Discovery of a Potent and Selective Protein Kinase CK2 Inhibitor by High-Throughput Docking

2003 ◽  
Vol 46 (13) ◽  
pp. 2656-2662 ◽  
Author(s):  
Eric Vangrevelinghe ◽  
Kaspar Zimmermann ◽  
Joseph Schoepfer ◽  
Robert Portmann ◽  
Doriano Fabbro ◽  
...  
Keyword(s):  
Protein Kinase ◽  
High Throughput ◽  
Protein Kinase Ck2 ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor

scholarly journals SGC-CK2-1 Is an Efficient Inducer of Insulin Production and Secretion in Pancreatic β-Cells

Pharmaceutics ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 19
Author(s):  
Mandy Pack ◽  
Claudia Götz ◽  
Selina Wrublewsky ◽  
Mathias Montenarh
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
High Specificity ◽  
Insulin Production ◽  
Biological Functions ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Storage Vesicles ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor

The pyrazolopyrimidine based compound SGC-CK2-1 is a potent and highly specific CK2 inhibitor and a new tool to study the biological functions of protein kinase CK2 irrespective from off-target effects. We used this compound in comparison with the well-established CK2 inhibitor CX-4945 to analyze the importance of CK2 for insulin production and secretion from pancreatic β-cells. Both inhibitors affected the proliferation and viability of MIN6 cells only marginally and downregulated the endogenous CK2 activity to a similar level. Furthermore, both inhibitors increased the message for insulin and boosted the secretion of insulin from storage vesicles. Thus, regarding the high specificity of SGC-CK2-1, we can clearly attribute the observed effects to biological functions of protein kinase CK2.

Quantitative analysis of a phosphoproteome readily altered by the protein kinase CK2 inhibitor quinalizarin in HEK-293T cells

2015 ◽  
Vol 1854 (6) ◽  
pp. 609-623 ◽  
Author(s):  
Cinzia Franchin ◽  
Luca Cesaro ◽  
Mauro Salvi ◽  
Renato Millioni ◽  
Elisabetta Iori ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor

Proteomics perturbations promoted by the protein kinase CK2 inhibitor quinalizarin

2015 ◽  
Vol 1854 (10) ◽  
pp. 1676-1686 ◽  
Author(s):  
Cinzia Franchin ◽  
Mauro Salvi ◽  
Giorgio Arrigoni ◽  
Lorenzo A. Pinna
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor

scholarly journals CX-4945: the protein kinase CK2 inhibitor and anti-cancer drug shows anti-fungal activity

2017 ◽  
Vol 435 (1-2) ◽  
pp. 193-196 ◽  
Author(s):  
Maciej Masłyk ◽  
Monika Janeczko ◽  
Aleksandra Martyna ◽  
Konrad Kubiński
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Cancer Drug ◽  
Fungal Activity ◽  
Anti Cancer ◽  
Anti Fungal ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor

scholarly journals Quinalizarin as a potent, selective and cell-permeable inhibitor of protein kinase CK2

2009 ◽  
Vol 421 (3) ◽  
pp. 387-395 ◽  
Author(s):  
Giorgio Cozza ◽  
Marco Mazzorana ◽  
Elena Papinutto ◽  
Jenny Bain ◽  
Matthew Elliott ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Protein Kinase Ck2 ◽  
Integration Site ◽  
Jurkat Cells ◽  
Mitogen Activated Protein Kinase ◽  
Leukaemia Virus ◽  
Kinase Ck2 ◽  
Ck2 Inhibitors ◽  
Ck2 Inhibitor

Emodin (1,3,8-trihydroxy-6-methyl-anthraquinone) is a moderately potent and poorly selective inhibitor of protein kinase CK2, one of the most pleiotropic serine/threonine protein kinases, implicated in neoplasia and in other global diseases. By virtual screening of the MMS (Molecular Modeling Section) database, we have now identified quinalizarin (1,2,5,8-tetrahydroxyanthraquinone) as an inhibitor of CK2 that is more potent and selective than emodin. CK2 inhibition by quinalizarin is competitive with respect to ATP, with a Ki value of approx. 50 nM. Tested at 1 μM concentration on a panel of 75 protein kinases, quinalizarin drastically inhibits only CK2, with a promiscuity score (11.1), which is the lowest ever reported so far for a CK2 inhibitor. Especially remarkable is the ability of quinalizarin to discriminate between CK2 and a number of kinases, notably DYRK1a (dual-specificity tyrosine-phosphorylated and -regulated kinase), PIM (provirus integration site for Moloney murine leukaemia virus) 1, 2 and 3, HIPK2 (homeodomain-interacting protein kinase-2), MNK1 [MAPK (mitogen-activated protein kinase)-interacting kinase 1], ERK8 (extracellular-signal-regulated kinase 8) and PKD1 (protein kinase D 1), which conversely tend to be inhibited as drastically as CK2 by commercially available CK2 inhibitors. The determination of the crystal structure of a complex between quinalizarin and CK2α subunit highlights the relevance of polar interactions in stabilizing the binding, an unusual characteristic for a CK2 inhibitor, and disclose other structural features which may account for the narrow selectivity of this compound. Tested on Jurkat cells, quinalizarin proved able to inhibit endogenous CK2 and to induce apoptosis more efficiently than the commonly used CK2 inhibitors TBB (4,5,6,7-tetrabromo-1H-benzotriazole) and DMAT (2-dimethylamino-4,5,6,7-tetrabromo-1H-benzimidazole).

Induction of cell death in antiestrogen resistant human breast cancer cells by the protein kinase CK2 inhibitor DMAT

2007 ◽  
Vol 256 (2) ◽  
pp. 229-237 ◽  
Author(s):  
Christina Westmose Yde ◽  
Thomas Frogne ◽  
Anne E. Lykkesfeldt ◽  
Iduna Fichtner ◽  
Olaf-Georg Issinger ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Death ◽  
Protein Kinase ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Protein Kinase Ck2 ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Kinase Ck2 ◽  
Ck2 Inhibitor
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