Oct-1 [corrected] and Oct-2 DNA-binding site specificity is regulated in vitro by different kinases

Grenfell, S. J.; Latchman, David S.; Thomas, Nancy

doi:10.1042/bj3150889

Cited by 28 publications

(25 citation statements)

References 41 publications

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“…Gene expression profiling of t(14;18) lymphoma cells has not revealed increased expression of Oct or Bob-1 mRNA, so it is likely that the augmented expression of these factors does not occur at the transcriptional level (Husson et al, 2002;Robetorye et al, 2002). Both Oct-2 and Bob-1 are Oct-2 regulates Bcl-2 expression CA Heckman et al post-translationally modified, and this may contribute to their stability and activity in t(14;18) lymphoma cells (Tanaka and Herr, 1990;Grenfell et al, 1996;Inamoto et al, 1997;Zwilling et al, 1997). In addition, there are a number of Oct-2 isoforms that result from alternative splicing, which may also lead to more stable Oct-2 expression (Wirth et al, 1991;Annweiler et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Oct transcription factors mediate t(14;18) lymphoma cell survival by directly regulating bcl-2 expression

et al. 2005

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Section: Discussionmentioning

confidence: 99%

Oct transcription factors mediate t(14;18) lymphoma cell survival by directly regulating bcl-2 expression

et al. 2005

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“…Interestingly, the Oct-1 protein can be phosphorylated by DNA-dependent protein kinase (41,53), which also phosphorylates IRF-3 (23). Notably, its phosphorylation can regulate its DNA binding activity (13,43). Furthermore, Oct-1 is postranslationally modified and its DNA binding activity is regulated during herpes simplex virus 1 infection (1).…”

Section: 59mentioning

confidence: 99%

“…Oct-1 is phosphorylated by different kinases in vitro (13,19) or in a cell cycle-dependent manner (38,43). On the other hand, Oct-1 phosphorylation is induced by stress stimuli and DNA damage (41).…”

Section: 59mentioning

confidence: 99%

The POU Transcription Factor Oct-1 Represses Virus-Induced Interferon A Gene Expression

Mésplède¹,

Island²,

Christeff³

et al. 2005

Molecular and Cellular Biology

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Alpha interferon (IFN-␣Alpha interferon (IFN-␣) and IFN-␤ are able to interfere with viral infection. They exert a vast array of biologic functions, including growth arrest, cell differentiation, and immune system regulation (for reviews, see references 28 and 51). This regulation extends from innate immunity to cellular and humoral adaptive immune responses. A strict control of expression is needed to prevent detrimental effects of unregulated IFN. IFN transcription is coordinately induced in human and mouse cells infected by virus. Multiple IFN-A subtypes exhibit differences in expression of their individual mRNAs.IFN-A transcription is regulated by a number of different activators and repressors. Among these factors, the interferon regulatory factors (IRFs) play an important role in the stimulation of cellular antiviral defense mechanisms in different cell types. IRFs regulate transcription by interacting with gene promoter sequences. Until now, repressors involved in negative regulation of the IFN-A genes have not been well characterized (for a review, see reference 29). We have shown that in addition to substitutions in proximal virus responsive element A (VRE-A) (2), the low expression levels of the IFN-A11 and IFN-A5 genes after virus induction are also due to the presence of a distal negative regulatory element (DNRE) of 20 bp, which is delimited upstream of VRE-A (20, 25, 26). The analysis of the DNRE responsible for the virus-induced transcription repression of some IFN-A promoters led us to study the homeodomain transcription factor Pitx1 (25). Upon virus induction, Pitx1 negatively regulates the transcription of DNREcontaining IFN-A11 and IFN-A5 promoters (20,25). We have recently shown that Pitx1 inhibits the IRF-3 and IRF-7 transcription activation of the IFN-A11 and IFN-A5 promoters and interacts physically with .Here we show that the POU protein Oct-1 binds in vitro to the DNRE and in vivo to the endogenous IFN-A11 promoter in mock-induced and induced cells. Furthermore, Oct-1 represses IFN-A11 expression upon IRF overexpression. Moreover, we show that Oct-1-deficient MEFs exhibit increased in vivo IFN-A gene expression and increased antiviral activity. Finally, the IFN-A expression pattern is modified in Oct-1-deficient MEFs. The broad representation of effective and potent octamer-like sequences within IFN-A promoters suggests an important role for Oct-1 in IFN-A regulation. We suggest this could have implications in IFN-␣-based combinatorial therapies. MATERIALS AND METHODSDNA transfection, viral induction, and transfection assays. Murine L929 cells were transfected by the standard calcium phosphate precipitation method as previously described (26). Newcastle disease virus (NDV) induction was carried out 24 h later. The mock-induced cells were set up as described above except that no NDV was added. Cells were harvested 24 h postinduction, and cytoplasm extracts were prepared. Luciferase activity was measured in cell lysates by using commercial reagents (Promega). Transfection efficiency was de...

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“…The binding site for Oct-1 has been identified and characterized at position 246 bp in the proximal human LPL promoter (32). Once phosphorylated on the homeodomain, its DNA binding activity could be inhibited in vivo and in vitro (33,34). Patients with a TYC substitution mutation in this region have low plasma LPL activity caused by an inability of Oct-1 binding (35).…”

Section: Discussionmentioning

confidence: 99%

Atorvastatin decreases lipoprotein lipase and endothelial lipase expression in human THP-1 macrophages

Qiu

Hill

2007

Journal of Lipid Research

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Macrophage-derived lipases are associated with atherosclerosis in human and animal studies. Despite numerous non-lipid-lowering effects of statins, their effect on macrophage LPL and endothelial lipase (EL) expression has not been investigated. In the present study, atorvastatin and simvastatin dose-dependently decreased LPL and EL expression as well as Rho, liver X receptor a (LXRa), and nuclear factor kB (NF-kB) activation in THP-1 macrophages. Atorvastatin-reduced LPL and EL expression was only partially recovered by mevalonate cotreatment, indicating that mechanisms independent of reductase inhibition may be present. By contrast, Rho activation by lysophosphatidyl acid further decreased LPL and EL expression in the presence or absence of atorvastatin. Another Rho activator, farnysyl pyrophosphate, decreased EL expression only in the absence of atorvastatin. LXRa activation by T0901317 and 22(R)-hydroxycholesterol not only rescued but also significantly increased LPL expression in the presence and absence of atorvastatin, respectively, whereas LXRa inhibition by 22(S)-hydroxycholesterol decreased LPL expression. By contrast, EL expression was suppressed by LXRa activation in the presence or absence of atorvastatin. NF-kB inhibition by SN50 was associated with an ?30% reduction of EL expression. Furthermore, atorvastatin treatment significantly attenuated the lipid accumulation in macrophages treated with oxidized LDL. We conclude that atorvastatin reduces LPL and EL expression by reducing the activation of LXRa and NF-kB, respectively.-Qiu, G. and J. S. Hill. Atorvastatin decreases lipoprotein lipase and endothelial lipase expression in human THP-1 macrophages. J. Lipid

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Oct-1 [corrected] and Oct-2 DNA-binding site specificity is regulated in vitro by different kinases

Cited by 28 publications

References 41 publications

Oct transcription factors mediate t(14;18) lymphoma cell survival by directly regulating bcl-2 expression

Oct transcription factors mediate t(14;18) lymphoma cell survival by directly regulating bcl-2 expression

The POU Transcription Factor Oct-1 Represses Virus-Induced Interferon A Gene Expression

Atorvastatin decreases lipoprotein lipase and endothelial lipase expression in human THP-1 macrophages

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