P38 and ERK mitogen-activated protein kinases mediate acrolein-induced apoptosis in Chinese hamster ovary cells

Tanel, André; Averill‐Bates, Diana A.

doi:10.1016/j.cellsig.2006.10.014

Cited by 60 publications

(44 citation statements)

References 85 publications

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“…SS-induced activation of Stat5 also was linked to reduced hepatic GH binding in rat hepatocytes (Murray et al 2004). It was shown recently that increased ERK and Akt activation was attended by increased p53 activation (Tanel & Averill-Bates 2007), suggesting that SSTR1A/ SSTR2-triggered ERK and/or PI3K/Akt activation of p53 may underlie, at least in part, SS-induced inhibition of IGFR expression in native gill filaments of trout.…”

Section: Discussionmentioning

confidence: 98%

“…Cells were allowed to adhere overnight and serum starved for 24 h. The serum-free medium was then removed, and the cells were treated with varying concentrations of SS ranging from 0 to 1000 ng/ml (0-610 nM) for the period of time specified in the figures. In combination experiments involving MEK and PI3K inhibitors, the specific inhibitor was added 1 h prior to hormone addition at a concentration recommended to be maximally effective by the manufacturer and which was used previously (Lahlou et al 2003, Tanel & Averill-Bates 2007. After treatments, incubations were stopped and the cells were lysed with 100 ml 1!…”

Section: Western Blottingmentioning

confidence: 99%

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Rainbow trout somatostatin receptor subtypes SSTR1A, SSTR1B, and SSTR2 differentially activate the extracellular signal-regulated kinase and phosphatidylinositol 3-kinase signaling pathways in transfected cells

Hagemeister

Kittilson²,

Bergan³

et al. 2010

Journal of Molecular Endocrinology

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Previously, we reported that extracellular signal-regulated kinase (ERK) and protein kinase B (Akt), a downstream target of phosphatidylinositol 3-kinase (PI3K), mediated somatostatin (SS) inhibition of GH receptor, IGF1, and IGF1 receptor expression. In this study, we used Chinese hamster ovary-K1 cells that stably transfected individually with trout SS receptors (SSTR1A, SSTR1B, and SSTR2) to elucidate receptor-effector pathway linkages. SS induced ERK and Akt activation in a time-and concentration-related manner in all SSTR-expressing cells; however, the PI3K/Akt pathway was activated to a greater extent through SSTR1A than through either SSTR1B or SSTR2, whereas the ERK pathway was activated to a greater extent though SSTR2 than through either SSTR1A or SSTR1B. Although the ERK pathway inhibitor U0126 had no effect on Akt activation, the PI3K inhibitor LY294002 reduced ERK activation to near control levels in all SSTR-expressing cell lines, suggesting some cross talk between the pathways, possibly at the level of c-Raf, the phosphorylation of which also was induced by SS via each SSTR. Pertussis toxin (PTX) completely abolished SS-induced activation of ERK and Akt in SSTR1A-, SSTR1B-, and SSTR2-expressing cells, suggesting that these receptors link to the ERK and PI3K/Akt pathways via PTX-sensitive G-proteins. SS-induced activation of Elk1, Stat3, and C/EBPb also was mediated by each of the trout SSTRs. These findings establish important receptor-effector pathway linkages for fish SSTRs and provide insight into the molecular mechanisms by which SSs may elicit diverse physiological effects in target cells.

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Section: Discussionmentioning

confidence: 98%

Section: Western Blottingmentioning

confidence: 99%

Rainbow trout somatostatin receptor subtypes SSTR1A, SSTR1B, and SSTR2 differentially activate the extracellular signal-regulated kinase and phosphatidylinositol 3-kinase signaling pathways in transfected cells

Hagemeister

Kittilson²,

Bergan³

et al. 2010

Journal of Molecular Endocrinology

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“…This data suggests that the activation of the p38MAPK signaling pathway is necessary for protection against CPF induced toxicity. This is surprising because p38 MAPK is a stress-related MAPK which is activated via phosphorylation in response to a myriad of chemical and oxidative insults (Namgung and Xia 2000;Cai et al 2006;Tanel and Averill-Bates 2007). Historically, sustained activation of p38MAPK is associated with apoptosis and conversely inhibition rescues cells from apoptotic death (Chang and Karin 2001;Mansouri et al 2003;Cai et al 2006;Zhou et al 2006;Tanel and Averill-Bates 2007).…”

Section: Discussionmentioning

confidence: 99%

Characterization of chlorpyrifos-induced apoptosis in placental cells

Saulsbury¹,

Heyliger²,

Wang³

et al. 2008

Toxicology

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The mechanism by which chlorpyrifos exerts its toxicity in fetal and perinatal animals has yet to be elucidated. Since the placenta is responsible for transport of nutrients and is a major supplier hormones to the fetus, exposure to xenobiotics that alter the function or viability of placenta cells could ostensibly alter the development of the fetus. In this study, JAR cells were used to determine if CPF and the metabolites 3,5,6-trichloro-2-pyridinol (TCP) and chlorpyrifos-oxon (CPO) are toxic to the placenta. Our results indicate that chlorpyrifos (CPF), and its metabolite chlorpyrifos-oxon (CPO) caused a dose-dependent reduction in cellular viability with CPF being more toxic than its metabolites. Chlorpyrifos-induced toxicity was characterized by the loss of mitochondrial potential, the appearance of nuclear condensation and fragmentation, down-regulation of Bcl-2 as well as upregulation of TNFα and FAS mRNA. Pharmacological inhibition of FAS, nicotinic and TNF-α receptors did not attenuate CPF-induced toxicity. Atropine exhibited minimal ability to reverse toxicity. Furthermore, signal transduction inhibitors PD98059, SP600125, LY294002 and U0126 failed to attenuate toxicity; however, SB202190 (inhibitor of p38α and p38β MAPK) sensitized cells to CPF-induced toxicity. Pan-caspase inhibitor Q-VD-OPh produced a slight but significant reversal of CPF-induced toxicity indicating that the major caspase pathways are not integral to CPF-induced toxicity. Taken collectively, these results suggest that chlorpyrifos induces apoptosis in placental cells through pathways not dependent on FAS/TNF signaling, activation of caspases or inhibition of cholinesterase. In addition, our data further indicates that activation of p38 MAPK is integral to the protection cells against CPF-induced injury.

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“…The mitogen-activated protein kinases (MAPKs) are indeed activated by several aldehydes including MDA, acrolein and HNE. MDA activates c-Jun N-terminal kinases (JNK) and extracellular signal-regulated kinases (ERK) (Cheng et al, 2011) and acrolein-induced apoptosis occurs through activation of p38 and ERK (Tanel & Averill-Bates, 2007). The activation of these three MAPK has also been described following treatment with HNE Zarrouki et al, 2007;Pillon et al, 2012) and HHE Bae et al, 2011).…”

Section: Signalling Pathways and Transcription Factorsmentioning

confidence: 99%