The kinase insert domain of colony stimulating factor‐1 receptor is dispensable for CSF‐1 induced phosphatidylcholine hydrolysis

Choudhury, Goutam Ghosh; Sylvia, V. L.; Wang, Ling Mei; Pierce, Joseph E.; Sakaguchi, Alan Y.

doi:10.1016/0014-5793(91)80511-z

Cited by 15 publications

(5 citation statements)

References 26 publications

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“…The kinetics and amount of diglyceride accumulation in BAC1.2F5 cells (Fig. 1) were the same as those observed in macrophages (72), monocytes (32), and a fibroblast cell line expressing CSF-1R (12).…”

Section: Resultssupporting

confidence: 72%

“…(B) Growth-arrested BAC1.2F5 cells were treated for the indicated times with CSF-1, the cellular lipids were extracted, and the cell-associated diglyceride mass was quantitated by its conversion to [32P]phosphatidic acid with diglyceride kinase as described in Materials and Methods. (12). We employed two different experimental approaches to determine whether CSF-1 stimulation correlates with diglyceride accumulation in the BAC1.2F5 cell line (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Hydrolysis of phosphatidylcholine (PtdCho) by a specific phospholipase C (PC-PLC) or phospholipase D (PC-PLD) is a potential alternate source for diglyceride generation (4,22). CSF-1 elevates intracellular concentrations of diglyceride derived from PtdCho in human monocytes (32), bone marrow-derived macrophages (72), and a fibroblast cell line expressing CSF-1R (12). PC-PLC activity is precipitated by anti-phosphotyrosine antibodies following activation of CSF-1R, indicating that tyrosine phosphorylation is associated with PC-PLC activation in a manner similar to that observed for phosphatidylinositol 3'-kinase and phospholipase Cyl (11).…”

mentioning

confidence: 86%

“…PC-PLC activity is precipitated by anti-phosphotyrosine antibodies following activation of CSF-1R, indicating that tyrosine phosphorylation is associated with PC-PLC activation in a manner similar to that observed for phosphatidylinositol 3'-kinase and phospholipase Cyl (11). However, deletion of the kinase insert region from CSF-1R does not diminish the extent of CSF-1-activated PtdCho hydrolysis, indicating that a different region of the receptor is involved in transducing the signal to PC-PLC (12 (65) and used as the source of CSF-1 for routine growth and maintenance of the BAC1.2F5 cell line. Antibody to the CSF-1 receptor (29) was kindly provided by Jim Downing, and polyclonal antiphosphotyrosine antibody (33) was provided by Albert Reynolds.…”

mentioning

confidence: 99%

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Phosphatidylcholine hydrolysis and c-myc expression are in collaborating mitogenic pathways activated by colony-stimulating factor 1.

Xu¹,

Tessner²,

Rock³

et al. 1993

Mol. Cell. Biol.

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Stimulation of diglyceride production via phospholipase C (PLC) hydrolysis of phosphatidylcholine was an early event in the mitogenic action of colony-stimulating factor 1 (CSF-1) in the murine macrophage cell line BAC1.2F5 and was followed by a second phase of diglyceride production that persisted throughout the G1 phase of the cell cycle. Addition of phosphatidylcholine-specific PLC (PC-PLC) from Bacillus cereus to the medium of quiescent cells raised the intracellular diglyceride concentration and stimulated [3H]thymidine incorporation, although PC-PLC did not support continuous proliferation. PC-PLC treatment did not induce tyrosine phosphorylation or turnover of the CSF-1 receptor. The major protein kinase C (PKC) isotype in BAC1.2F5 cells was PKC-delta. Diglyceride production from PC-PLC did not target PKC-delta, since unlike phorbol esters, PC-PLC treatment neither decreased the electrophoretic mobility of PKC-delta nor increased the amount of GTP bound to Ras, and PC-PLC was mitogenically active in BAC1.2F5 cells in which PKC-delta was downregulated by prolonged treatment with phorbol ester. PC-PLC mimicked CSF-1 action by elevating c-fos and junB mRNAs to 40% of the level induced by CSF-1; however, PC-PLC induced c-myc mRNA to only 5% of the level in CSF-1-stimulated cells. PC-PLC addition to CSF-1-dependent BAC1.2F5 clones that constitutively express c-myc increased [3H]thymidine incorporation to 86% of the level evoked by CSF-1 and supported slow growth in the absence of CSF-1. Therefore, PC-PLC is a component of a signal transduction pathway leading to transcription of c-fos and junB that collaborates with c-myc and is independent of PKC-delta and Ras activation.

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Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 86%

mentioning

confidence: 99%

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Phosphatidylcholine hydrolysis and c-myc expression are in collaborating mitogenic pathways activated by colony-stimulating factor 1.

Xu¹,

Tessner²,

Rock³

et al. 1993

Mol. Cell. Biol.

