Regulation of phospholipase C-gamma 2 via phosphatidylinositol 3-kinase in macrophages.
(2002) In Cellular Signalling 14(2). p.169-173- Abstract
- Phospholipase C-gamma (PLC-gamma) isoforms are thought to be activated by both tyrosine phosphorylation and phosphatidylinositol 3,4,5 trisphosphate (PtdIns 3,4,5 P(3)), the product of phosphatidylinositol 3-kinase (PtdIns 3-kinase). In this study, we show that stimulation of mouse macrophages with either zymosan beads or bacteria (Prevotella intermedia) induced tyrosine phosphorylation of PLC-gamma 2. Zymosan stimulation also induced translocation to membrane and cytoskeleton fractions, which was inhibited by the PtdIns 3-kinase inhibitors wortmannin and LY 294002. However, the tyrosine phosphorylation of PLC-gamma 2 induced by zymosan was not affected by the inhibitors wortmannin and LY 294002. In contrast to zymosan and bacteria,... (More)
- Phospholipase C-gamma (PLC-gamma) isoforms are thought to be activated by both tyrosine phosphorylation and phosphatidylinositol 3,4,5 trisphosphate (PtdIns 3,4,5 P(3)), the product of phosphatidylinositol 3-kinase (PtdIns 3-kinase). In this study, we show that stimulation of mouse macrophages with either zymosan beads or bacteria (Prevotella intermedia) induced tyrosine phosphorylation of PLC-gamma 2. Zymosan stimulation also induced translocation to membrane and cytoskeleton fractions, which was inhibited by the PtdIns 3-kinase inhibitors wortmannin and LY 294002. However, the tyrosine phosphorylation of PLC-gamma 2 induced by zymosan was not affected by the inhibitors wortmannin and LY 294002. In contrast to zymosan and bacteria, PLC-gamma 2 was not phosphorylated by stimulation with lipopolysaccharide (LPS), phorbol ester or calcium ionophore. Moreover, the PLC-gamma 1 isoform was not detected in mouse macrophages. These data indicate that PtdIns 3-kinase is critical for the translocation but not for the tyrosine phosphorylation of PLC-gamma 2 in mouse macrophages and that the latter may be insufficient for enzyme activation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/106811
- author
- Hiller, Gösta and Sundler, Roger LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Chromones : pharmacology, Cytoskeleton : enzymology, Dose-Response Relationship Drug, Female, Macrophages : drug effects : enzymology, Isoenzymes : metabolism, Mice, Morpholines : pharmacology, Phosphotyrosine : metabolism, Phosphorylation, Phospholipase C : metabolism, Prevotella intermedia, Protein Transport, Signal Transduction, Support Non-U.S. Gov't, Zymosan : pharmacology, Cells Cultured, Cell Membrane : enzymology, Animal, Androstadienes : pharmacology, 1-Phosphatidylinositol 3-Kinase : antagonists & inhibitors : physiology
- in
- Cellular Signalling
- volume
- 14
- issue
- 2
- pages
- 169 - 173
- publisher
- Elsevier
- external identifiers
-
- wos:000173433000011
- pmid:11781142
- scopus:0036142839
- ISSN
- 1873-3913
- DOI
- 10.1016/S0898-6568(01)00252-2
- language
- English
- LU publication?
- yes
- id
- 56503472-cbeb-44b6-b3c3-be678075f9a6 (old id 106811)
- alternative location
- http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11781142&dopt=Abstract
- date added to LUP
- 2016-04-01 12:27:16
- date last changed
- 2022-03-13 18:05:55
@article{56503472-cbeb-44b6-b3c3-be678075f9a6,
abstract = {{Phospholipase C-gamma (PLC-gamma) isoforms are thought to be activated by both tyrosine phosphorylation and phosphatidylinositol 3,4,5 trisphosphate (PtdIns 3,4,5 P(3)), the product of phosphatidylinositol 3-kinase (PtdIns 3-kinase). In this study, we show that stimulation of mouse macrophages with either zymosan beads or bacteria (Prevotella intermedia) induced tyrosine phosphorylation of PLC-gamma 2. Zymosan stimulation also induced translocation to membrane and cytoskeleton fractions, which was inhibited by the PtdIns 3-kinase inhibitors wortmannin and LY 294002. However, the tyrosine phosphorylation of PLC-gamma 2 induced by zymosan was not affected by the inhibitors wortmannin and LY 294002. In contrast to zymosan and bacteria, PLC-gamma 2 was not phosphorylated by stimulation with lipopolysaccharide (LPS), phorbol ester or calcium ionophore. Moreover, the PLC-gamma 1 isoform was not detected in mouse macrophages. These data indicate that PtdIns 3-kinase is critical for the translocation but not for the tyrosine phosphorylation of PLC-gamma 2 in mouse macrophages and that the latter may be insufficient for enzyme activation.}},
author = {{Hiller, Gösta and Sundler, Roger}},
issn = {{1873-3913}},
keywords = {{Chromones : pharmacology; Cytoskeleton : enzymology; Dose-Response Relationship Drug; Female; Macrophages : drug effects : enzymology; Isoenzymes : metabolism; Mice; Morpholines : pharmacology; Phosphotyrosine : metabolism; Phosphorylation; Phospholipase C : metabolism; Prevotella intermedia; Protein Transport; Signal Transduction; Support Non-U.S. Gov't; Zymosan : pharmacology; Cells Cultured; Cell Membrane : enzymology; Animal; Androstadienes : pharmacology; 1-Phosphatidylinositol 3-Kinase : antagonists & inhibitors : physiology}},
language = {{eng}},
number = {{2}},
pages = {{169--173}},
publisher = {{Elsevier}},
series = {{Cellular Signalling}},
title = {{Regulation of phospholipase C-gamma 2 via phosphatidylinositol 3-kinase in macrophages.}},
url = {{http://dx.doi.org/10.1016/S0898-6568(01)00252-2}},
doi = {{10.1016/S0898-6568(01)00252-2}},
volume = {{14}},
year = {{2002}},
}