Involvement of CK2 in activation of electrophilic genes in endothelial cells by oxidized phospholipids

Afonyushkin, Taras; Oskolkova, Olga; Binder, Bernd R.; Bochkov, Valery N.

doi:10.1194/jlr.m009480

Cited by 27 publications

(25 citation statements)

References 29 publications

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“…This inhibiting effect of PRH on genes encoding components of the VEGF signalling pathway is abrogated by CK2 phosphorylation [43] indicating that VEGF may be one target of CK2 in regulating angiogenesis. It was also recently shown that oxidized phospholipids induced the expression of VEGF in foetal human retinal pigment epithelial (RPE) cells [44]. Inhibition of CK2 in these primary RPE cells resulted in a significant inhibition of the upregulation of VEGF by oxidized phospholipids [45] further supporting the idea that CK2 is acting via VEGF in the process of angiogenesis.…”

Section: Ck2 and Angiogenesissupporting

confidence: 51%

Protein Kinase CK2 and Angiogenesis

Montenarh¹

2014

Adv Clin Exp Med

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CK2 is an ubiquitously expressed protein kinase, which is composed of two catalytic a-and a'-and two noncatalytic b-subunits. CK2 protein levels and kinase activity is elevated in rapidly proliferating cells including cancer cells. There is increasing evidence that CK2 also plays an essential role in angiogenesis, either by interaction or phosphorylation of growth factors or by phosphorylation or binding to proteins in signalling cascades, which are implicated in angiogenesis. Over the last ten years a great number of inhibitors for CK2 were detected, two of them are now in clinical phase II trials for the treatment of cancer patients. Some of these inhibitors were also found to be active in the inhibition of angiogenesis. Thus, CK2 inhibitors probably together with inhibitors of other signalling molecules involved in angiogenesis might be powerful tools for the treatment of cancer and cancer connected angiogenesis (Adv Clin Exp Med 2014, 23, 2, 153-158).

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Section: Ck2 and Angiogenesissupporting

confidence: 51%

Protein Kinase CK2 and Angiogenesis

Montenarh¹

2014

Adv Clin Exp Med

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“…Similar results were observed when comparing DHA/AA supplemented cells to cells supplemented with Palmitic acid:Oleic acid at molar ratio of 1:4 and to un-supplemented cells (Supplementary Figure 1) PEIPC [35] and several isoforms of Oxo-DHA [36] are established agonists of Nrf2. While Oxo-DHA are likely to activate Nrf2 as electrophilic compounds [37] PEIPC might also utilize EP receptors and/or the induction of transient unfolded protein response may activate Nrf2 signaling [38,39].…”

Section: Resultsmentioning

confidence: 99%

Nrf2 deficiency causes lipid oxidation, inflammation, and matrix-protease expression in DHA-supplemented and UVA-irradiated skin fibroblasts

Грубер

Ornelas

Karner

et al. 2015

Free Radical Biology and Medicine

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“…It has been reported that Nrf2 is phosphorylated by CK2 and that this phosphorylation regulates the transcriptional activity of Nrf2 (32,33). The effect of the CK2-mediated phosphorylation on Nrf2 activity is controversial, but several reports have shown that CK2 inhibition results in Nrf2 inactivation (32,34,35). The CK2-mediated phosphorylation of Nrf2 facilitates its nuclear translocation and the upregulation of Nrf2 target gene expression.…”

Section: Discussionmentioning

confidence: 99%

The Casein Kinase 2-Nrf1 Axis Controls the Clearance of Ubiquitinated Proteins by Regulating Proteasome Gene Expression

Tsuchiya

Taniguchi

Ito

et al. 2013

Molecular and Cellular Biology

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c Impairment of the ubiquitin-proteasome system (UPS) has been implicated in the pathogenesis of human diseases, including neurodegenerative disorders. Thus, stimulating proteasome activity is a promising strategy to ameliorate these age-related diseases. Here we show that the protein kinase casein kinase 2 (CK2) regulates the transcriptional activity of Nrf1 to control the expression of the proteasome genes and thus the clearance of ubiquitinated proteins. We identify CK2 as an Nrf1-binding protein and find that the knockdown of CK2 enhances the Nrf1-dependent expression of the proteasome subunit genes. Real-time monitoring of proteasome activity reveals that CK2 knockdown alleviates the accumulation of ubiquitinated proteins upon proteasome inhibition. Furthermore, we identify Ser 497 of Nrf1 as the CK2 phosphorylation site and demonstrate that its alanine substitution (S497A) augments the transcriptional activity of Nrf1 and mitigates proteasome dysfunction and the formation of p62-positive juxtanuclear inclusion bodies upon proteasome inhibition. These results indicate that the CK2-mediated phosphorylation of Nrf1 suppresses the proteasome gene expression and activity and thus suggest that the CK2-Nrf1 axis is a potential therapeutic target for diseases associated with UPS impairment.

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Involvement of CK2 in activation of electrophilic genes in endothelial cells by oxidized phospholipids

Cited by 27 publications

References 29 publications

Protein Kinase CK2 and Angiogenesis

Protein Kinase CK2 and Angiogenesis

Nrf2 deficiency causes lipid oxidation, inflammation, and matrix-protease expression in DHA-supplemented and UVA-irradiated skin fibroblasts

The Casein Kinase 2-Nrf1 Axis Controls the Clearance of Ubiquitinated Proteins by Regulating Proteasome Gene Expression

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