Phospholipase D has been recognized as playing an important role in signal transduction in many types of cells. We investigated the expression of phospholipase D during the differentiation of F9 embryonal teratocarcinoma cells. The ADP ribosylation factor-dependent phospholipase D activity, as measured by an in vitro assay, and H2O2-induced phospholipase D activity and phospholipase D protein content in whole cells were decreased during the differentiation of F9 cells induced by a combination of dibutyryl cyclic AMP and all-trans retinoic acid. In contrast, these changes were not observed when cells were induced by retinoic acid. These results suggest that down-regulation of phospholipase D protein is associated with differentiation of F9 cells to a parietal endoderm lineage. Copyright (C) 1999 Federation of European Biochemical Societies.
Bibliographical noteFunding Information:
A~knowledgements." This work was supported by a research Grant (HMP-98-N-1-0012) from the Good Health R and D Project and the Ministry of Health and Welfare, R.O.K.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology