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

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L. Lauritzen, Harald S. Hansen

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.
OriginalsprogEngelsk
TidsskriftBiochemical and Biophysical Research Communications
Vol/bind217
Udgave nummer3
Sider (fra-til)747-754
Antal sider8
ISSN0006-291X
DOI
StatusUdgivet - 1 jan. 1995

ID: 45561551