PLD in rat Leydig cells exhibited any substrate preferences for the alkyl- or acyl-form of phosphatidylcholine (PtdCho). The [H] phosphatidylethanol formation in response to 4ß-phorbol 12-myristate 13-acetate (PMA), sphingosine, or Ca-ionophore A23187, was lower when Leydig cells were labeled with 1-O-[H]alkyl lysoPtdCho compared with the responses when [H]myristic acid was employed. In contrast, the results for the receptor agonists (vasopressin, bradykinin, and lysophosphatidic acid), using the two labels, showed mole consistency. Thus, the PLD-activity induced by PMA, sphingosine, or A23187 has a more selective substrate range (i.e. mainly acyl-linked PtdCho) than the PLD-activity stimulated via a receptor. Our data suggests the existence of PLD isozymes that differ with respect to substrate specificity and activation mechanisms.

UR - http://www.scopus.com/inward/record.url?scp=0029417188&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1995.2836

DO - 10.1006/bbrc.1995.2836

M3 - Journal article

AN - SCOPUS:0029417188

VL - 217

SP - 747

EP - 754

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

ID: 45561551