Casein kinase II is a selective target of HIV-1 transcriptional inhibitors

Critchfield, J. William; Coligan, John E.; Folks, Thomas M.; Butera, Salvatore T.

doi:10.1073/pnas.94.12.6110

Cited by 122 publications

(79 citation statements)

References 46 publications

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“…Recent studies have shown that LY294002 inhibits both PI3-kinase and casein kinase II (Davies et al, 2000). We used apigenin, a casein kinase II inhibitor (Critchfield et al, 1997), to support our conclusion that PI3-kinase is involved in TNFa-induced degradation of ERa. Apigenin failed to inhibit TNFa-induced degradation of ERa in MCF-7 cells ( Figure 4D).…”

Section: Phosphatidylinositol-3-kinase Inhibitor Ly294002 Stabilises mentioning

confidence: 56%

Tumour necrosis factor and PI3-kinase control oestrogen receptor alpha protein level and its transrepression function

et al. 2004

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Oestrogen receptor alpha (ERa) is an oestrogen-activated transcription factor, which regulates proliferation and differentiation of mammary epithelial cells by activating or repressing gene expression. ERa is a critical prognostic indicator and a therapeutic target for breast cancer. Patients with tumours that express higher level of ERa have better prognosis than patients with tumours that are ERa negative or express lower level of ERa. Better prognosis in ERa-positive patients is believed to be due to repression of proinvasive gene expression by ERa. Oestrogen receptor alpha represses gene expression by transrepressing the activity of the transcription factors such as nuclear factor-kappaB or by inducing the expression of transcriptional suppressors such as MTA3. In this report, we show that ERa transrepresses the expression of the proinvasive gene interleukin 6 (IL-6) in ERa-negative MDA-MB-231 breast cancer cells stably overexpressing ERa. Using these cells as well as ERa-positive MCF-7 and ZR-75-1 cells, we show that tumour necrosis factor alpha (TNFa) and the phosphatidylinositol-3-kinase (PI3-kinase) modulate transrepression function of ERa by reducing its stability. From these results, we propose that TNFa expression or PI3-kinase activation lead to reduced levels of ERa protein in cancer cells and corresponding loss of transrepression function and acquisition of an invasive phenotype.

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Section: Phosphatidylinositol-3-kinase Inhibitor Ly294002 Stabilises mentioning

confidence: 56%

Tumour necrosis factor and PI3-kinase control oestrogen receptor alpha protein level and its transrepression function

et al. 2004

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“…CK2 is known to phosphorylate a variety of transcription factors in vivo and in vitro so that their activities are either positively or negatively modulated. The phosphorylation by CK2 can affect transcription factors by changing the DNA-binding activity as it is observed for c-Jun 25 and Sp1, 26 by modulating their transcriptional activities such as for MyoD, 27 HIV-1, 22 or IRF-1, 28 and by affecting protein stability, as observed for IjBa, 29,30 PTEN 31 and connexin 45.6. 32 In this work, by using classical selective inhibitors of this kinase such as apigenin, [33][34][35][36] DRB (5,6-dichloro-1-b-D-ribofuranosylbenzimidazole) 22,37,38 and TBB (4,5,6,7-tetrabromobenzotriazole), [39][40][41] we investigated the effect of hypoxia on CK2 activity and the role that this kinase may play to regulate HIF-1 activity.…”

mentioning

confidence: 97%

“…CK2 has also been described to be overexpressed in cancer cells. 22 The human CK2 is composed of 2 catalytic subunits, a and a 0 , and 2 regulatory b subunits with molecular masses of 43, 38 and 28 kDa, respectively. The heterotetramer holoenzyme exists as a 2 b 2 , aa 0 b 2 , or a 0 2 b 2 tetramers.…”

