Characterization of phospholipase D activation by muscarinic receptors in human neuroblastoma SH-SY5Y cells
(1997) In Neuropharmacology 36(3). p.295-304- Abstract
- The cholinergic regulation of phospholipase D activity was studied in SH-SY5Y human neuroblastoma cells with phosphatidylethanol formation as a specific marker for the enzyme activity. The muscarinic antagonists, hexahydrosiladifenidol and pirenzepine, inhibited carbachol-induced phosphatidylethanol formation in a concentration-dependent manner and the inhibitory constants indicated that muscarinic M1 receptors are responsible for the major part of the phospholipase D activation. The mechanism of receptor-mediated phospholipase D activation varies between different cell types and receptors. In SH-SY5Y cells, the carbachol-induced phospholipase D activity was inhibited by protein kinase C inhibitors. Since both phospholipases D and C are... (More)
- The cholinergic regulation of phospholipase D activity was studied in SH-SY5Y human neuroblastoma cells with phosphatidylethanol formation as a specific marker for the enzyme activity. The muscarinic antagonists, hexahydrosiladifenidol and pirenzepine, inhibited carbachol-induced phosphatidylethanol formation in a concentration-dependent manner and the inhibitory constants indicated that muscarinic M1 receptors are responsible for the major part of the phospholipase D activation. The mechanism of receptor-mediated phospholipase D activation varies between different cell types and receptors. In SH-SY5Y cells, the carbachol-induced phospholipase D activity was inhibited by protein kinase C inhibitors. Since both phospholipases D and C are activated by muscarinic stimulation in SH-SY5Y cells, most of the phospholipase D activation is probably secondary to the protein kinase C activation that follows phospholipase C-mediated increase in diacylglycerols. Other kinases may be involved in the regulation since also a tyrosine kinase inhibitor decreased the phosphatidylethanol formation. Stimulation of G-protein(s) and increase in the intracellular Ca2+ concentration activated phospholipase D and may be additional mechanisms for the muscarinic regulation of phospholipase D in SH-SY5Y cells. Propranolol, an inhibitor of phosphatidic acid phosphohydrolase, increased the carbachol-induced formation of phosphatidic acid at the expense of 1,2-diacylglycerol. This indicates that phospholipase D contributes to the formation of 1,2-diacylglycerol after carbachol stimulation in SH-SY5Y cells. (Less)
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- author
- Boyano-Adanez, M C ; Lundqvist, C ; Larsson, Christer LU and Gustavsson, L
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- G-protein, acetylcholine, muscarinic receptor, phosphatidylethanol, phospholipase D, protein kinases, signal transduction
- in
- Neuropharmacology
- volume
- 36
- issue
- 3
- pages
- 295 - 304
- publisher
- Elsevier
- external identifiers
-
- pmid:9175607
- scopus:0343416940
- ISSN
- 1873-7064
- DOI
- 10.1016/S0028-3908(96)00178-5
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Tumour Cell Biology (013017530)
- id
- 1b8edece-ac08-4e30-9e8c-455b71ce3ca9 (old id 1111182)
- date added to LUP
- 2016-04-01 11:52:59
- date last changed
- 2022-01-26 19:37:15
@article{1b8edece-ac08-4e30-9e8c-455b71ce3ca9,
abstract = {{The cholinergic regulation of phospholipase D activity was studied in SH-SY5Y human neuroblastoma cells with phosphatidylethanol formation as a specific marker for the enzyme activity. The muscarinic antagonists, hexahydrosiladifenidol and pirenzepine, inhibited carbachol-induced phosphatidylethanol formation in a concentration-dependent manner and the inhibitory constants indicated that muscarinic M1 receptors are responsible for the major part of the phospholipase D activation. The mechanism of receptor-mediated phospholipase D activation varies between different cell types and receptors. In SH-SY5Y cells, the carbachol-induced phospholipase D activity was inhibited by protein kinase C inhibitors. Since both phospholipases D and C are activated by muscarinic stimulation in SH-SY5Y cells, most of the phospholipase D activation is probably secondary to the protein kinase C activation that follows phospholipase C-mediated increase in diacylglycerols. Other kinases may be involved in the regulation since also a tyrosine kinase inhibitor decreased the phosphatidylethanol formation. Stimulation of G-protein(s) and increase in the intracellular Ca2+ concentration activated phospholipase D and may be additional mechanisms for the muscarinic regulation of phospholipase D in SH-SY5Y cells. Propranolol, an inhibitor of phosphatidic acid phosphohydrolase, increased the carbachol-induced formation of phosphatidic acid at the expense of 1,2-diacylglycerol. This indicates that phospholipase D contributes to the formation of 1,2-diacylglycerol after carbachol stimulation in SH-SY5Y cells.}},
author = {{Boyano-Adanez, M C and Lundqvist, C and Larsson, Christer and Gustavsson, L}},
issn = {{1873-7064}},
keywords = {{G-protein; acetylcholine; muscarinic receptor; phosphatidylethanol; phospholipase D; protein kinases; signal transduction}},
language = {{eng}},
number = {{3}},
pages = {{295--304}},
publisher = {{Elsevier}},
series = {{Neuropharmacology}},
title = {{Characterization of phospholipase D activation by muscarinic receptors in human neuroblastoma SH-SY5Y cells}},
url = {{http://dx.doi.org/10.1016/S0028-3908(96)00178-5}},
doi = {{10.1016/S0028-3908(96)00178-5}},
volume = {{36}},
year = {{1997}},
}