Expression of cytosolic phospholipase A2 alpha in murine C12 cells, a variant of L929 cells, induces arachidonic acid release in response to phorbol myristate acetate and Ca2+ ionophores, but not to tumor necrosis factor-alpha.

@article{Shimizu2004ExpressionOC,
  title={Expression of cytosolic phospholipase A2 alpha in murine C12 cells, a variant of L929 cells, induces arachidonic acid release in response to phorbol myristate acetate and Ca2+ ionophores, but not to tumor necrosis factor-alpha.},
  author={Masaya Shimizu and Chihiro Azuma and Tomoko Taniguchi and Toshihiko Murayama},
  journal={Journal of pharmacological sciences},
  year={2004},
  volume={96 3},
  pages={
          324-32
        }
}
Tumor necrosis factor-alpha (TNFalpha)-induced cell death is regulated through the release of arachidonic acid (AA) by group IVA cytosolic phospholipase A2 (cPLA2alpha) in the murine fibroblast cell line L929. However, the signaling pathway by which TNFalpha activates cPLA2alpha remained to be solved. We examined AA release in L929 cells, in a variant of L929 (C12 cells) lacking cPLA2alpha, and in C12 cells transfected with cPLA2alpha expression vectors. In transient and stable clones of C12… 

Figures from this paper

Activation of cytosolic phospholipase A2alpha 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.

Parmacological 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-alpha-type cytosolic phospholipase A(2) (cPLA( 2)alpha) pathway and that EGFR couples with the pathway in a manner insensitive to sorafenib.

Amyloid beta enhances cytosolic phospholipase A2 level and arachidonic acid release via nitric oxide in APP-transfected PC12 cells.

Results indicate that Abeta peptides enhance the protein level and phosphorylation of cPLA2 and AA release by the NO signaling pathway.

Inhibition of cytosolic Phospholipase A2 prevents prion peptide-induced neuronal damage and co-localisation with Beta III Tubulin

It is suggested that cPLA2 plays a vital role in the action of HuPrP106-126 and that the colocalisation of p-cPLA2 with beta III tubulin could be central to the progress of neurodegeneration caused by prion peptides.

Effects of synthetic sphingosine-1-phosphate analogs on cytosolic phospholipase A2alpha-independent release of arachidonic acid and cell toxicity in L929 fibrosarcoma cells: the structure-activity relationship.

Synthetic phosphorylated lipid analogs may be useful for studying PLA(2) activity and its toxicity in cells, and a high correlation coefficient was observed.

Cytosolic PLA2α activation in Purkinje neurons and its role in AMPA-receptor trafficking

Results suggest that cPLA2α regulates the persistent decrease in the expression of AMPA receptors, underscoring the role of c PLA2α in cerebellar LTD.

Cytotoxicity induced by inhibition of thioredoxin reductases via multiple signaling pathways: Role of cytosolic phospholipase A2α‐dependent and ‐independent release of arachidonic acid

The data suggest that a dysfunctional Trx system triggers multiple signaling pathways, and that the AA released by cPLA2α‐dependent and ‐independent pathways is important to cytotoxicity.

References

SHOWING 1-10 OF 40 REFERENCES

Phospholipase A2 Is Necessary for Tumor Necrosis Factor α-induced Ceramide Generation in L929 Cells*

The introduction of the cPLA2 gene into C12 cells resulted in partial restoration of TNFα-induced arachidonate release, ceramide accumulation, and cytotoxicity, suggesting that c PLA2 is a necessary component in the pathways leading to ceramic accumulation and cell death.

Failure to activate cytosolic phospholipase A2 causes TNF resistance in human leukemic cells.

The data suggest that cPLA2 activity is involved in TNF-induced cytotoxicity in leukemic cells, and resistance to TNF's cytotoxic action may involve either protein inhibitors that act upstream of c PLA2 in the TNF -signaling pathway or constitutive defects of cPLA1 itself, possibly involving calcium utilization.

Cross-talk between Cytosolic Phospholipase A2α (cPLA2α) and Secretory Phospholipase A2 (sPLA2) in Hydrogen Peroxide-induced Arachidonic Acid Release in Murine Mesangial Cells

The effect of group IIa and V PLA2s on H2O2-induced AA release is dependent upon the presence of cPLA2α and the activation of PKC and ERK1/2.

Different apoptotic pathways mediated by Fas and the tumor-necrosis-factor receptor. Cytosolic phospholipase A2 is not involved in Fas-mediated apoptosis.

It is indicated that cPLA2 is required for TNF-induced apoptosis, whereas it is dispensable for Fas-mediated apoptosis and suggested that the TNF receptor and Fas use different signaling pathways for apoptosis.

Role of PKC and MAPK in cytosolic PLA2 phosphorylation and arachadonic acid release in primary murine astrocytes.

Together, the results provided evidence for an important role of PKC in mediating cPLA2 phosphorylation and AA release in astrocytes through both ERK1/2-dependent and ERK2-independent pathways.

Cooperative Signaling by Tumor Necrosis Factor Receptors CD120a (p55) and CD120b (p75) in the Expression of Nitric Oxide and Inducible Nitric Oxide Synthase by Mouse Macrophages*

While cross-linking of CD120a (p55) is necessary and sufficient for iNOS mRNA and NO2 − expression, CD120b (p75) participates by increasing the sensitivity of the cells to TNFα and initiating a signaling event that results in a more sustained induction of iN OS mRNA and protein and thereby augments the production of nitric oxide.

Involvement of NF-kappaB in the protection of cell death by tumor necrosis factor in L929 derived TNF resistant C12 cells.

Pretreatment with the known potent NF-kappaB inhibitor pyrolidine dithiocarbamate (PDTC) profoundly suppressed the activation of NF- kappaB induced by TNF and potentiated TNF cytotoxicity in all 3 cell lines, consistent with the recently found anti-apoptotic action of NF.

Protein Kinase C Modulates Tumor Necrosis Factor-related Apoptosis-inducing Ligand-induced Apoptosis by Targeting the Apical Events of Death Receptor Signaling*

Results show that PKC activation specifically inhibits the recruitment of key obligatory death domain-containing adaptor proteins to their respective membrane-associated signaling complexes, thereby modulating TRAIL-induced apoptosis and TNF-induced NF-κB activation, respectively.

Role of PKC and MAPK in cytosolic PLA2 phosphorylation and arachadonic acid release in primary murine astrocytes

Evidence is provided for an important role of PKC in mediating cPLA2 phosphorylation and AA release in astrocytes through both ERK1/2‐dependent and ERK2‐independent pathways and for the sensitivity of PMA‐induced responses to PKC down‐regulation.