Phosphorylation and cytoplasmic localization of MAPK p38 during apoptosis signaling in bone marrow granulocytes of mice irradiated in vivo and the role of amifostine in reducing these effects

Segreto, Helena Regina Cômodo; Oshima, Celina T. F.; Franco, Marcello; Silva, Maria Regina R.; Egami, Mizue Imoto; Teixeira, Vicente P.C.; Segreto, Roberto Araújo

doi:10.1016/j.acthis.2009.12.002

Cited by 14 publications

(13 citation statements)

References 57 publications

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“…The phosphorylation of p38 kinase by various kinds of stresses occurs at the Tyr and Thr residues with subsequent induction cell death [Segreto et al, 2011]. The phosphorylation of p38 kinase by various kinds of stresses occurs at the Tyr and Thr residues with subsequent induction cell death [Segreto et al, 2011].…”

Section: Discussionmentioning

confidence: 99%

“…Also p38 kinase is suggested a proximal effector of apoptosis in many cell types. The phosphorylation of p38 kinase by various kinds of stresses occurs at the Tyr and Thr residues with subsequent induction cell death [Segreto et al, 2011]. On the other hand, it has been shown that activated p38 might have a protective role as well [Sun et al, 2006].…”

Section: Discussionmentioning

confidence: 99%

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Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs

Bironaitė

Brunk

Venalis

2013

J of Cellular Biochemistry

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The involvement of extracellular signal-regulated kinases 1 and 2 (ERK1,2), stress kinase p38 and c-Jun NH2 -terminal kinases 1 and 2 (JNK1,2) on Hsp70-upregulation following mild heat shock, and resulting cell protection, was studied on rabbit primary myoblasts. Cells subjected to heat stress (42°C; 60 min) showed a significantly enhanced amount of heat-shock-induced protein 70 (Hsp70), correlating with sustained phosphorylation of MAP kinases ERK1,2, inhibition of p38 and JNK1,2 activation. Induced Hsp70 did not autocrinally suppress activation of transcription factor c-Jun, suggesting involvement of the latter in the protection of myoblasts following heat shock. The inhibition of stress kinases p38, JNK1,2, and MEK1,2 by SP600125, SB203580, and UO126, respectively, established the involvement of JNK1,2 and p38 as upstream, and ERK1,2 as downstream targets of Hsp70 induction. Moreover, the effect of the MEK1,2 inhibitor UO126 revealed a new pathway of c-Jun activation by ERK1,2 in myogenic heat-stressed stem cells. The presented data show that transient activation of JNK1, JNK2, and p38 is necessary for Hsp70 induction and ensuing cell protection. In conclusion, affecting myogenic stem cell protective mechanisms might be a useful strategy in improving stem cell survival and their expanded application in therapy.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs

Bironaitė

Brunk

Venalis

2013

J of Cellular Biochemistry

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“…Phosphorylation of p38 MAPK has been coupled to activated caspase-3 (Segreto et al, 2011). Caspases are synthesized as inactive proenzymes and activated by cleavage at specific Asp residues.…”

Section: Discussionmentioning

confidence: 99%

Epoxyeicosatrienoic Acids Prevent Cisplatin-Induced Renal Apoptosis through a p38 Mitogen-Activated Protein Kinase–Regulated Mitochondrial Pathway

et al. 2013

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Soluble epoxide hydrolase (sEH) catalyzes the conversion of epoxyeicosatrienoic acids into less active eicosanoids, and inhibitors of sEH have anti-inflammatory and antiapoptotic properties. Based on previous observations that sEH inhibition attenuates cisplatin-induced nephrotoxicity by modulating nuclear factor-kB signaling, we hypothesized that this strategy would also attenuate cisplatin-induced renal apoptosis. Inhibition of sEH with AR9273 [1-adamantan-1-yl-3-(1-methylsulfonyl-piperidin-4-ylurea)] reduced cisplatin-induced apoptosis through mechanisms involving mitochondrial apoptotic pathways and by reducing reactive oxygen species. Renal mitochondrial Bax induction following cisplatin treatment was significantly decreased by treatment of mice with AR9273 and these antiapoptotic effects involved p38 mitogen-activated protein kinase signaling. Similar mechanisms contributed to reduced apoptosis in Ephx2 2/2 mice treated with cisplatin. Moreover, in pig kidney proximal tubule cells, cisplatin-induced mitochondrial trafficking of Bax and cytochrome c, caspase-3 activation, and oxidative stress are significantly attenuated in the presence of epoxyeicosatrienoic acids (EETs). Collectively, these in vivo and in vitro studies demonstrate a role for EETs in limiting cisplatin-induced renal apoptosis. Inhibition of sEH represents a novel therapeutic strategy for protection against cisplatin-induced renal damage.

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“…26,27 Many studies have shown that some clinical chemotherapeutic agents could induce cancer cell apoptosis via regulating MAPKs and Akt kinase activity. [28][29][30] To determine the role of these kinases in tetrandrine-induced HCC apoptosis, Western blot analysis was used to evaluate the activity of MAPKs and Akt-related proteins after tetrandrine treatment. Cancer Therapy The results showed that phosphorylated levels of ERK1/2, JNK and Akt decreased after tetrandrine treatment, but there was no significant change in phospho-p38 protein level (Fig.…”

Section: Tetrandrine Induces Hcc Cell Apoptosis Through Inhibition Ofmentioning

confidence: 99%

Tetrandrine induces apoptosis by activating reactive oxygen species and repressing Akt activity in human hepatocellular carcinoma

Liu¹,

Gong²,

Mao³

et al. 2011

Intl Journal of Cancer

130

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Tetrandrine, a bisbenzylisoquinoline alkaloid component of broadly used traditional Chinese medicine, has antitumor effects against some cancers. In our study, we investigated the effects of tetrandrine on the human hepatocellular carcinoma (HCC) in vitro and in vivo. The results showed that tetrandrine effectively induced apoptosis of liver cancer cell in a dose-and time-dependent manner accompanied by alteration of cell morphology, chromatin fragmentation and caspase activation. Tetrandrine treatment also induced intracellular accumulation of reactive oxygen species (ROS), and ROS scavengers (LNAC and GSH) completely blocked the effects of tetrandrine-induced apoptosis, suggesting that the generation of ROS plays an important role in tetrandrine-induced apoptosis. Although the activities of JNK and ERK were inhibited significantly by tetrandrine treatment, JNK and ERK are not involved in the tetrandrine-induced apoptosis. In contrast, Akt activity was found to be closely related to tetrandrine-induced apoptosis. The data demonstrated that Akt activity inhibitor LY294002 synergistically promoted tetrandrine-induced apoptosis of HCC, whereas ectopic expression of Akt contrastly abrogated partial of the tetrandrine-induced apoptosis. These data suggest that Akt signal is the downstream event of ROS generation in the tetrandrine-induced HCC cell apoptosis. Moreover, the results of xenograft in nude mice were consistent with that of the in vitro studies. Therefore, our data suggest that tetrandrine may be a promising agent for the treatment of HCC as a regulator of ROS/Akt pathway.

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Phosphorylation and cytoplasmic localization of MAPK p38 during apoptosis signaling in bone marrow granulocytes of mice irradiated in vivo and the role of amifostine in reducing these effects

Cited by 14 publications

References 57 publications

Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs

Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs

Epoxyeicosatrienoic Acids Prevent Cisplatin-Induced Renal Apoptosis through a p38 Mitogen-Activated Protein Kinase–Regulated Mitochondrial Pathway

Tetrandrine induces apoptosis by activating reactive oxygen species and repressing Akt activity in human hepatocellular carcinoma

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