期刊
BIOCHEMICAL JOURNAL
卷 415, 期 -, 页码 353-365出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20080309
关键词
ATP mimetics; casein kinase 2 (CK2) inhibitor; drug design; homeodomain-interacting protein kinase 2 (HIPK2); provirus integration site for Moloney murine leukaemia virus 1 (PIM 1); selectivity
资金
- AIRC (Associazione italiana per la Ricerca sul Cancro)
- European Commission [(PRO-KlNASERESEARCH 503467)]
- Ministry of Education and Science [PBZ-MIN 014/P05/2004 (Poland)]
- Medical Research Council [MC_EX_G0800765] Funding Source: researchfish
- MRC [MC_EX_G0800765] Funding Source: UKRI
CK2 (casein kinase 2) is a very pleiotropic serine/threonine protein kinase whose abnormally high constitutive activity has often been correlated to pathological conditions with special reference to neoplasia. The two most widely used cell permeable CK2 inhibitors, TBB (4,5,6,7-tetrabromo-1H-benzotriazole) and DMAT (2-dimethylamino-4,5,6,7-tetrabromo-1H-benzimidazole), are marketed as quite specific CK2 blockers. In the present study we show, by using a panel of approx. 80 protein kinases, that DMAT and its parent compound TBI (or TBBz; 4,5,6,7-tetrabronio-1H-benzimidazole) are potent inhibitors of several other kinases, with special reference to PIM (provirus integration site for Moloney murine leukaemia virus)1, PIM2, PIM3, PKD1 (protein kinase D1), HIPK2 (homeodomain-interacting protein kinase 2) and DYRK 1a (dual-specificity tyrosine-phosphorylated and -regulated kinase 1a). In contrast, TBB is significantly more selective toward CK2, although it also inhibits PIM1 and PIM3. In an attempt to
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