146 research outputs found
Screening of DTP Compound Libraries for CK2 Inhibitors with Focus on Natural Products
No full textVarious compound libraries of the Drug Therapeutic Program (DTP) of the NIH/NCI were screened against the catalytic subunit and the tetrameric holoenzyme of protein kinase CK2. Different IC50 values were obtained for the two CK2 molecules. In the case of nortangeretin, the IC50 value was 0.34 μM for the catalytic subunit and 15 μM for the holoenzyme. In the case of coumestrol, opposite results were obtained, i.e., high IC50 for the CK2α subunit (2.7 μM) and a lower IC50 value for the holoenzyme (0.19 μM). From the many compounds identified to inhibit CK2, we have selected 14 different compounds and listed them according to their CK2α/CK2 holoenzyme IC50 ratio. Four compounds were tested on a panel of seven cell lines revealing considerable differences in the degree of CK2 inhibition inside the cells.</p
Synthesis of Triazenoazaindoles: a New Class of Triazenes with Antitumor Activity
No full textDespite improvements in the treatment and prevention of cancer, the number of new diagnoses continues to rise; this has fuelled substantial interest in the development of new and effective chemotherapeutic agents. Compounds of the triazene class, such as dacarbazine, have been used in the clinical management
of many cancer types including brain, leukemia, and melanoma. A new compound class bearing a triazenoazaindole
scaffold was synthesized with the aim of identifying new antiproliferative
agents. Compounds 5a–g and 6a–c were
screened against a panel of human tumor cell lines, and two of them, 5e and 5 f, showed cytotoxicity (GI50 range: 2.2–8.2 mm) in all cell lines. These two compounds even maintained their cytotoxicity in some multidrug-resistant cell lines. Flow cytometry analysis demonstrated their ability to induce cell death by apoptosis with involvement of lysosomes
Characterization of ATM and DNA-PK wild-type and mutant cell lines upon DSB induction in the presence and absence of CK2 inhibitors
No full textA-Raf kinase is a new interacting partner of protein kinase CK2 β subunit
No full textAbstractIn a search for protein kinase CK2 β subunit binding proteins using the two-hybrid system, more than 1000 positive clones were isolated. Beside clones for the α′ and β subunit of CK2, there were clones coding for a so far unknown protein, whose partial cDNA sequence was already deposited in the EMBL database under the accession numbers R08806 and Z17360, for the ribosomal protein L5 and for A-Raf kinase. All isolated clones except the one for CK2 β showed no interaction with the catalytic α subunit of CK2. A-Raf kinase is a new interesting partner of CK2 β. The isolated A-Raf clone represented amino acids 268–606, but also a full length A-Raf clone interacted with CK2 β. At the site of CK2 β, residue 175 and amino acids between residues 194 and 200 are likely to be involved in direct interaction.© 1997 Federation of European Biochemical Societies
Protein kinase CK2:from a molecular biology approach to protein function: 15 years of protein kinase CK2 research
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