On the relation between the mass of Compact Massive Objects and their host galaxies

Supermassive black holes and/or very dense stellar clusters are found in the central regions of galaxies. Nuclear star clusters are present mainly in faint galaxies while upermassive black holes are common in galaxies with masses $\geq 10^{10}$ M$_\odot$. In the intermediate galactic mass range both types of central massive objects (CMOs) are found. Here we present our collection of a huge set of nuclear star cluster and massive black hole data that enlarges significantly already existing data bases useful to investigate for correlations of their absolute magnitudes, velocity dispersions and masses with structural parameters of their host galaxies. In particular, we directed our attention to some differences between the correlations of nuclear star clusters and massive black holes as subsets of CMOs with hosting galaxies. In this context, the mass-velocity dispersion relation plays a relevant role because it seems the one that shows a clearer difference between the supermassive black holes and nuclear star clusters. The $M_{MBH}-{\sigma}$ has a slope of $5.19\pm 0.28$ while $M_{NSC}-{\sigma}$ has the much smaller slope of $1.84\pm 0.64$. The slopes of the CMO mass- host galaxy B magnitude of the two types of CMOs are indistinguishable within the errors while that of the NSC mass-host galaxy mass relation is significantly smaller than for supermassive black holes. Another important result is the clear depauperation of the NSC population in bright galaxy hosts, which reflects also in a clear flattening of the NSC mass vs host galaxy mass at high host masses.Comment: 12 pages, 22 figures, 2 tables, accepted for publication in MNRA

Overexpression of Aurora-A enhances the degradation of AP-2α.

<p>(A) KYSE150/GFP-Aurora-A and KYSE150/GFP cells were treated with CHX respectively, and then harvested at the indicated time points. AP-2α protein level at each time point was determined by Western Blot. (B) The amounts of AP-2α were calculated by densitometry and normalized to corresponding actin levels. The column diagram represents the amount of normalized AP-2α at each time point comparing with the original levels (0 h). (C) Aurora-A enhances the proteasome-dependent degradation of AP-2α. KYSE150/GFP-Aurora-A and KYSE150/GFP cells were treated with CHX alone or combination with MG-132. AP-2α protein level was determined by Western Blot.</p

Transcription activity of AP-2α is downregulated by Aurora-A.

<p>(A) The summary of the transcription factors with significant changes in their activities by transcription factors array when Aurora-A was overexpressed. (B) Fluorescence images of the transcription factors arrays hybridized with nuclear extracts from KYSE150/GFP-Aurora-A and KYSE150/GFP cells. The analysis of arrays was replicated twice, exchanging the Cy3- and Cy5- label. Magnified panels show the spots representing the activity of AP-2 transcription factor that was down-regulated upon Aurora-A overexpression. (C) The summary of the AP-2α-regulated genes with significant down-expression when Aurora-A was overexpressed by mRNA expression profiling array. The black bars represent the AP-2α-regulated genes, and the gray bars represent the genes which were not the AP-2α-regulated genes. (D) The nucleoprotein extraction of KYSE150/GFP-Aurora-A and KYSE150/GFP cells were incubated with AP-2α binding DNA double-stranded oligonucleotidic probe on multi-well plates, then anti-AP-2α antibodies and the peroxidase-conjugated anti-mouse IgG were subsequently added. At last, the samples could be read for the colorimetric detection. (E) KYSE150/GFP-Aurora-A and KYSE150/GFP cells were cotransfected with (AP-2)₃-TK-LUC expression vector and a pRL-SV40 expression vector. Transcription activities were expressed as luciferase values after normalization. All experiments were performed three times and described as mean ± SD.</p

Aurora-A-mediated AP-2α degradation depends on Aurora-A kinase activity.

<p>(A) KYSE150/GFP-Aurora-A cells were exposed to 1 µM of Aurora-A kinase inhibitor and cellular proteins were collected 2 hours later. Western Blot was performed with antibodies to pThr288 on Aurora-A or total Aurora-A. DMSO was used as a negative control. (B) KYSE150/GFP-Aurora-A cells were exposed to Aurora-A kinase inhibitor or DMSO for 2 hours prior to treatment with CHX. Cells were harvested at the indicated time points and analyzed by Western Blot. (C) The amounts of AP-2α were calculated by densitometry and normalized to corresponding actin levels. The column diagram represents the amount of normalized AP-2α at each time point comparing with the original levels (0 h).</p

Mussel-Inspired Synthesis of Polydopamine-Functionalized Graphene Hydrogel as Reusable Adsorbents for Water Purification

We present a one-step approach to polydopamine-modified graphene hydrogel, with dopamine serving as both reductant and surface functionalization agents. The synthetic method is based on the spontaneous polymerization of dopamine and the self-assembly of graphene nanosheets into porous hydrogel structures. Benefiting from the abundant functional groups of polydopamine and the high specific surface areas of graphene hydrogel with three-dimensional interconnected pores, the prepared material exhibits high adsorption capacities toward a wide spectrum of contaminants, including heavy metals, synthetic dyes, and aromatic pollutants. Importantly, the free-standing graphene hydrogel can be easily removed from water after adsorption process, and can be regenerated by altering the pH values of the solution for adsorbed heavy metals or using low-cost alcohols for synthetic dyes and aromatic molecules

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Electronic Supplementary Information from Colorimetric and fluorescent probes for real-time naked eye sensing of copper ion in solution and on paper substrate

The synthesis of intermediates and some measurement information

Determination of transcript levels of <i>PtrDFR1</i> and <i>PtrDFR2</i> in transgenic poplar plants by quantitative real-time PCR.

<p>The <i>PtrDFR1</i> expression was significantly increased in transgenic lines 4 and 12, whereas the <i>PtrDFR2</i> transcript level was higher in all three transgenic lines than in wild-type and pBI121 transgenic controls.</p

<i>PtrDFR1</i> and <i>PtrDFR2</i> transcript levels in different tissues of <i>P. trichocarpa</i>.

<p>(<b>A</b>) Gel analysis of semiquantitative reverse transcriptase (RT)-PCR with transcript-specific <i>DFR</i> primers. (<b>B</b>) Expression levels were determined by qRT-PCR. Values represent averages of three biological replicates, each with two technical replicates. <i>Actin</i> expression of poplar was used as a control. Total RNA was isolated from poplar tissues: root (R), shoot (S), young leaf (YL), old leaf (OL), young petiole (YP) and old petiole (OP).</p

Effect of <i>PtrDFR1</i> and <i>PtrDFR2 in vivo</i> on anthocyanin accumulation in transgenic tobacco flowers.

<p>(<b>A</b>) Overexpression of <i>PtrDFR1</i> resulted in a visible increase in anthocyanin accumulation in the corolla of transgenic tobacco flowers (lines 3 and 11), relative to untransformed lines (WT) and pBI121 transgenic control (pBI121) or the <i>35S:PtrDFR2</i> transgenics (5 and 9). (<b>B</b>) Quantitation of anthocyanin levels in transgenic tobacco flowers with a spectrophotometer. Error bars are SDs from three independent experiments. Both the lines harboring the <i>35S:PtrDFR1</i> gene had significantly higher anthocyanin levels compared with wild-type and the pBI121 transgenic control (based on a Student's <i>t</i> test analysis limit of <i>P</i>≤0.05). No lines overexpressing the <i>35S:PtrDFR2</i> gene showed significant increases in anthocyanins. (<b>C</b>) RT-PCR analysis of <i>PtrDFR1</i> and <i>PtrDFR2</i> expression in transgenic tobacco plants.</p