Relevant bibliographies by topics / Protein kinase CK2 – Pathophysiology

Academic literature on the topic 'Protein kinase CK2 – Pathophysiology'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Protein kinase CK2 – Pathophysiology"

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Piazza, Francesco A., Maria Ruzzene, Carmela Gurrieri, Barbara Montini, Luca Bonanni, Gino Chioetto, Giovanni Di Maira, et al. "Multiple myeloma cell survival relies on high activity of protein kinase CK2." Blood 108, no. 5 (September 1, 2006): 1698–707. http://dx.doi.org/10.1182/blood-2005-11-013672.

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Casein kinase 2 (CK2) is a ubiquitous cellular serine-threonine kinase that regulates relevant biologic processes, many of which are dysregulated in malignant plasma cells. Here we investigated its role in multiple myeloma (MM). Analysis of MM cell lines and highly purified malignant plasma cells in patients with MM revealed higher protein and CK2 activity levels than in controls (normal in vitro-generated polyclonal plasma cells and B lymphocytes). The inhibition of CK2 with specific synthetic compounds or by means of RNA interference caused a cytotoxic effect on MM plasma cells that could not be overcome by IL-6 or IGF-I and that was associated with the activation of extrinsic and intrinsic caspase cascades. CK2 blockage lowered the sensitivity threshold of MM plasma cells to the cytotoxic effect of melphalan. CK2 inhibition also resulted in impaired IL-6-dependent STAT3 activation and in decreased basal and TNF-α-dependent IκBα degradation and NF-κB-driven transcription. Our data show that CK2 was involved in the pathophysiology of MM, suggesting that it might play a crucial role in controlling survival and sensitivity to chemotherapeutics of malignant plasma cells.
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Strum, Scott W., Laszlo Gyenis, and David W. Litchfield. "CSNK2 in cancer: pathophysiology and translational applications." British Journal of Cancer 126, no. 7 (November 12, 2021): 994–1003. http://dx.doi.org/10.1038/s41416-021-01616-2.

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AbstractProtein kinase CSNK2 (CK2) is a pleiotropic serine/threonine kinase frequently dysregulated in solid and hematologic malignancies. To consolidate a wide range of biological and clinically oriented data from this unique kinase in cancer, this systematic review summarises existing knowledge from in vitro, in vivo and pre-clinical studies on CSNK2 across 24 different human cancer types. CSNK2 mRNA transcripts, protein levels and activity were found to be routinely upregulated in cancer, and commonly identified phosphotargets included AKT, STAT3, RELA, PTEN and TP53. Phenotypically, it frequently influenced evasion of apoptosis, enhancement of proliferation, cell invasion/metastasis and cell cycle control. Clinically, it held prognostic significance across 14 different cancers, and its inhibition in xenograft experiments resulted in a positive treatment response in 12. In conjunction with commentary on preliminary studies of CSNK2 inhibitors in humans, this review harmonises an extensive body of CSNK2 data in cancer and reinforces its emergence as an attractive target for cancer therapy. Continuing to investigate CSNK2 will be crucial to advancing our understanding of CSNK2 biology, and offers the promise of important new discoveries scientifically and clinically.
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Valentin-Berrios, Shirley D., Jose R. Romero, and Alicia Rivera. "Protein Disulfide Isomerase Regulates Sickle Erythrocyte Volume Via ET-1 Dependent Casein Kinase II Mechanism." Blood 118, no. 21 (November 18, 2011): 2114. http://dx.doi.org/10.1182/blood.v118.21.2114.2114.

