Hydrogen peroxide-induced arachidonic acid release in L929 cells; roles of Src, protein kinase C and cytosolic phospholipase A2α

Taniguchi, Takeo; Shimizu, Masaya; Nakamura, Hiroyuki; Hirabayashi, Tetsuya; Fujino, Hiromichi; Murayama, Toshihiko

doi:10.1016/j.ejphar.2006.06.071

Cited by 10 publications

(25 citation statements)

References 40 publications

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“…1 and Table 1). As mentioned in the Introduction, the MEK-ERK pathway regulates the activation of cPLA 2 α in many cell types (10,26,27). Treatment with both PMA and EGF caused phosphorylation of ERK1/2 within 10 min, and the response continued for at least 30 min ( (Table 1).…”

Section: Egf Released Aa Via Activation Of the Mek-erkcpla 2 α Pathwamentioning

confidence: 99%

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

et al. 2009

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Abstract. In several types of cancer cells, prostaglandins produced via the over-expression of epidermal growth factor receptor (EGFR) and cyclooxygenases regulate cell growth. We investigated the signaling mechanisms for the release of arachidonic acid (AA, a precursor for prostaglandins) in human cervical carcinoma HeLa cells. Treatment with EGF and 4β-phorbol 12-myristate 13-acetate (PMA) with A23187 released AA accompanied by the phosphorylation of extracellular signal-regulated kinases (ERK1/2). Pharmacological experiments showed that the responses (ERK phosphorylation and AA release) induced by EGF and PMA were mediated by a mitogen-activated protein kinase /ERK kinase (MEK) -ERK -α-type cytosolic phospholipase A 2 (cPLA 2 α) pathway and that EGFR couples with the pathway in a manner insensitive to sorafenib, an inhibitor of B-and C-Raf, enzymes upstream of MEK. Activation of protein kinase C by PMA couples with the pathway partly in a sorafenib-sensitive and probably C-Raf-mediated manner and partly in a family of Src tyrosine kinases (Src)-dependent and sorafenib-insensitive manner. Co-treatment with sorafenib and an inhibitor of Src family members additionally inhibited the PMA-induced release of AA. Cross-talk between EGFR and protein kinase C was not observed. In human lung carcinoma A549 cells, the release of AA by EGF was insensitive to sorafenib. Possible mechanisms for the sorafenib-insensitive activation of the MEK-ERK-cPLA 2 α pathway are discussed.

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Section: Egf Released Aa Via Activation Of the Mek-erkcpla 2 α Pathwamentioning

confidence: 99%

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

et al. 2009

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“…The release of AA induced by 30 μM DMB-mC11S (GS13) was not marked for 15 and 30 min after stimulation, and treatment with DMB-mC11S (GS13) at 10 μM for 1 h showed a moderate response (150% -200% of the control response), although the response at 5 μM was marginal (data not shown). The responses by the effective S1P analogs including DMBmC11S (GS13) were less than that of the positive control, which is co-stimulation with 4β-phorbol 12-myristate 13-acetate and A23187, a strong releaser of AA via cPLA 2 α activation in L929 cells (25). To examine a possible interaction between the compounds, DMBmC11S (GS13) was used in the following experiments since that was a strongest compound in the tested analogs.…”

Section: Resultsmentioning

confidence: 99%

“…As a positive control, release of AA induced by 100 nM 4β-phorbol 12-myristate 13-acetate plus 10 μM A23187 was measured (25). It is reported that there is release of 3 Hlabeled membrane vesicles and fragments as components of apoptotic bodies in apoptotic cells (27).…”

Section: Cell Culture and Measurement Of Release Of [ 3 H]aamentioning

confidence: 99%

“…PLA 2 assay in vitro PLA 2 activity in bee venom secretory PLA 2 (type III, Cayman, No 60500; Cayman Chemical Co., Ann Arbor, MI, USA) was measured using phospholipid vesicles containing 1-palmitoyl-2-[ 14 C]-arachidonyl phosphatidylcholine (1776 MBq/mmol; Perkin Elmer, Boston, MA, USA) as described previously (25).…”

Section: Cell Viability and Morphological Changesmentioning

confidence: 99%

“…The effects of the compounds were examined at pharmacological concentrations (10 and 30 μM). The concentrations of other reagents including enzyme inhibitors were the same as those in previous reports (18,24,25). The S1P analogs having a dimethylated phosphate group were dissolved in dimethyl sulfoxide, and the final concentration of dimethyl sulfoxide was under 0.5%.…”

