New Approach to the Aneurysm Originating in the Ascending Aorta, Eroding the Sternum and Extending to the Cervix

1988-03When operating on a false aneurysm arising in the ascending aorta, protruding over the sternum, and eroding the sternum, the problems are how to approach the aneurysm and how to preserve the myocardium and the brain safely. In the present case, the operation was performed for the first time, to the best of our knowledge, safely by flipping up the eroded upper half of the sternum with separated clavicles and ribs, under a femoro-femoro (F-F) bypass and isolated brain perfusion.departmental bulletin pape

シリーズ リンショウ シンリガク ケンキュウ ト トウケイガク 2 tケンテイ ノ ガンケンセイ tケンテイ オ ツカエル ジョウケン

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Conducting linear chains of sulphur inside carbon nanotubes

Despite extensive research for more than 200 years, the experimental isolation of monatomic sulphur chains, which are believed to exhibit a conducting character, has eluded scientists. Here we report the synthesis of a previously unobserved composite material of elemental sulphur, consisting of monatomic chains stabilized in the constraining volume of a carbon nanotube. This one-dimensional phase is confirmed by high-resolution transmission electron microscopy and synchrotron X-ray diffraction. Interestingly, these one-dimensional sulphur chains exhibit long domain sizes of up to 160 nm and high thermal stability (similar to 800 K). Synchrotron X-ray diffraction shows a sharp structural transition of the one-dimensional sulphur occurring at similar to 450-650 K. Our observations, and corresponding electronic structure and quantum transport calculations, indicate the conducting character of the one-dimensional sulphur chains under ambient pressure. This is in stark contrast to bulk sulphur that needs ultrahigh pressures exceeding similar to 90 GPa to become metallic.ArticleNATURE COMMUNICATIONS. 4:2162 (2013)journal articl

Mutations Disrupting Histone Methylation Have Different Effects on Replication Timing in <i>S. pombe</i> Centromere

<div><p>The fission yeast pericentromere comprises repetitive sequence elements packaged into heterchromatin marked by histone H3K9 methylation and Swi6 binding. Transient disruption of Swi6 during S phase allows a period of RNA synthesis which programs the RNAi machinery to maintain histone methylation. However, Swi6 is also required for early replication timing. We show that not only Swi6 but also the chromodomain protein Chp1 are delocalized during S phase. Different from loss of <i>swi6</i>, mutations that disrupt histone methylation in the centromere, <i>chp1</i>Δ and <i>clr4</i>Δ, undergo early DNA replication. However, timing is modestly delayed in RNAi mutants <i>dcr1</i>Δ or <i>rdp1</i>Δ, while <i>hrr1</i>Δ mutants resemble <i>swi6</i>Δ in their replication delay. Finally, we show that recruitment of RNA polymerase II in the centromere occurs independently of replication. These different effects indicate that replication timing is not simply linked to histone methylation.</p></div

Centromere replication is delayed in RNAi mutants.

<p>A, schematic showing the experimental procedure. Cells were arrested in G1 by nitrogen depletion and released into the cell cycle by refeeding. BrdU and HU were added at 1.5 hours after release. B-D, BrdU ChIP in different mutants at the early origin <i>ars2004</i> (B), and the centromere repeats <i>dg</i> (C), and <i>dh</i> (D). BrdU enrichment was calculated by the ratio of IP versus Input by semi-quantitative PCR and at least two independent experiments were performed. Each mutant compared to its 0 timepoint. Asterisks mark samples with BrdU signal significantly higher than the WT at 6 h timepoint with p<0.05 (Student's T test). Primers: #1041/1042(dg), #1033/1034 (dh), and #1257/1258 (ars2004).</p

The centromere replicates early in <i>clr4</i>Δ or <i>chp1</i>Δ mutants.

<p>A, the structure of the three <i>S. pombe</i> centromeres. Repetitive sequences <i>dg</i> and <i>dh</i> in the outer repeats (<i>otr</i>) are present in slightly different organization in each centromere <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0061464#pone.0061464-Tran1" target="_blank">[66]</a>. The length of <i>dg</i> or <i>dh</i> is around 4-6 kb. B, scheme of the experimental protocol. <i>cdc25-22</i> mutants were shifted to 36°C for 4 hours. One hour prior to release to 25°C, 10 mM of HU was added so that only early origins fire. Upon release, 100 µg/ml BrdU was added to label new DNA synthesis. C, incorporation of BrdU in the <i>dg</i> region was detected by BrdU enrichment, which was calculated by the ratio of IP versus Input by semi-quantitative PCR using primers #1536/1537 (dg). Three independent experiments were performed. Asterisks mark samples with BrdU signal significantly higher than the WT at 90 min with p<0.05 (Student's T test). The quality of synchronization is determined by flow cytomertry. There is no significant different among WT, <i>chp1</i>Δ and <i>clr4</i>Δ (Figure S1A).</p

Swi6 and Chp1 each delocalize from the centromere between M and S phase.

