Phospholipase D Activity in PC12 Cells
| Autor: | Jin Hyouk Park, Krishna M. Ella, Anthony F. McNair, Kathryn E. Meier, April E. Wisehart-Johnson, Chen Qi |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Phospholipase D
Cellular differentiation PC12 cell line Cell Biology Biology Pertussis toxin Biochemistry Cell biology enzymes and coenzymes (carbohydrates) chemistry.chemical_compound chemistry Heterotrimeric G protein Phorbol Phospholipase D activity lipids (amino acids peptides and proteins) Receptor Molecular Biology |
| Zdroj: | Journal of Biological Chemistry. 272:12909-12912 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.20.12909 |
| Popis: | PC12 neuronal cells express a membrane phospholipase D (PLD) activity that is detected at similar levels in undifferentiated or differentiated cells. The regulation of this activity by agonists was explored. Membrane phospholipase D activity was increased by treatment of cells with the phorbol ester phorbol 12-myristate 13-acetate (PMA) or with nerve growth factor. The ability of PMA to activate PLD was confirmed in intact PC12 cells. Basal activity of PLD in membranes was reduced in RG20, a PC12 cell line overexpressing the human α2A-adrenergic receptor. PMA did not increase PLD activity in RG20 cells, as assessed both in membrane preparations and in intact cells. Cyclic AMP levels did not regulate phospholipase D activity in either cell type. However, incubation of RG20 cells with the α2-adrenergic antagonist rauwolscine or with pertussis toxin increased membrane PLD activity and restored activation of PLD by PMA. These data suggest that the effects of the overexpressed α2A-adrenergic receptor on PLD activity are mediated by precoupling of the receptor to the heterotrimeric GTP-binding protein, Gi, but are independent of adenylate cyclase regulation. The results of this study suggest that membrane phospholipase D activity can be negatively regulated via Gi in PC12 cells. |
| Databáze: | OpenAIRE |
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