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Regulation of phospholipase C-gamma 2 via phosphatidylinositol 3-kinase in macrophages.

Hiller, Gösta and Sundler, Roger LU (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)
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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
2025-04-04 14:37:38
@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}},
}