Kanfer J N, McCartney D G, Singh I N, Freysz L
Department of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Canada.
FEBS Lett. 1996 Mar 25;383(1-2):6-8. doi: 10.1016/0014-5793(96)00205-0.
An oleate dependent form of phospholipase D is present in rat brain neuronal nuclei and both the hydrolytic and transphosphatidylation activities measured. Several acidic phospholipids were found to inhibit this activity in a dose dependent manner. The IC50 values varied from 3.5 microM for PIP2 to 200 microM for phosphatidic acid. The hydrolysis of PIP2 by phospholipase C would be expected to result in the disinhibition of the oleate dependent phospholipase D activity.