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Abstract Abstract 2114 Disordered K+ efflux and osmotically induced water loss leads to red blood cell (RBC) dehydration and plays a role in the pathophysiology of Sickle Cell Disease. We previously reported that activation of endothelin-1 (ET-1) receptors in sickle erythrocyte was partially responsible for dense sickle cell formation. However, the mechanism by which ET-1 regulates RBC volume remains unclear. Serine/threonine kinases have been shown to regulate K+ transport in RBC. Casein Kinase II (CK2), a serine/threonine kinase, phosphorylates acidic proteins, regulates calmodulin activity and cytoskeletal proteins and is present in RBC. CK2 activity is blocked by apigenin, emodin, heparin, and ornithine decarboxylase. Previous reports have shown a role for flavonoids such as apigenin as substrates for erythrocyte plasma membrane oxidoreductases. We recently observed a role for Protein Disulfide Isomerase (PDI) in regulating cellular hydration and K+ efflux in human RBC. PDI catalyzes disulfide interchange reactions in the plasma membrane, mediates redox modifications and is up-regulated under hypoxic conditions. However the relationship between CK2 and PDI in the setting of cellular hydration status is un-explored. Our results indicate that erythrocyte membrane CK2 activity increases when sickle cells are incubated with 500 nM ET-1 for 30 min (2.8 ± 0.1 to 4.9 ± 0.01 nmol/min/mL * 106 cell) an event that is blunted by pre-incubation with the ET-1 B receptor blocker, BQ788 (2.5 ± 0.1 nmol/min/mL * 106 cell, n=3, p<0.04) and 20 μM apigenin (2.7 ± 0.4 nmol/min/mL * 106 cell, n=3, p<0.04). We examined the role of CK2 activation on cellular dehydration. We incubated sickle erythrocytes for 3 hours in deoxygenation-oxygenation cycles in the presence or absence of 20μM apigenin or 2μM 4,5,6,7-tetrabromobenzotriazole (TBB), a specific CK2 inhibitor, and measured the changes in erythrocyte density by phthalate oil density analysis. We observed that inhibition of CK2 led to reduced deoxygenation-stimulated cellular dehydration in sickle erythrocytes by apigenin (D50= 1.106 to 1.100 g/mL) or TBB (D50 =1.097 g/mL). We then studied the role of CK2 inhibitors on PDI activity by Insulin Turbidity Assay and observed that apigenin and TBB led to significant reductions in PDI activity in vitro (64% and 42% respectively). We also studied the effects of the flavonoids: naringenin, naringin, apigenin and rutin on PDI activity and observed reductions in PDI activity that were greater with apigenin>rutin>TBB>naringin>naringenin (n=2, P<0.05). Furthermore, we observed that K+ flux via Gardos channel activation is correlated with PDI activity in vitro in sickle erythrocytes. Taken together our results implicate CK2 and PDI as intermediate regulators of ET-1 stimulated cellular volume systems in red blood cells. Supported by NIH R01-HL09632 to AR. Disclosures: No relevant conflicts of interest to declare.
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Strum, Scott, Laszlo Gyenis, and David W. Litchfield. "CSNK2 in cancer: Pathophysiology and translational applications." Journal of Clinical Oncology 38, no. 15_suppl (May 20, 2020): e15594-e15594. http://dx.doi.org/10.1200/jco.2020.38.15_suppl.e15594.

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e15594 Background: Protein kinase CSNK2 (CK2) is a pleiotropic serine/threonine kinase whose expression levels are frequently elevated in solid and hematologic malignancies. CSNK2 has been discovered to hold prognostic and therapeutic significance across multiple cancers and is an excellent target for oncology research. This systematic review summarizes the current knowledge from in vitro and in vivo studies on the biology of this kinase in cancer alongside pre-clinical/clinical investigations from 24 different human cancer types. Methods: PRISMA methodology was used to generate a study protocol and building-block search strategy, from which a total of 796 publications in PubMed were retrieved across 24 human cancers. 245 of these publications met both screening and inclusion criteria. Data was then systematically extracted, including information about CSNK2 subunit mRNA/protein/activity levels, phosphorylation targets, phenotypic changes, in vivo studies, and prognostic/therapeutic data. The data was thereafter summarized and analyzed. Results: Five targets phosphorylated by CSNK2 were identified in at least 4 cancers: AKT, STAT3, RELA, PTEN, and TP53. The most heavily cited was AKT, identified in 15 cancers. Phenotypically, behaviors influenced by CSNK2 that were reported in 11 or more cancers included: evasion of apoptosis, enhancement of proliferation, enhancement of invasion/metastasis, and cell cycle control. Interestingly, these pathways correlated heavily with the most commonly cited CSNK2 targets. From a clinical perspective, CSNK2 held prognostic significance in 17 of the cancers. Additionally, xenograft experiments were found to have been performed in 13 cancers where CSNK2 inhibition resulted in a positive response to treatment. Lastly, early studies have shown promising results through the clinical application of CSNK2-specific inhibitors, with several clinical trials now underway for further assessment. Conclusions: Overall, our analysis supports CSNK2 as an attractive target for cancer therapy and points to specific areas where additional investigation is critical to advance our understanding of CSNK2 biology. The design of targeted therapies by exploiting the pathophysiology of CSNK2 has the potential to generate impactful treatment strategies across a wide range of cancers, promising exciting new discoveries scientifically and clinically.
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Abu Shehab, Majida, Ian Damerill, Tong Shen, Fredrick J. Rosario, Mark Nijland, Peter W. Nathanielsz, Amrita Kamat, Thomas Jansson, and Madhulika B. Gupta. "Liver mTOR Controls IGF-I Bioavailability by Regulation of Protein Kinase CK2 and IGFBP-1 Phosphorylation in Fetal Growth Restriction." Endocrinology 155, no. 4 (April 1, 2014): 1327–39. http://dx.doi.org/10.1210/en.2013-1759.

