Regulation of phospholipase D activity in neuroblastoma cells.

Abstract

The regulation of phospholipase D was studied in human neuroblastoma cells using phosphatidylethanol as a marker of the enzyme activity. Carbachol induced phospholipase D activity in SH-SY5Y cells. Muscarinic antagonists inhibited the response with potencies suggesting that muscarinic M1 receptors are responsible for the activation. In permeabilized SH-SY5Y cells, both the carbachol- and GTP gamma S-induced Peth formation was inhibited by GDP beta S, indicating that both responses are mediated via a G-protein. The protein kinase C inhibitors, bisindolylmaleimide and staurosporine significantly inhibited the carbachol-induced Peth formation whereas H7 had no effect. Thus, the cholinergic activation of phospholipase D in SH-SY5Y cells is probably mediated via a direct receptor-G-protein coupling but an involvement of protein kinase C cannot be excluded. Calmidazolium, a calmodulin antagonist, induced an increase in phosphatidylethanol formation in both SH-SY5Y and IMR-32 cells. This effect was inhibited by genistein and tyrphostin, indicating a tyrosine kinase dependent pathway for phospholipase D activation in neuroblastoma cells.

• Authors: L Gustavsson, M C Boyano-Adánez, C Larsson, S Aradottir, C Lundqvist
• Journal: Journal of lipid mediators and cell signalling (J Lipid Mediat Cell Signal) Vol. 14 Issue 1-3 Pg. 229-35 (Sep 1996) ISSN: 0929-7855 [Print] Netherlands
• PMID: 8906567 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Muscarinic Antagonists
• Receptors, Muscarinic
• Phospholipase D

Topics

• Humans
• Muscarinic Antagonists (pharmacology)
• Neuroblastoma (metabolism)
• Phospholipase D (metabolism)
• Receptors, Muscarinic (metabolism)
• Signal Transduction (drug effects)
• Tumor Cells, Cultured