ArticleInternational journal of oncology2013
Okadaic acid activates the PKR pathway and induces apoptosis through PKR stimulation in MG63 osteoblast-like cells.
Article in International journal of oncology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- PKR Inhibitor C16 Regulates HIV-gp120 Induced Neuronal Injury and Cognitive Impairment in Vivo and in Vitro Models.Neurochemical research · 2025Article
- Functional Role of Protein Phosphatase-6 (Current medicinal chemistry · 2025Review
- Anticancer Potential of Damnacanthal and Nordamnacanthal fromMolecules (Basel, Switzerland) · 2021Article
- DENV up-regulates the HMG-CoA reductase activity through the impairment of AMPK phosphorylation: A potential antiviral target.PLoS pathogens · 2017 · on this mapArticle
- The Roles of Histone Demethylase Jmjd3 in Osteoblast Differentiation and Apoptosis.Journal of clinical medicine · 2017Review
- Inhibition of PKR protects against HScientific reports · 2016Article
- Deletion of Pr130 Interrupts Cardiac Development in Zebrafish.International journal of molecular sciences · 2016Article
- Protein phosphatase 2A Cα regulates proliferation, migration, and metastasis of osteosarcoma cells.Laboratory investigation; a journal of technical methods and pathology · 2016Article
- Protein Phosphatase 2A Mediates Oxidative Stress Induced Apoptosis in Osteoblasts.Mediators of inflammation · 2015Article
- Comparative analysis of the cytotoxic effects of okadaic acid-group toxins on human intestinal cell lines.Marine drugs · 2014Article
- DADS suppresses human esophageal xenograft tumors through RAF/MEK/ERK and mitochondria-dependent pathways.International journal of molecular sciences · 2014Article
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4 authors at 2 institutions in 1 country.
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Abstract
Double-stranded RNA-dependent protein kinase (PKR) is one of the players in the cellular antiviral responses and is involved in transcriptional stimulation through activation of NF-κB. Treatment of the human osteosarcoma cell line MG63 with the protein phosphatase inhibitor okadaic acid stimulated the expression and phosphorylation of IκBα, as judged from the results of real-time PCR and western blot analysis. We investigated the functional relationship between PKR and signal transduction of NF-κB by establishing PKR-K/R cells that produced a catalytically inactive mutant of PKR. Phosphorylation of eIF-2α, a substrate of PKR, was not stimulated by okadaic acid in the PKR-K/R cells, whereas okadaic acid induced phosphorylation of eIF-2α in MG63 cells. Phosphorylation of NF-κB in MG63 cells was stimulated by okadaic acid; however, okadaic acid did not induce phosphorylation of NF-κB in the PKR-K/R cells. Finally, okadaic acid-induced apoptosis was inhibited in the PKR-K/R cells. Our results suggest that okadaic acid-induced phosphorylation of IκBα was mediated by PKR kinase activity, thus, indicating the involvement of this kinase in the control mechanism governing the activation of NF-κB and induction of apoptosis.
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