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Fetal growth restriction (FGR) increases the risk for perinatal complications and predisposes the infant to diabetes and cardiovascular disease later in life. No treatment for FGR is available, and the underlying pathophysiology remains poorly understood. Increased IGFBP-1 phosphorylation has been implicated as an important mechanism by which fetal growth is reduced. However, to what extent circulating IGFBP-1 is phosphorylated in FGR is unknown, and the molecular mechanisms linking FGR to IGFBP-1 phosphorylation have not been established. We used umbilical cord plasma of appropriate for gestational age (AGA) and growth–restricted human fetuses and determined IGFBP-1 and IGF-I concentrations (ELISA) and site-specific IGFBP-1 phosphorylation (Western blotting using IGFBP-1 phospho-site specific antibodies). In addition, we used a baboon model of FGR produced by 30% maternal nutrient restriction and determined mammalian target of rapamycin (mTOR)C1 activity, CK2 expression/activity, IGFBP-1 expression and phosphorylation, and IGF-I levels in baboon fetal liver by Western blot, enzymatic assay, and ELISA. HepG2 cells and primary fetal baboon hepatocytes were used to explore mechanistic links between mTORC1 signaling and IGFBP-1 phosphorylation. IGFBP-1 was hyperphosphorylated at Ser101, Ser119, and Ser169 in umbilical plasma of human FGR fetuses. IGFBP-1 was also hyperphosphorylated at Ser101, Ser119, and Ser169 in the liver of growth–restricted baboon fetus. mTOR signaling was markedly inhibited, whereas expression and activity of CK2 was increased in growth–restricted baboon fetal liver in vivo. Using HepG2 cells and primary fetal baboon hepatocytes, we established a mechanistic link between mTOR inhibition, CK2 activation, IGFBP-1 hyperphosphorylation, and decreased IGF-I–induced IGF-I receptor autophosphorylation. We provide clear evidence for IGFBP-1 hyperphosphorylation in FGR and identified an mTOR and CK2-mediated mechanism for regulation of IGF-I bioavailability. Our findings are consistent with the model that inhibition of mTOR in the fetal liver, resulting in increased CK2 activity and IGFBP-1 hyperphosphorylation, constitutes a novel mechanistic link between nutrient deprivation and restricted fetal growth.
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Laher, Ismail, and John H. Zhang. "Protein Kinase C and Cerebral Vasospasm." Journal of Cerebral Blood Flow & Metabolism 21, no. 8 (August 2001): 887–906. http://dx.doi.org/10.1097/00004647-200108000-00001.

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Twenty-five years after the discovery of protein kinase C (PKC), the physiologic function of PKC, and especially its role in pathologic conditions, remains a subject of great interest with 30,000 studies published on these aspects. In the cerebral circulation, PKC plays a role in the regulation of myogenic tone by sensitization of myofilaments to calcium. Protein kinase C phosphorylates various ion channels including augmenting voltage-dependent Ca2+ channels and inhibiting K+ channels, which both lead to vessel contraction. These actions of PKC amplify vascular reactivity to different agonists and may be critical in the regulation of cerebral artery tone during vasospasm. Evidence accumulated during at least the last decade suggest that activation of PKC in cerebral vasospasm results in a delayed but prolonged contraction of major arteries after subarachnoid hemorrhage. Most of the experimental results in vitro or in animal models support the view that PKC is involved in cerebral vasospasm. Implication of PKC in cerebral vasospasm helps explain increased arterial narrowing at the signal transduction level and alters current perceptions that the pathophysiology is caused by a combination of multiple receptor activation, hemoglobin toxicity, and damaged neurogenic control. Activation of protein kinase C also interacts with other signaling pathways such as myosin light chain kinase, nitric oxide, intracellular Ca2+, protein tyrosine kinase, and its substrates such as mitogen-activated protein kinase. Even though identifying PKC revolutionized the understanding of cerebral vasospasm, clinical advances are hampered by the lack of clinical trials using selective PKC inhibitors.
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Wong, Aaron K. F., Jacqueline Howie, John R. Petrie, and Chim C. Lang. "AMP-activated protein kinase pathway: a potential therapeutic target in cardiometabolic disease." Clinical Science 116, no. 8 (March 16, 2009): 607–20. http://dx.doi.org/10.1042/cs20080066.

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AMPK (AMP-activated protein kinase) is a heterotrimetric enzyme that is expressed in many tissues, including the heart and vasculature, and plays a central role in the regulation of energy homoeostasis. It is activated in response to stresses that lead to an increase in the cellular AMP/ATP ratio caused either by inhibition of ATP production (i.e. anoxia or ischaemia) or by accelerating ATP consumption (i.e. muscle contraction or fasting). In the heart, AMPK activity increases during ischaemia and functions to sustain ATP, cardiac function and myocardial viability. There is increasing evidence that AMPK is implicated in the pathophysiology of cardiovascular and metabolic diseases. A principle mode of AMPK activation is phosphorylation by upstream kinases [e.g. LKB1 and CaMK (Ca2+/calmodulin-dependent protein kinase], which leads to direct effects on tissues and phosphorylation of various downstream kinases [e.g. eEF2 (eukaryotic elongation factor 2) kinase and p70 S6 kinase]. These upstream and downstream kinases of AMPK have fundamental roles in glucose metabolism, fatty acid oxidation, protein synthesis and tumour suppression; consequently, they have been implicated in cardiac ischaemia, arrhythmias and hypertrophy. Recent mechanistic studies have shown that AMPK has an important role in the mechanism of action of MF (metformin), TDZs (thiazolinediones) and statins. Increased understanding of the beneficial effects of AMPK activation provides the rationale for targeting AMPK in the development of new therapeutic strategies for cardiometabolic disease.
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Cereijido, M., L. Shoshani, and R. G. Contreras. "Molecular Physiology and Pathophysiology of Tight Junctions I. Biogenesis of tight junctions and epithelial polarity." American Journal of Physiology-Gastrointestinal and Liver Physiology 279, no. 3 (September 1, 2000): G477—G482. http://dx.doi.org/10.1152/ajpgi.2000.279.3.g477.