Section: Introductionmentioning

confidence: 99%

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Effects of Synthetic Sphingosine-1-Phosphate Analogs on Cytosolic Phospholipase A2α–Independent Release of Arachidonic Acid and Cell Toxicity in L929 Fibrosarcoma Cells: the Structure–Activity Relationship

et al. 2009

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Abstract. Sphingolipid metabolites including ceramide, sphingosine, and their phosphorylated products [sphingosine-1-phosphate (S1P) and ceramide-1-phosphate] regulate cell functions including arachidonic acid (AA) metabolism and cell death. The development of analogs of S1P may be useful for regulating these mediator-induced cellular responses. We synthesized new analogs of S1P and examined their effects on the release of AA and cell death in L929 mouse fibrosarcoma cells. Among the analogs tested, several compounds including DMB-mC11S [dimethyl (2S,3R)-2-tert-butoxycarbonylamino-3-hydroxy-3-(3'-undecyl)phenylpropyl phosphate] and DMB-mC9S [dimethyl (2S,3R)-2-tert-butoxycarbonylamino-3-hydroxy-3-(3'-nonyl)phenylpropyl phosphate] released AA within 1 h and caused cell death 6 h after treatment. The release of AA was observed in C12 cells [a L929 variant lacking a type α cytosolic phospholipase A 2 (cPLA 2 α)] and L929-cPLAα-siRNA cells (L929 cells treated with small interference RNA for cPLA 2 α). Treatment with pharmacological inhibitors of secretory and Ca 2+ -independent PLA 2 s decreased the DMB-mC11S-induced release of AA. The effect of the S1P analogs tested on the release of AA was comparable to that on cell death in L929 cells, and a high correlation coefficient was observed. Two analogs lacking a butoxycarbonyl moiety phenylpropyl phosphate] and DMAm-mC11S [dimethyl (2S,3R)-2-amino-3-hydroxy-3-(3'-undecyl)phenylpropyl phosphate)] had inhibitory effects on the release of AA and cell toxicity induced by DMB-mC11S. Synthetic phosphorylated lipid analogs may be useful for studying PLA 2 activity and its toxicity in cells.[ Supplementary Fig. 1: available only at http://dx

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Lactosylceramide‐Induced Phosphorylation Signaling to Group IVA Phospholipase A₂ via Reactive Oxygen Species in Tumor Necrosis Factor‐α‐Treated Cells

Nakamura

Moriyama

Watanabe

et al. 2017

J of Cellular Biochemistry

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The activity of α-type cytosolic phospholipase A (cPLA α, group IVA PLA ), which releases arachidonic acid (AA), is mainly regulated by the Ca -induced intracellular translocation/attachment of the enzyme to substrate membranes and its phosphorylation. We previously reported that tumor necrosis factor-α (TNFα) stimulated the formation of lactosylceramide (LacCer) in L929 fibroblast cells, and this lipid directly bound with and activated cPLA α [Nakamura et al. [2013] J. Biol. Chem. 288:23264-23272]. We herein investigated the role of phosphorylation signaling in the TNFα/LacCer-induced activation of cPLA α in cells. TNFα-treated L929 cells released AA via the phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2) and cPLA α, while a treatment with LacCer alone released AA in a similar manner. The TNFα-induced responses including release of AA were decreased by the inhibition of LacCer synthesis. The treatment with TNFα and LacCer increased the levels of reactive oxygen species (ROS), and the reduction/scavenging of ROS decreased the phosphorylation cascade and release of AA in TNFα/LacCer-treated L929 cells. In the cell line CHO, the treatment with LacCer stimulated the phosphorylation cascade and release of AA via the formation of ROS. Treatments with the anti-LacCer antibody and 4β-phorbol 12-myristate 13-acetate stimulated the phosphorylation cascade, but did not release AA by itself. When combined with the Ca ionophore A23187, treatments with the anti-LacCer antibody and 4β-phorbol 12-myristate 13-acetate released AA. These results, including our previous findings, showed that LacCer alone simultaneously stimulates two processes to activate cPLA α: a phosphorylation signal and attachment of the enzyme to substrate membranes. J. Cell. Biochem. 118: 4370-4382, 2017. © 2017 Wiley Periodicals, Inc.

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Hydrogen peroxide-induced arachidonic acid release in L929 cells; roles of Src, protein kinase C and cytosolic phospholipase A2α

Cited by 10 publications

References 40 publications

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

Effects of Synthetic Sphingosine-1-Phosphate Analogs on Cytosolic Phospholipase A2α–Independent Release of Arachidonic Acid and Cell Toxicity in L929 Fibrosarcoma Cells: the Structure–Activity Relationship

Lactosylceramide‐Induced Phosphorylation Signaling to Group IVA Phospholipase A₂ via Reactive Oxygen Species in Tumor Necrosis Factor‐α‐Treated Cells

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Hydrogen peroxide-induced arachidonic acid release in L929 cells; roles of Src, protein kinase C and cytosolic phospholipase A2α

Cited by 10 publications

References 40 publications

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

Activation of Cytosolic Phospholipase A2α by Epidermal Growth Factor (EGF) and Phorbol Ester in HeLa Cells: Different Effects of Inhibitors for EGF Receptor, Protein Kinase C, Src, and C-Raf

Effects of Synthetic Sphingosine-1-Phosphate Analogs on Cytosolic Phospholipase A2α–Independent Release of Arachidonic Acid and Cell Toxicity in L929 Fibrosarcoma Cells: the Structure–Activity Relationship

Lactosylceramide‐Induced Phosphorylation Signaling to Group IVA Phospholipase A2 via Reactive Oxygen Species in Tumor Necrosis Factor‐α‐Treated Cells

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Lactosylceramide‐Induced Phosphorylation Signaling to Group IVA Phospholipase A₂ via Reactive Oxygen Species in Tumor Necrosis Factor‐α‐Treated Cells