The phosphorylation state of MAP‐kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide

Cantoni, Orazio; Boscoboinik, Daniel; Fiorani, Mara; Stäuble, Barbara; Azzi, Angelo

doi:10.1016/0014-5793(96)00605-9

Cited by 23 publications

(13 citation statements)

References 19 publications

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“…In previous studies, we showed that FCS leads to the activation of MAP kinase and induction of cyclin D1 [12], and that H 2 O 2 is able to activate MAP kinase by inducing its phosphorylation [5]. Other groups have also reported the activation of MAP kinase by H 2 O 2 [6,7] The cells can also be treated with PBS gluc for 4 h without losing their integrity (data not shown).…”

Section: Effect Of H 2 O 2 On Cyclin D Expressionmentioning

confidence: 90%

The effect of hydrogen peroxide on the cyclin D expression in fiborblasts

Muñoz¹,

Post²,

Verkleij³

et al. 2001

CMLS, Cell. Mol. Life Sci.

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Activation of mitogen-activated protein (MAP) kinase is essential for cyclin D1 expression and provides a link between mitogenic signalling and cell cycle progression. Hydrogen peroxide (H2O2) activates MAP kinase; however, it is not known whether this leads to cyclin D expression. Sustained expression of cyclin D1 and D2 was observed when Her14 fibroblasts were incubated with 3 mM or higher H2O2 concentrations. Similar results were obtained when cells were incubated in the presence of serum (FCS). However, the sustained expression of cyclin D1 and D2 upon H2O2 treatment was not due to the MAP kinase pathway, because MAP kinase kinase inhibitors did not inhibit cyclin D expression. Furthermore, cyclin D1 and D2 levels remained constant even after addition of a protein synthesis inhibitor, indicating that the effect of H2O2 was not due to induction of protein synthesis. These results indicate that H2O2 reversibly inhibits the ubiquitin-proteasome dependent degradation of cyclin D1 and D2, probably by transiently inhibiting ubiquitination and/or the proteasome.

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Section: Effect Of H 2 O 2 On Cyclin D Expressionmentioning

confidence: 90%

The effect of hydrogen peroxide on the cyclin D expression in fiborblasts

Muñoz¹,

Post²,

Verkleij³

et al. 2001

CMLS, Cell. Mol. Life Sci.

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“…H4IIE cells were incubated for an additional 24 h before detection of the optic densities (450 nm) on an enzyme‐linked immunoassay reader (Anthos Labotec Instruments). Lactate dehydrogenase (LDH) activity was taken as a measure of arsenite tolerance after a priming heat shock and was determined in the culture medium and cell lysates as described (27). LDH release was expressed as the percentage of total enzyme activity released into the supernatant of the H4IIE cells.…”

Section: Methodsmentioning

confidence: 99%

Osmotic regulation of the heat shock response in H4IIE rat hepatoma cells

1999

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The influence of cell hydration on the heat shock response was investigated in H4IIE hepatoma cells at the levels of HSP70 expression, MAP kinase activation, induction of c-jun and the MAP kinase phosphatase MKP-1, heat resistance, and development of tolerance/sensitization to arsenite after a priming heat treatment. Induction of HSP70, MKP-1, and c-jun by heat was delayed, but more pronounced or sustained, under hyperosmotic conditions compared with normo- and hypo-osmotically exposed cells. Anisosmolarity per se was ineffective to induce HSP70; some expression of the mRNAs for MKP-1 and c-jun in response to hyperosmolarity was found, but was small compared with the response to heat. Heat-induced activation of JNK-1 was increased under hyperosmotic conditions and more sustained than the JNK-activity induced by hyperosmolarity at 37 degrees C. A prominent Erk-2 activation was found immediately after heat shock under hypo- and normo-osmotic conditions, but Erk-2 activation was weak in hyperosmolarity-exposed cells. Despite anisosmotic alterations of the heat shock response at the molecular level, the heat resistance of H4IIE cells toward heat shock was not affected by ambient osmolarity. However, an osmolarity-dependent sensitization to arsenite was induced by a priming heat shock. The osmodependence of the H4IIE cell response to heat differs from that recently found in primary rat hepatocytes. The data are discussed in terms of cellular adaption mechanisms and their physiological relevance.

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“…The MAPK family is particularly sensitive to H 2 O 2 (Whisler et al . 1995; Cantoni et al . 1996; Guyton et al .…”

Section: Discussionmentioning

confidence: 99%

“…The tyrosine phosphorylation of MAPK in response to H 2 O 2 has functional significance since it induces MAPK‐dependent gene expression (Guyton et al . 1996) and modulates the cytotoxic response to H 2 O 2 (Cantoni et al . 1996; Guyton et al .…”

Section: Discussionmentioning

confidence: 99%

Tyrosine phosphorylation of insulin receptor substrate‐1 (IRS‐1) by oxidant stress in cerebellar granule neurons: modulation by N‐methyl‐d‐aspartate through calcineurin activity

Hallak¹,

Ramadan²,

Rubin³

2001

Journal of Neurochemistry

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Insulin receptor‐substrate‐1 (IRS‐1) is a docking protein for several tyrosine kinase receptors. Upon tyrosine phosphorylation, IRS‐1 binds to signaling molecules that express Src homology 2 (SH‐2) binding domains, including phosphatidylinositol 3‐kinase (PI 3‐kinase), phosphotyrosine phosphatase SHP‐2 (Syp), Nck, Crk and Grb‐2. Hydrogen peroxide (H2O2) induces tyrosine phosphorylation of key signaling mediators presumably by inhibition of tyrosine phosphatases. In many cell types, the activation of extracellular signal‐related kinases (e.g. MAPK) and other protein kinases by H2O2 leads to transcriptional activation. In the current study, we examined the effect of H2O2 on IRS‐1 tyrosine phosphorylation in primary cultured rat cerebellar granule neurons. H2O2 stimulated the rapid tyrosine phosphorylation of IRS‐1 and p42/p44 MAP kinase, and induced its association with PI 3‐kinase. H2O2‐induced IRS‐1 phosphorylation was rapidly reversible (5 min) whereas MAPK phosphorylation persisted for up to 1 h. NMDA reversed H2O2‐mediated tyrosine phosphorylation of IRS‐1 and its association with PI 3‐kinase. The dephosphorylation of IRS‐1 by NMDA was calcium‐dependent and was inhibited by the calcineurin inhibitor cyclosporine. Calmodulin‐dependent tyrosine phosphatase activity of calcineurin was observed in vitro using both immunoprecipitated and recombinant tyrosine‐phosphorylated IRS‐1 as substrates. These data highlight the role of multiple phosphatases in the regulation of IRS‐1 tyrosine phosphorylation and identify a novel functional property of calcineurin.

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The phosphorylation state of MAP‐kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide

Cited by 23 publications

References 19 publications

The effect of hydrogen peroxide on the cyclin D expression in fiborblasts

The effect of hydrogen peroxide on the cyclin D expression in fiborblasts

Osmotic regulation of the heat shock response in H4IIE rat hepatoma cells

Tyrosine phosphorylation of insulin receptor substrate‐1 (IRS‐1) by oxidant stress in cerebellar granule neurons: modulation by N‐methyl‐d‐aspartate through calcineurin activity

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