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The tight junction (TJ) was first noticed through its ability to control permeation across the paracellular route, but the homologies of its molecular components with peptides that participate in tumor suppression, nuclear addressing, and cell proliferation indicate that it may be involved in many other fundamental functions. TJs are formed by a dozen molecular species that assemble through PDZ and other protein-protein clustering promoting sequences, in response to the activation of E-cadherin. The TJ occupies a highly specific position between the apical and the basolateral domains. Its first molecular components seem to be delivered to such a position by addressing signals in their molecule and, once anchored, serve as a clustering nucleus for further TJ-associated molecules. Although in mature epithelial cells TJs and E-cadherin do not colocalize, a complex chain of reactions goes from one to the other that involves α-, β-, and γ-catenins, two different G proteins, phospholipase C, protein kinase C, calmodulin, mitogen-activated protein kinase, and molecules pertaining to the cytoskeleton, which keep the TJ sensitive to physiological requirements and local conditions (notably to Ca2+-dependent cell-cell contacts) throughout the life of the epithelium.
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Baroudi, Ghayath, Yongxia Qu, Omar Ramadan, Mohamed Chahine, and Mohamed Boutjdir. "Protein kinase C activation inhibits Cav1.3 calcium channel at NH2-terminal serine 81 phosphorylation site." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 4 (October 2006): H1614—H1622. http://dx.doi.org/10.1152/ajpheart.00095.2006.

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The Cav1.3 (α1D) variant of L-type Ca2+ channels plays a vital role in the function of neuroendocrine and cardiovascular systems. In this article, we report on the molecular and functional basis of α1D Ca2+ channel modulation by protein kinase C (PKC). Specifically, we show that the serine 81 (S81) phosphorylation site at the NH2-terminal region plays a critical role in α1D Ca2+ channel modulation by PKC. The introduction of a negatively charged residue at position 81, by converting serine to aspartate, mimicked the PKC phosphorylation effect on α1D Ca2+ channel. The modulation of α1D Ca2+ channel by PKC was prevented by dialyzing cells with a 35-amino acid peptide mimicking the α1D NH2-terminal region comprising S81. In addition, the data revealed that only βII- and εPKC isozymes are implicated in this regulation. These novel findings have significant implications in the pathophysiology of α1D Ca2+ channel and in the development of PKC isozyme-targeted therapeutics.
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Mika, Delphine, Wito Richter, and Marco Conti. "A CaMKII/PDE4D negative feedback regulates cAMP signaling." Proceedings of the National Academy of Sciences 112, no. 7 (February 2, 2015): 2023–28. http://dx.doi.org/10.1073/pnas.1419992112.

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cAMP production and protein kinase A (PKA) are the most widely studied steps in β-adrenergic receptor (βAR) signaling in the heart; however, the multifunctional Ca2+/calmodulin-dependent protein kinase II (CaMKII) is also activated in response to βAR stimulation and is involved in the regulation of cardiac excitation-contraction coupling. Its activity and expression are increased during cardiac hypertrophy, in heart failure, and under conditions that promote arrhythmias both in animal models and in the human heart, underscoring the clinical relevance of CaMKII in cardiac pathophysiology. Both CaMKII and PKA phosphorylate a number of protein targets critical for Ca2+ handling and contraction with similar, but not always identical, functional consequences. How these two pathways communicate with each other remains incompletely understood, however. To maintain homeostasis, cyclic nucleotide levels are regulated by phosphodiesterases (PDEs), with PDE4s predominantly responsible for cAMP degradation in the rodent heart. Here we have reassessed the interaction between cAMP/PKA and Ca2+/CaMKII signaling. We demonstrate that CaMKII activity constrains basal and βAR-activated cAMP levels. Moreover, we show that these effects are mediated, at least in part, by CaMKII regulation of PDE4D. This regulation establishes a negative feedback loop necessary to maintain cAMP/CaMKII homeostasis, revealing a previously unidentified function for PDE4D as a critical integrator of cAMP/PKA and Ca2+/CaMKII signaling.
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Dissertations / Theses on the topic "Protein kinase CK2 – Pathophysiology"

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Holland, Zoe. "Plasmodium falciparum protein kinase CK2." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/606/.