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“…The results of the present study indicated that LTA might activate PC‐PLC and PC‐PLD to induce PKC activation, which in turn induces COX‐2 expression and PGE 2 release. However, the mechanism involved in the activation of PC‐PLC and PC‐PLD is still not well defined, but may involve tyrosine phosphorylation (Choudhury et al ., 1991).…”

Section: Discussionmentioning

confidence: 99%

Induction of cyclooxygenase‐2 protein by lipoteichoic acid from Staphylococcus aureus in human pulmonary epithelial cells: involvement of a nuclear factor‐κB‐dependent pathway

Lin

Kuan

Lee

et al. 2001

British J Pharmacology

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1 This study investigated the role of protein kinase C (PKC) and transcription factor nuclear factor-kB (NF-kB) in cyclooxygenase-2 (COX-2) expression caused by lipoteichoic acid (LTA), a cell wall component of the gram-positive bacterium Staphylococcus aureus, in human pulmonary epithelial cell line (A549). 2 LTA caused dose-and time-dependent increases in COX-2 expression and COX activity, and a dose-dependent increase in PGE 2 release in A549 cells. The LTA-induced increases in COX-2 expression and COX activity were markedly inhibited by dexamethasone, actinomycin D or cyclohexamide, but not by polymyxin B, which binds and inactivates endotoxin. 3 The phosphatidylcholine-phospholipase C (PC-PLC) inhibitor (D-609) and the phosphatidate phosphohydrolase inhibitor (propranolol) reduced the LTA-induced increases in COX-2 expression and COX activity, while phosphatidylinositol-phospholipase C inhibitor (U-73122) had no e ect. The PKC inhibitors (Go 6976, Ro 31-8220 and GF 109203X) and NF-kB inhibitor, pyrrolidine dithiocarbamate (PDTC), also attenuated the LTA-induced increases in COX-2 expression and COX activity. 4 Treatment of A549 cells with LTA caused an increase in PKC activity in the plasma membrane; this stimulatory e ect was inhibited by D-609, propranolol, or Go 6976, but not by U-73122. 5 Exposure of A549 cells to LTA caused a translocation of p65 NF-kB from the cytosol to the nucleus and a degradation of IkB-a in the cytosol. Treatment of A549 cells with LTA caused NF-kB activation by detecting the formation of NF-kB-speci®c DNA-protein complex in the nucleus; this e ect was inhibited by dexamethasone, D-609, propranolol, Go 6976, Ro 31-8220, or PDTC. 6 These results suggest that LTA might activate PC-PLC and phosphatidylcholine-phospholipase D to induce PKC activation, which in turn initiates NF-kB activation, and ®nally induces COX-2 expression and PGE 2 release in human pulmonary epithelial cell line.

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Macrophage colony stimulating factor activates phosphatidylcholine hydrolysis by cytoplasmic phospholipase A2.

et al. 1992

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The macrophage colony stimulating factor (M‐CSF) is required for the proliferation and differentiation of monocytes. Previous studies have demonstrated that M‐CSF stimulation is associated with phosphatidylcholine (PC) hydrolysis and increased formation of both diacylglycerol (DAG) and phosphorylcholine. The present work extends those results by demonstrating that treatment of human monocytes with M‐CSF is associated with increases in a cytoplasmic Ca(2+)‐dependent activity which hydrolyzes 1‐palmitoyl,2‐arachidonoyl PC to arachidonic acid. The finding that this hydrolysis of PC is associated with increases in production of lysophosphatidylcholine indicates that M‐CSF stimulates a cytoplasmic phospholipase A2 (cPLA2) activity. These results are supported by the demonstration that M‐CSF induces cPLA2 gene expression. M‐CSF‐induced increases in cPLA2 mRNA levels were biphasic and corresponded with rapid (30–60 min) and delayed (24–72 h) increases in cPLA2 activity. The results demonstrate that this effect of M‐CSF on cPLA2 expression is controlled at least in part by post‐transcriptional stabilization of cPLA2 transcripts. The finding that M‐CSF treatment is also associated with phosphorylation of the cPLA2 protein further suggests that expression of this enzyme is regulated at multiple levels. Finally, the stimulation of cPLA2 activity and arachidonate release is supported by increases in prostaglandin (PG) synthesis. In this regard, levels of both PGE2 and PGF2 alpha were increased in response to M‐CSF. Taken together, these results indicate that M‐CSF stimulates PC hydrolysis in human monocytes by inducing cPLA2 activity and thereby formation of eicosanoids.

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The kinase insert domain of colony stimulating factor‐1 receptor is dispensable for CSF‐1 induced phosphatidylcholine hydrolysis

Cited by 15 publications

References 26 publications

Phosphatidylcholine hydrolysis and c-myc expression are in collaborating mitogenic pathways activated by colony-stimulating factor 1.

Phosphatidylcholine hydrolysis and c-myc expression are in collaborating mitogenic pathways activated by colony-stimulating factor 1.

Induction of cyclooxygenase‐2 protein by lipoteichoic acid from Staphylococcus aureus in human pulmonary epithelial cells: involvement of a nuclear factor‐κB‐dependent pathway

Macrophage colony stimulating factor activates phosphatidylcholine hydrolysis by cytoplasmic phospholipase A2.

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