Regulation of phospholipase D activity in neuroblastoma cells
(1996) In Journal of Lipid Mediators and Cell Signalling 14(1-3). p.229-235- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1109867
- author
- Gustavsson, Lena ; Boyano-Adanez, Maria del Carmen ; Larsson, Christer LU ; Aradottir, Steina LU and Lundqvist, Cristofer
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Calmidazolium, Muscarinic receptors, Phosphatidylethanol, Phosphatidic acid, Phospholipase D, Signal transduction
- in
- Journal of Lipid Mediators and Cell Signalling
- volume
- 14
- issue
- 1-3
- pages
- 229 - 235
- publisher
- Elsevier
- external identifiers
-
- pmid:8906567
- scopus:0030238946
- ISSN
- 0929-7855
- DOI
- 10.1016/0929-7855(96)00530-5
- 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: Oncology, MV (013035000), Tumour Cell Biology (013017530)
- id
- dda7f951-3e01-48bc-993d-998f9669ea9a (old id 1109867)
- date added to LUP
- 2016-04-01 15:44:10
- date last changed
- 2022-01-28 06:49:26
@article{dda7f951-3e01-48bc-993d-998f9669ea9a,
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.}},
author = {{Gustavsson, Lena and Boyano-Adanez, Maria del Carmen and Larsson, Christer and Aradottir, Steina and Lundqvist, Cristofer}},
issn = {{0929-7855}},
keywords = {{Calmidazolium; Muscarinic receptors; Phosphatidylethanol; Phosphatidic acid; Phospholipase D; Signal transduction}},
language = {{eng}},
number = {{1-3}},
pages = {{229--235}},
publisher = {{Elsevier}},
series = {{Journal of Lipid Mediators and Cell Signalling}},
title = {{Regulation of phospholipase D activity in neuroblastoma cells}},
url = {{http://dx.doi.org/10.1016/0929-7855(96)00530-5}},
doi = {{10.1016/0929-7855(96)00530-5}},
volume = {{14}},
year = {{1996}},
}