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Malaria, caused by infection with intracellular protozoan parasites of the genus Plasmodium, is responsible for 300 to 600 million clinical cases annually (Snow et al., 2005), resulting in the deaths of up to three million people every year (Breman, 2001, Breman et al., 2004). There is a clear need for further research aimed at identifying novel drug targets (Ridley, 2002). Reversible phosphorylation of proteins is a major regulatory mechanism in most cellular processes, and protein kinases are considered promising drug targets, comprising as much as 30% of all protein targets under investigation (Cohen, 2002). The divergences between human and plasmodial protein kinases suggest that specific inhibition of the latter is an achievable goal (Doerig, 2004, Doerig and Meijer, 2007). This study investigates protein kinase CK2 of Plasmodium falciparum, seeking to establish by reverse genetics and biochemical approaches whether it represents a possible antimalarial drug target. Protein-kinase CK2, formerly known as Casein Kinase II, is a dual-specificity (Serine/Threonine and Tyrosine) protein kinase ubiquitously expressed in eukaryotes. It has over 300 cellular substrates catalogued to date (Meggio and Pinna, 2003). Consistent with its multiple substrates, the enzyme plays a crucial role in many cellular processes, and is essential to viability in yeast and slime mould (Padmanabha et al., 1990, Kikkawa et al., 1992). The human CK2 holoenzyme consists of two catalytic a or a’ subunits and two regulatory b subunits, and recent evidence indicates that the latter interact with several protein kinases in addition to CK2a (reviewed in (Bibby and Litchfield, 2005)), pointing to a likely role in the integration of numerous signalling pathways. A putative CK2a orthologue and two predicted CK2b subunits were identified in the P. falciparum genome (Ward et al., 2004, Anamika et al., 2005). Here we present the biochemical characterisation of the PfCK2a orthologue and both PfCK2b orthologues, and demonstrate by using a reverse genetics approach that each of the three subunits is essential for completion of the erythrocytic asexual cycle of the parasite, thereby validating the enzyme as a possible drug target. Recombinant PfCK2a possesses protein kinase activity, exhibits similar substrate and co-substrate preferences to those of CK2a subunits from other organisms, and interacts with both of the PfCK2b subunits in vitro. PfCK2a is amenable to inhibitor screening, and we report differential susceptibility between the human and P. falciparum CK2a enzymes to a small molecule inhibitor. Taken together, the data indicate that PfCK2a is an attractive, validated target for antimalarial chemotherapeutic intervention.
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Ling, Ann Lee. "Protein kinase CK2 : structure, interactions and inhibition." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609645.

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Ganley, Ian Gordon. "Interaction of phospholipase D1 with protein kinase CK2." Thesis, University of Cambridge, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.620410.

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Heriche, Jean-Karim. "Protéine kinase CK2 et prolifération cellulaire." Grenoble 1, 1996. http://www.theses.fr/1996GRE10174.

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La proteine kinase ck2 est une serine/threonine kinase dont la sous-unite catalytique (ck2a) est souvent associee a une sous-unite regulatrice (ck2b) au sein d'un tetramere a#2b#2. Bien que sa fonction et sa regulation ne soient pas connues, on suppose qu'elle participe au controle de la proliferation cellulaire. Un signal mitogene majeur dans de nombreux types cellulaires est forme par l'activation sequentielle des trois kinases raf/mek1/mapk. Nous nous sommes donc demandes si la ck2 pouvait etre connectee a cette voie de transduction du signal proliferatif. Pour cela, nous avons suivi une demarche a base de transfections et d'experiences in vitro en utilisant des mutants des proteines impliquees. Nous avons ainsi pu montrer qu'une population de ck2a independante de ck2b presente les caracteristiques d'un nouveau substrat pour raf. En effet, ck2a est phosphorylee et inhibee en presence de raf actif in vitro et in vivo et la presence de ck2b empeche cette phosphorylation. Nous avons egalement montre que ck2a peut s'associer a mek1 et inhiber son activation par le serum. Cet effet de ck2a sur mek1 passe par l'association de ck2a avec la phosphatase pp2a car un mutant de ck2a incapable de s'associer a la phosphatase n'a plus d'effet sur mek1. L'inhibition de mek1 par ck2a correle avec une forte inhibition de la croissance clonale des cellules en presence de ck2a. De plus, le complexe ck2a/pp2a est dissocie en reponse au pdgf in vivo et par raf in vitro, suggerant que ce complexe est bien un regulateur physiologique de mek1 et de la proliferation cellulaire. Enfin, en exploitant les analogies entre ck2a et la serine/threonine kinase apparentee gsk-3, nous avons egalement trouve que ck2a pouvait etre un substrat associe de la tyrosine kinase abl. La signification biologique de cette association est discutee
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Wang, Zilong. "Expression of epitope-tagged protein kinase CK2 in mammalian cells." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ32281.pdf.

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Lee, Yew. "Molecular and transgenic approaches to understanding the function of protein kinase CK2 in plants /." Digital version accessible at:, 1998. http://wwwlib.umi.com/cr/utexas/main.

