PHOSPHORUS RECOVERY FROM SEWAGE-SLUDGE MOLTEN SLAG USING A COMBINATION OF ACID-DISSOLUTION, ALKALI-PRECIPITATION, AND ION-EXCHANGE

We recently reported an efficient procedure for recovering phosphoric acid from dephosphorization slag. This recovery procedure consists of a combination of the following four processes: (1) A first dissolution process of slag in a nitric acid solution; (2) a precipitation process then adds ammonia to the obtained eluate; (3) a second dissolution process dissolves the precipitation from the nitric acid eluate; and, (4) the final process involves ion exchange in which the obtained eluate is passed through an ion exchange resin. In the present study, this recovery procedure was applied to concentrate and recover phosphorus from sewage-sludge molten slag, which is an unused resource that should be considered a new resource for phosphorus. As a result, our procedure for recovery from dephosphorization slag was viable following two revisions. Initially, the time for the first dissolution process was extended from 0.2 h to 1 h, but 0.2 h proved to be the optimum time for dephosphorization slag. Next, we discovered it was better to perform the filtration one day after adding the ammonia instead of immediately after adding it. The other two processes could be treated under substantially the same conditions as in the case of dephosphorization slag, and high-purity phosphorus was obtained

Calcineurin-mediated dephosphorylation enhances the stability and transactivation of c-Myc

Abstract c-Myc, a transcription factor, induces cell proliferation and is often aberrantly or highly expressed in cancers. However, molecular mechanisms underlying this aberrantly high expression remain unclear. Here, we found that intracellular Ca2+ concentration regulates c-Myc oncoprotein stability. We identified that calcineurin, a Ca2+-dependent protein phosphatase, is a positive regulator of c-Myc expression. Calcineurin depletion suppresses c-Myc targeted gene expression and c-Myc degradation. Calcineurin directly dephosphorylates Thr58 and Ser62 in c-Myc, which inhibit binding to the ubiquitin ligase Fbxw7. Mutations within the autoinhibitory domain of calcineurin, most frequently observed in cancer, may increase phosphatase activity, increasing c-Myc transcriptional activity in turn. Notably, calcineurin inhibition with FK506 decreased c-Myc expression with enhanced Thr58 and Ser62 phosphorylation in a mouse xenograft model. Thus, calcineurin can stabilize c-Myc, promoting tumor progression. Therefore, we propose that Ca2+ signaling dysfunction affects cancer-cell proliferation via increased c-Myc stability and that calcineurin inhibition could be a new therapeutic target of c-Myc-overexpressing cancers

The Rice Annotation Project Database (RAP-DB): 2008 update

The Rice Annotation Project Database (RAP-DB) was created to provide the genome sequence assembly of the International Rice Genome Sequencing Project (IRGSP), manually curated annotation of the sequence, and other genomics information that could be useful for comprehensive understanding of the rice biology. Since the last publication of the RAP-DB, the IRGSP genome has been revised and reassembled. In addition, a large number of rice-expressed sequence tags have been released, and functional genomics resources have been produced worldwide. Thus, we have thoroughly updated our genome annotation by manual curation of all the functional descriptions of rice genes. The latest version of the RAP-DB contains a variety of annotation data as follows: clone positions, structures and functions of 31 439 genes validated by cDNAs, RNA genes detected by massively parallel signature sequencing (MPSS) technology and sequence similarity, flanking sequences of mutant lines, transposable elements, etc. Other annotation data such as Gnomon can be displayed along with those of RAP for comparison. We have also developed a new keyword search system to allow the user to access useful information. The RAP-DB is available at: http://www.w3.org/1999/ http://rapdb.dna.affrc.go.jp/ and http://rapdb.lab.nig.ac.jp/.</p