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Differential Phospholipid-Labeling Suggests Two Subtypes of Phospholipase D in Rat Leydig Cells

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 1995 Denmark Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 217, pages 747-754 (issn: 0006-291X,

Authors: Lauritzen, L.; Hansen, Harald S.;

doi: 10.1006/bbrc.1995.2836

pmid: 8554594

Differential Phospholipid-Labeling Suggests Two Subtypes of Phospholipase D in Rat Leydig Cells

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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 [3H]phosphatidylethanol formation in response to 4 beta-phorbol 12-myristate 13-acetate (PMA), sphingosine, or Ca(++)-ionophore A23187, was lower when Leydig cells were labeled with 1-O-[3H]alkyl lysoPtdCho compared with the responses when [3H]myristic acid was employed. In contrast, the results for the receptor agonists (vasopressin, bradykinin, and lysophosphatidic acid), using the two labels, showed more 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.

Country

Denmark

Related Organizations

University of Copenhagen
Denmark
University of Copenhagen
Denmark

Keywords

Male, Leydig Cells, Rats, Substrate Specificity, Enzyme Activation, Rats, Sprague-Dawley, Sphingosine, Phorbol Esters, Phospholipase D, Animals, Calcimycin, Phospholipids

1 Research products, page 1 of 1

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