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Hou, Zengye. "Development of Novel Protein Kinase CK2 Inhibitors with Nitrogen Heterocyclic Scaffolds." 京都大学 (Kyoto University), 2013. http://hdl.handle.net/2433/174543.

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Mitchell, Louise E. "The regulation of RNA polymerase III transcription by protein kinase CK2." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/399/.

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In order for cells to proliferate, a certain size has to be reached, which depends primarily on the rate of translation. RNA polymerase (pol) III plays a key role in protein synthesis by catalysing the production of small, untranslated RNA molecules such as transfer (tRNA) and 5S ribosomal RNA (5S rRNA). Indeed, recent evidence suggests that tRNAiMet production is limiting for translation and proliferation in some cell types. Therefore, the rate of pol III transcription plays a fundamental role in cellular growth and proliferation. Regulation of pol III output is mediated via a number of different mechanisms that can alter the activities of the transcription factors which are responsible for directing pol III transcription. Work presented in this thesis aimed at investigating the mechanisms behind the regulation of pol III transcription by the protein kinase CK2.
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Llinas, Alexander J. "The activities of protein kinase CK2 in oogenesis of Xenopus laevis." Thesis, University of St Andrews, 1999. http://hdl.handle.net/10023/14510.

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Protein kinases play important roles in regulating cellular functions in many organisms. This work deals specifically with the protein kinase CK2 (casein kinase II) and its role in regulating the activity of proteins involved in oocyte development in Xenopus laevis. Protein kinase CK2 is a tetrameric enzyme containing two catalytic subunits (alpha and alpha') and two identical regulatory subunits (beta) which forms the holoenzyme. CK2 phosphorylates many different proteins involved in many aspects of cellular functions. It phosphorylates serine and threonine sites and is considered to be a ubiquitous enzyme, expressed at different levels in different cell types. In this study CK2 activity was characterized in material from two sources: from isolated nuclei and messenger ribonucleoprotein (mRNP) particles from Xenopus oocytes. cDNAs expressing both the alpha and the beta subunits were cloned and antibodies were raised against the fusion protein containing the beta-subunit. The main objective of this study was to determine the effects that CK2 had on proteins involved in oocyte development. The interaction of CK2 with a protein known as histone deacetylase was studied in depth to determine how phosphorylation might influence its function and cellular compartmentalisation. Specifically, phosphorylation by CK2 is shown to improve the kinetics of nuclear unport, and the interaction of histone deacetylase with alpha-importin, a well-established nuclear transport protein, is revealed to be dependent on the phosphorylation state of histone deacetylase. Another aspect of this work is related to the association of CK2 with mRNP particles in the cytoplasm. mRNP particles function as long term storage units for mRNA to be used during oocyte maturation and early embryogenesis. It has been postulated that a protein kinase associated with these particles plays a role in controlling the binding of mRNA to proteins involved in translation repression (mRNA masking proteins). This study lends support to that theory, and the possible effects of CK2 phosphorylation on the masking "Y-box" proteins are discussed.
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Bestgen, Benoit. "Selective modulation of the Protein Kinase CK2 : discovery, syntheses and characterization of non-ATP site inhibitors of CK2." Thesis, Lyon 1, 2015. http://www.theses.fr/2015LYO10247.