<p>Asynchronously growing cells containing CFP-Cnp1 Sad1-DsRed (FY4229), GFP-Swi6 Sad1-DsRed (FY3665), or Chp1-GFP Sad1-DsRed (FY5911) were imaged every three minutes and the images were projected as described in materials and methods. A, quantitation of the data. The first frame in which spindle pole body duplication was observed was assigned as “0”. The first frame in which re-association of the GFP marked protein with the SPB occurred, and was maintained for at least three frames, was recorded. The re-association timing of CFP-Cnp1 (green), GFP-Swi6 (purple), or Chp1-GFP (black) with Sad1-DsRed is summarized in this distribution. Y axis, number of cells; X axis, time (minutes) after duplication of Sad1-DsRed, which is used to mark the beginning of M phase. Representative frames of GFP-Swi6, or Chp1-GFP are provided here B-C, respectively; selected original movies are provided in Movies S1, S2, S3. Arrows show cells with delocalization of the GFP signal from the SPB.</p

Replication timing and polymerases recruitment in wild type and <i>swi6</i>Δ.

<p>Cells were synchronized by <i>cdc25-22</i> block and release. Two independent experiments were performed and the representative result is presented. The signals were determined by quantitative real-time PCR. A, position of PCR probes used in this experiment. B–C, recruitment of DNA polymerase alpha (blue line), RNA polymerase II (green line) and incorporation of BrdU (red line) in euchromatin and the centromere, respectively. Left Y axis, DNA polymerase alpha or RNA polymerase II enrichment; right Y axis, BrdU enrichment. Red arrow, early replication time-point; blue arrow, late replication time-point. Primers: #1257/1258 (ars2004), #1265/1266 (non-ars), #875/876 (AT2080), #1628/1629 (dg), #1183/1184 (dh), and #879/880 (cnt2).</p

FOXO3a decreases expression of ER-regulated genes and increases CDK inhibitors in MCF7-FO breast tumors

At 35 days after tumor cell implantation, breast tumors derived from female athymic mice bearing MCF7-FO or MCF7-C (control) tumors were resected, fixed, sectioned, and placed on slides. Five independent tumors (each from a different mouse) were tested in each mouse group. Tumor specimens were subjected to immunohistochemical (IHC) staining with antibodies specific to forkhead box class O (FOXO)3a, hemagglutinin (HA)-tag, pS2, complement C3, cathepsin (Cath)-D, progesterone receptor (PgR), and cyclin D. Slides were examined at 40× magnification with a microscope. Numbers of positively staining cells in four random fields were counted in each tumor section, and representative fields are shown. Scale bars indicate 50 μm. *< 0.01 between control MCF7-C group versus MCF7-FO group. At 35 days after tumor cell implantation, breast tumors derived from female athymic mice bearing MCF7-FO or MCF7-C (control) tumors were resected, fixed, sectioned, and placed on slides. Five independent tumors (each from a different mouse) were tested in each mouse group. Tumor specimens were subjected to IHC staining with antibodies to p21Cip1, p27Kip1, p57Kip2, estrogen receptor (ER)-α, and ER-β. Numbers of positively staining cells in four random fields were counted in each tumor section, and representative fields are shown. Scale bars indicate 50 μm. *< 0.02 between control MCF7-C group versus MCF7-FO group. Confirmation that FOXO3a enhances expression of cyclin-dependent kinase (CDK) inhibitors and reduces expression of cyclin Din tumors in immunoblotting (IB) analysis. Whole lysates of MCF7-FO or MCF7-C breast tumor specimens were subjected to IB analysis with antibodies to p21Cip1, p27Kip1, p57Kip2, cyclin D, ER-α, ER-β, HA-tag and FOXO3a (positive controls), and β-actin (loading control).<p><b>Copyright information:</b></p><p>Taken from "Forkhead box transcription factor FOXO3a suppresses estrogen-dependent breast cancer cell proliferation and tumorigenesis"</p><p>http://breast-cancer-research.com/content/10/1/R21</p><p>Breast Cancer Research : BCR 2008;10(1):R21-R21.</p><p>Published online 29 Feb 2008</p><p>PMCID:PMC2374977.</p><p></p

Ectopic expression of FOXO3a in estrogen-dependent breast cancer cells suppresses breast tumor development

Forkhead box class O (FOXO)3a suppresses estrogen receptor (ER)-positive breast tumor development in a mouse model of breast cancer. The MCF7-FO pooled cell lines and the control MCF7-C pooled cell lines were injected (2 × 10cells/mouse) into the mammary fat pads of female athymic mice given supplementary 17β-estradiol (E2), as described in Materials and methods. Growth curves of tumor size are the means of the MCF7-FO pooled cell lines (designated MCF7-FO) and the control MCF7-C pooled cell lines (designated MCF7-C); error bars indicate standard deviation from three experiments. *< 0.05 between control MCF7-C group versus MCF7-FO group.<p><b>Copyright information:</b></p><p>Taken from "Forkhead box transcription factor FOXO3a suppresses estrogen-dependent breast cancer cell proliferation and tumorigenesis"</p><p>http://breast-cancer-research.com/content/10/1/R21</p><p>Breast Cancer Research : BCR 2008;10(1):R21-R21.</p><p>Published online 29 Feb 2008</p><p>PMCID:PMC2374977.</p><p></p