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A biofilm sequencing batch reactor with a volume of 1.42 m3, nylon nets providing a 4,140 m2/m3 support area for biofilms and an automated operation with 8 hour cycles was studied. The duration of the experiment was 135 days. Removal efficiencies e≧ 80% were obtained for carbonaceous matter, producing an effluent with 31±26.8 mg/L of filtered COD, 7±3.6 mg/L of BOD5 and 12±3.2 mg/L of TOC. The average removal efficiency of ammonium was 77 ± 16.6%, with a mean concentration in the effluent of 14 ± 10.2 mg NH4-N/L. The denitrification efficiency was 80±14.7%. The effluent characteristics met the requirements of Brazilian environmental standard for discharge to receiving water bodies. A kinetic study of nitrification and denitrification showed that during the aerobic phase the specific rate of ammonium consumption was 0.057 g NH4-N/g VSS.d and the production of NOx-N was 0.074 g NOx-N/g VSS.d, while the specific rate of NOx-N consumption was 0.05 g NOx-N/g VSS.d during the anoxic phase. The suspended and fixed biomass was composed of 50% ammonium-oxidizing bacteria (AOB). [ABSTRACT FROM AUTHOR]

The forkhead box m1 (Foxm1 or Foxm1b) protein (previously called HFH-11B, Trident, Win or MPP2) is abundantly expressed in human non-small cell lung cancers where it transcriptionally induces expression of genes essential for proliferation of tumor cells. In this study, we used Rosa26-Foxm1 transgenic mice, in which the Rosa26 promoter drives ubiquitous expression of Foxm1 transgene, to identify new signaling pathways regulated by Foxm1. Lung tumors were induced in Rosa26-Foxm1 mice using the 3-methylcholanthrene (MCA)/butylated hydroxytoluene (BHT) lung tumor initiation/promotion protocol. Tumors from MCA/BHT-treated Rosa26-Foxm1 mice displayed a significant increase in the number, size and DNA replication compared to wild-type mice. Elevated tumor formation in Rosa26-Foxm1 transgenic lungs was associated with persistent pulmonary inflammation, macrophage infiltration and increased expression of cyclooxygenase-2 (Cox-2), Cdc25C phosphatase, cyclin E2, chemokine ligands CXCL5, CXCL1 and CCL3, cathepsins and matrix metalloprotease-12. Cell culture experiments with A549 human lung adenocarcinoma cells demonstrated that depletion of Foxm1 by either short interfering RNA transfection or treatment with Foxm1-inhibiting ARF 26-44 peptide significantly reduced Cox-2 expression. In co-transfection experiments, Foxm1 protein-induced Cox-2 promoter activity and directly bound to the −2566/−2580 bp region of human Cox-2 promoter.Oncogene (2008) 27, 4137–4149; doi:10.1038/onc.2008.60; published online 17 March 2008 [ABSTRACT FROM AUTHOR]

The FoxM1 transcription factor plays critical roles in the expression of genes that are essential for cell proliferation. FoxM1 null or depleted cells fail to progress through mitosis, as expression of several mitotic genes depends upon FoxM1. The transcriptional activity of FoxM1 is stimulated by cyclin-cdk-mediated phosphorylation at a site within the transcriptional activation domain. Here, we characterize the role of an N-terminal inhibitory domain in the transcriptional activity of FoxM1. Deletion of the N-terminal 232 amino-acid residues increases the transcriptional and transforming activities of FoxM1. Moreover, while the activity of the full-length FoxM1 is stimulated by growth factors, the activity of the N-terminal deletion mutant is constitutively high in all phases of the cell cycle. The N-terminal deletion also eliminates the requirement for cyclin-cdk to activate FoxM1. We provide evidence that the N-terminal domain interacts with the C-terminal half of the transcription factor to attenuate its transcriptional activity. Moreover, the N-terminal fragment inhibits the transcriptional activity of FoxM1 in G1/S cells, but not in G2/M cells. Our results suggest that cyclin-cdk phosphorylates FoxM1 to counteract the inhibition by the N-terminal domain to fully activate FoxM1 in G2/M phase.Oncogene (2008) 27, 1696–1704; doi:10.1038/sj.onc.1210814; published online 24 September 2007 [ABSTRACT FROM AUTHOR]