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La Protéine Kinase CK2 est une enzyme tétramérique composé d'un dimère de sous-unité régulatrice (β) et de deux sous-unités catalytiques, CK2α et/ou CK2α'. La sous-unité catalytique de CK2 est constitutivement active alors que la sous-unité régulatrice régule seulement la sélection des substrats phosphorylés par CK2. CK2 est une Ser/Thr protéine kinase ubiquitaire impliquée dans le contrôle de nombreuses voies de signalisations. La dérégulation de CK2 promeut le développement des cancers et il a été démontré que CK2 est une cible pertinente dans le traitement des cancers. Notre objectif était de cibler la protéine kinase CK2 de manière indépendante du site actif. Deux séries de composés ont été étudiés : Basé sur un premier hit faiblement actif (CI50 = 30 μM) mais inhibant CK2 de manière non- ATP compétitive, des dérivés comportant le noyau 2-aminothiazole ont été synthétisés et un composé actif (CI50 = 0,6 μM) et efficace in cellulo a été obtenu. Grace à des expériences sur des mutants ponctuels de CK2, des expériences de dichroïsme circulaire, de la STD-RMN et de la modélisation moléculaire, le site de fixation de nos inhibiteurs a été précisément défini à l'interface de la boucle riche en glycine et de l'hélice-αC. Des inhibiteurs de l'interaction α/β ont été étudiés à partir d'un peptide cyclique jusqu'au développement de petites molécules via un screening virtuel. Des études de relations structure-activité ont été réalisé sur la série de composés synthétisées et des tests cellulaires ont été mis en place afin d'évaluer ces composés. Les deux classes de molécules décrites sont des outils intéressants pour comprendre la régulation physiologique de la protéine kinase CK2 et des opportunités prometteuses dans le traitement de certains cancers
The protein kinase CK2 is a tetrameric enzyme composed of a dimer of regulatory subunits (β) and two catalytic subunits, CK2α and/or CK2α’. The catalytic subunit of CK2 is constitutively active, while the regulatory subunit modulates the selectivity toward a subset of substrate proteins. CK2 is a ubiquitous Ser/Thr protein kinase involved in the control of various signaling pathways, and dysregulation of CK2 promotes cancer development. CK2 has been proved to be a valuable target in cancer treatment. Our objective was to target CK2 outside the ATP-pocket. Two independent classes of compounds were studied: Based on a first hit with a low potency (IC50 = 30 μM) but a non-ATP competitive mechanism of action, several 2-aminothiazole derivatives were synthesized to lead to a potent (IC50 = 0.6 μM) and cell efficient allosteric inhibitor of CK2. Using single mutation scanning, CD spectrometry, STD-NMR and docking experiments, the binding site of our compounds was precisely defined outside the ATP-pocket, at the interface of the glycine-rich loop and the αC-helix. Inhibitors of the α/β interaction were studied from a small cyclic peptide to the development of small molecules through Virtual Ligand Screening. Structures Activity Studies were conducted on the synthesized derivatives and cellular based assays to evaluate the α/β inhibitors were set up. The two classes of compounds developed herein are valuable tools to understand the physiological regulation of the protein kinase CK2, and potential new opportunities in cancer treatment
Das Protein Kinase CK2 ist ein tetrameres Enzym, das aus einem Dimer von regulatorischen Untereinheiten (β) und zwei katalytischen Untereinheiten (CK2α und/oder CK2α’) besteht. Die katalytische Untereinheit der CK2 ist konstitutiv aktiv, während die regulatorische Untereinheit die Auswahl einiger der durch CK2 phosphorylierten Substrate steuert. CK2 ist eine ubiquitäre Proteinkinase, die an der Kontrolle zahlreicher Signalwege beteiligt ist. Eine Fehlregulation der CK2 fördert die Tumorenstehung. Es konnte gezeigt werden, dass CK2 eine vielversprechende Zielstruktur für die Entwicklung neuer Therapeutika ist. Unser Ziel war es, neue Hemmstoffe der Proteinkinase CK2 zu entwickeln, die an anderen Stellen als dem aktiven Zentrum angreifen. Zwei Serien von Verbindungen sind untersucht worden: Basierend auf einem ersten schwach aktiven “Hit” (IC50 = 30 μM), der einen nicht-ATPkompetitiven Wirkmechanismus aufwies, wurden einige neue 2-Aminothiazol-Derivate synthetisiert. Dadurch wurden allosterische Inhibitoren mit einer deutlich gesteigerte Potenz (IC50 = 0,6 μM) und einer beachtlichen Zellaktivität erhalten. Mittels eines CK2- Punktmutanten-Screenings, Zirkulardichroismus-Spektrometrie, STD-NMR und molekularer Docking-Simulationen konnte die Bindestelle unserer Hemmstoffe außerhalb der ATPBindetasche, zwischen der Glycin-reichen Schleife und der αC-Helix, lokalisiert werden. Desweiteren wurden niedermolekulare Inhibitoren der α/β-Interaktion entwickelt, ausgehend von einem zyklischen Peptid sowie von Hitverbindungen aus einem virtuellen Screening. Neue Verbindungen wurden synthetisiert und die Struktur- Wirkungsbeziehungen analysiert; zusätzlich wurde ein Zellassay zur Überprüfung des postulierten Wirkmechanismus etabliert. Die beiden entwickelten Verbindungsklassen sind interessante Werkzeuge, um die physiologische Regulation der Proteinkinase CK2 näher zu analysieren; überdies stellen sie Ausgangspunkte für die Entwicklung neuartiger Krebstherapeutika dar
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Books on the topic "Protein kinase CK2 – Pathophysiology"

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Pinna, Lorenzo A., ed. Protein Kinase CK2. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.

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Ahmed, Khalil, Olaf-Georg Issinger, and Jorge E. Allende, eds. Protein Kinase CK2 — From Structure to Regulation. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1723-8.

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Ahmed, Khalil, O. G. Issinger, and E. Chambaz, eds. A Molecular and Cellular View of Protein Kinase CK2. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4419-8624-5.

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Ahmed, Khalil, Olaf-Georg Issinger, and Ryszard Szyszka, eds. Protein Kinase CK2 Cellular Function in Normal and Disease States. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-14544-0.

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Protein kinase C in insulin action, resistance, and secretion. Austin: R.G. Lanes Co., 1994.

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Farese, Robert V. The role of protein kinase C in insulin action, resistence and secretion. Austin: R.G. Landes, 1994.

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1934-, Ahmed Khalil, Allende Jorge E. Dr, and Issinger O. G, eds. Protein kinase CK2: From structure to regulation. Dordrecht: Kluwer Academic Publishers, 2001.