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confidence: 99%

Role for casein kinase 2 in the regulation of HIF‐1 activity

Mottet

Ruys

Demazy

et al. 2005

Intl Journal of Cancer

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Hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor that plays a major role in cellular adaptation to hypoxia. The mechanisms regulating HIF-1 activity occurs at multiple levels in vivo. The HIF-1a subunit is highly sensible to oxygen and is rapidly degraded by the proteasome 26S in normoxia. Activation in hypoxia occurs through a multistep process including inhibition of HIF-1a degradation, but also increase in the transactivation activity of HIF-1. Several data indicate that phosphorylation could play a role in this regulation. In this report, we investigated the role of casein kinase 2 (CK2), an ubiquitous serine/ threonine kinase, in the regulation of HIF-1 activity. Hypoxia was capable of increasing the expression of the b subunit of CK2, of inducing a relocalization of this subunit at the plasma membrane, of inducing nuclear translocation of the a subunit and of increasing CK2 activity. Three inhibitors of this kinase, DRB (5,6-dichloro-1-b-D-ribofuranosyl-benzimidazole), TBB (4,5,6,7-tetrabromotriazole) and apigenin, as well as overexpression of a partial dominant negative mutant of CK2a, were shown to inhibit HIF-1 activity as measured by a reporter assay and through hypoxiainduced VEGF and aldolase expression. This does not occur at the stabilization process since they did not affect HIF-1a protein level. DNA-binding activity was also not inhibited. We conclude that CK2 is an important regulator of HIF-1 transcriptional activity but the mechanism of this regulation remains to be determined. Since HIF-1 plays a major role in tumor angiogenesis and since CK2 has been described to be overexpressed in tumor cells, this new pathway of regulation can be one more way for tumor cells to survive. ' 2005 Wiley-Liss, Inc.Key words: casein kinase 2; HIF-1; neoangiogenesis HIF-1 (hypoxia-inducible factor-1) is a key regulator of cell response to reduced oxygen level. In response to hypoxic conditions, HIF-1 increases the expression of downstream target genes such as erythropoietin (EPO), vascular endothelial growth factor (VEGF) and glycolytic enzymes (aldolase A, enolase-a) and mediates adaptation of cells to decreased oxygen level. 1 The role of HIF-1 in the regulation of tumor growth by hypoxia via the initiation of angiogenesis is certainly the best example of such an adaptive response. 2 Oncogene activation and tumor-suppressor inactivation result in deregulated cellular proliferation. However, most tumors grown larger than 1 mm 3 contain regions of low oxygen tension (hypoxia) due to an imbalance between oxygen supply and consumption. Formation of new blood vessels or ''neoangiogenesis'' is thus essential for further tumor growth. It is also important to allow tumor cell dissemination at distant sites, i.e., metastasis.Several studies using HIF-1 mutant cells have shown that HIF-1 has a profound effect on tumor biology. For example, tumors grown from HIF-1a-defective embryonic stem cells display abnormal vascularity and reduced growth rate. 3 Moreover, HIF-1 is upregulated in a broad r...

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“…Given this observation, the HL-60 and OM-10.1 cell lines have been used in several studies that simply aim at examining the levels of CD4, CXCR4, and CCR5 or other surface markers under various cellular physiological conditions and drug treatments [138,[144][145][146][147][148][149][150][151][152][153][154][155][156][157][158][159]. These cells have also been used to screen methodologies or drugs that may inhibit HIV-1 infection or reduce transcriptional activation of the virus [117,[160][161][162][163][164][165][166][167][168][169][170][171][172][173]. These cell lines have also been used in studies of drug toxicity, permeability, and/or effects on cellular activation and differentiation to gain an understanding of what specific drugs might do to cells in the bone marrow [144,154,[174][175][176][177][178][179][180][181][182]…”

Section: Hl-60mentioning

confidence: 99%

Myelomonocytic Cell Lines in Modeling HIV-1 Infection of the Bone Marrow

Nonnemacher¹,

Quiterio²,

Allen³

et al. 2017

Biology of Myelomonocytic Cells

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Human immunodeficiency virus type 1 (HIV-1), the etiologic agent of acquired immunodeficiency syndrome (AIDS), primarily infects T cells and cells of the monocyte-macrophage lineage. This is due to the presence of the cell surface receptor CD4 and the coreceptors, CXCR4, and CCR5. While the T-cell has classically been the cell type associated with HIV-1 disease progression, cells of the monocyte-macrophage lineage have also been shown to play a major role in this viral pathologic process. Classically, this has involved monocytic cells in the peripheral blood and tissue macrophages, however, over the course of HIV disease, the promyelomonocytic cells of the bone marrow (BM) have also been shown to play a role in pathogenesis retroviral disease in that they play an integral role in the reseeding of the periphery and end-organ tissues. This has involved an initial infection of the bone marrow hematopoietic progenitor cells. Given this observation, over the years there have been a number of cell lines that have been developed and provided valuable insights into research questions surrounding HIV-1 infection of the monocyte-macrophage cell lineage. In this regard, we will examine the biological and immunological properties of these BM-derived cell lines with respect to their utility in exploring the pathogenesis of HIV-1 in humans.

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Casein kinase II is a selective target of HIV-1 transcriptional inhibitors

Cited by 122 publications

References 46 publications

Tumour necrosis factor and PI3-kinase control oestrogen receptor alpha protein level and its transrepression function

Tumour necrosis factor and PI3-kinase control oestrogen receptor alpha protein level and its transrepression function

Role for casein kinase 2 in the regulation of HIF‐1 activity

Myelomonocytic Cell Lines in Modeling HIV-1 Infection of the Bone Marrow

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