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Pinna, Lorenzo A. Protein Kinase CK2. Wiley & Sons, Incorporated, John, 2012.

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Pinna, Lorenzo A. Protein Kinase CK2. Wiley & Sons, Incorporated, John, 2012.

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Pinna, Lorenzo A. Protein Kinase CK2. Wiley & Sons, Incorporated, John, 2012.

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Book chapters on the topic "Protein kinase CK2 – Pathophysiology"

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Protein Kinase CK2." In Encyclopedia of Signaling Molecules, 1482. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101098.

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Niefind, Karsten, and Roberto Battistutta. "Structural Bases of Protein Kinase CK2 Function and Inhibition." In Protein Kinase CK2, 1–75. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch1.

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Seldin, David C., and Esther Landesman-Bollag. "The Oncogenic Potential of CK2." In Protein Kinase CK2, 292–304. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch10.

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Ruzzene, Maria. "Addiction of Cancer Cells to CK2: Survival at All Costs or Achilles' Heel?" In Protein Kinase CK2, 305–18. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch11.

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Trembley, Janeen H., JingJiang Wu, Gretchen M. Unger, Betsy T. Kren, and Khalil Ahmed. "CK2 Suppression of Apoptosis and Its Implication in Cancer Biology and Therapy." In Protein Kinase CK2, 319–43. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch12.

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Piazza, Francesco. "Protein Kinase CK2 in Normal and Malignant Hematopoiesis." In Protein Kinase CK2, 344–62. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch13.

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Filhol, Odile, Alexandre Deshiere, and Claude Cochet. "Role of CK2 in the Control of Cell Plasticity in Breast Carcinoma Progression." In Protein Kinase CK2, 363–82. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch14.

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Drygin, Denis. "CK2 as a Logical Target in Cancer Therapy: Potential for Combining CK2 Inhibitors with Various Classes of Cancer Therapeutic Agents." In Protein Kinase CK2, 383–439. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch15.

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Montenarh, Mathias, and Claudia Götz. "The Interactome of Protein Kinase CK2." In Protein Kinase CK2, 76–116. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch2.

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Cesaro, Luca, and Mauro Salvi. "CK2 Contribution to the Generation of the Human Phosphoproteome." In Protein Kinase CK2, 117–28. Oxford, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118482490.ch3.

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Conference papers on the topic "Protein kinase CK2 – Pathophysiology"

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Reykhardt, Boris A., and Peter D. Shabanov. "Neuroprotective effects of protein kinase CK2 modulators." In II Международная конференция, посвящеенная 100- летию И.А. Држевецкой. СКФУ, 2022. http://dx.doi.org/10.38006/9612-62-6.2022.271.275.

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Zhou, Bingying, Michelle Kassner, Holly Yin, Channing J. Der, and Adrienne D. Cox. "Abstract LB-217: CK2 protein kinase promotes resistance to MAPK pathway inhibition." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-217.

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Lian, Haiwei, Ning Shen, Yun Zhou, Dun Li, and Hui Feng. "Abstract 240: Therapeutic targeting of protein kinase ck2 in mycn-driven neuroblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-240.

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Lian, Haiwei, Ning Shen, Yun Zhou, Dun Li, and Hui Feng. "Abstract 240: Therapeutic targeting of protein kinase ck2 in mycn-driven neuroblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-240.

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Nienberg, Christian, Anika Retterath, Kira Becher, Henning D. Mootz, and Joachim Jose. "Click chemistry for advanced drug discovery applications of human protein kinase CK2." In 1st International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2015. http://dx.doi.org/10.3390/ecmc-1-a020.

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Turner, Joel G., Jana L. Dawson, Elizabeth J. Ciaravino, John M. Koomen, and Daniel M. Sullivan. "Abstract 725: Protein kinase-CK2 inhibition as a potential treatment for multiple myeloma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-725.

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Turowec, Jacob P., James S. Duncan, Shawn Li, Greg Gloor, and David W. Litchfield. "Abstract 4970: Convergence of protein kinase and caspase signaling: A mechanism for pathological rewiring of survival pathways by protein kinase CK2." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4970.

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Drygin, Denis, Joshua Bliesath, Nanni Huser, Chris Proffitt, Adam Siddiqui-Jain, Mayuko Omori, Ryan Stansfield, et al. "Abstract 3765: Discovery and biological characterization of CX-8184, a potent inhibitor of protein kinase CK2." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3765.

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Padgaonkar, Amol, Olga Rechkoblit, Stephen Cosenza, Venkat R. Pallela, Venkata Subbaiah DRC, MV Ramana Reddy, Aneel Aggarwal, and E. Premkumar Reddy. "Abstract 3239: Discovery and biological characterization of ON108600, a small molecule inhibitor of protein kinase CK2." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3239.

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Nickelsen, Anna, and Joachim Jose. "Photo-crosslinking of human protein kinase regulatory subunit CK2β for the identification of CK2 binding partners." In 5th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecmc2019-06334.

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