Health-Related Quality-of-Life after Percutaneous Coronary Intervention in Patients with UA/NSTEMI and STEMI: the Korean Multicenter Registry

Compared with ST elevation myocardial infarction (STEMI), long-term outcomes are known to be worse in patients with unstable angina/non-STEMI (UA/NSTEMI), which might be related to the worse health status of patients with UA/STEMI. In patients with UA/NSTEMI and STEMI underwent percutaneous coronary intervention (PCI), angina-specific and general health-related quality-of-life (HRQOL) was investigated at baseline and at 30 days after PCI. Patients with UA/NSTEMI were older and had higher frequencies in female, diabetes and hypertension. After PCI, both angina-specific and general HRQOL scores were improved, but improvement was much more frequent in angina-related HRQOL of patients with UA/NSTEMI than those with STEMI (44.2% vs 36.8%, P < 0.001). Improvement was less common in general HRQOL. At 30-days after PCI, angina-specific HRQOL of the patients with UA/NSTEMI was comparable to those with STEMI (56.1 ± 18.6 vs 56.6 ± 18.7, P = 0.521), but general HRQOL was significantly lower (0.86 ± 0.21 vs 0.89 ± 0.17, P = 0.001) after adjusting baseline characteristics (P < 0.001). In conclusion, the general health status of those with UA/NSTEMI was not good even after optimal PCI. In addition to angina-specific therapy, comprehensive supportive care would be needed to improve the general health status of acute coronary syndrome survivors.     

Comparison of Complications between Endoscopic and Percutaneous Replacement of Percutaneous Endoscopic Gastrostomy Tubes

When replacing percutaneous endoscopic gastrostomy (PEG) tubes, an internal bolster may be retrieved either percutaneously or endoscopically. The aim of this study was to compare the complications of percutaneous and endoscopic method during PEG tube replacement. The medical records of 330 patients who received PEG tube replacement were retrospectively analyzed. According to the removal method of internal bolster, we categorized as endoscopic group and percutaneous group. Demographic data, procedure-related complications and risk factors were investigated. There were 176 cases (53.3%) in endoscopic group and 154 cases (46.7%) in percutaneous group. The overall immediate complication rate during PEG tube replacement was 4.8%. Bleeding from the stoma (1.3%) occurred in percutaneous group, whereas esophageal mucosal laceration (7.4%) and microperforation (0.6%) occurred in endoscopic group. The immediate complication rate was significantly lower in the percutaneous method (OR, 6.57; 95% CI, 1.47-29.38, P=0.014). In multivariate analysis, old age was a significant risk factor of esophageal laceration and microperforation during PEG tube replacement (OR, 3.83; 95% CI, 1.04-14.07, P=0.043). The percutaneous method may be more safe and feasible for replacing PEG tubes than the endoscopic method in old patients.     

Influence of Body Mass Index,Smoking, and Blood Pressure on Survival of Patients with Surgically-Treated,Low Stage Renal Cell Carcinoma: A 14-Year Retrospective Cohort Study

The association of body mass index, smoking, and blood pressure, which are related to the three well-established risk factors of renal cell carcinoma, and survival in patients with renal cell carcinoma is not much studied. Our objective was to evaluate this association. A cohort of 1,036 patients with low stage (pT1 and pT2) renal cell carcinoma who underwent radical or partial nephrectomy were enrolled. We retrospectively reviewed medical records and collected survival data. The body mass index, smoking status, and blood pressure at the time of surgery were recorded. Patients were grouped according to their obesity grade, smoking status, and hypertension stage. Survival analysis showed a significant decrease in overall (P = 0.001) and cancer-specific survival (P < 0.001) with being underweight, with no differences of smoking status or perioperative blood pressure. On multivariate analysis, perioperative blood pressure ≥ 160/100 mmHg (HR, 2.642; 95% CI, 1.221-5.720) and being underweight (HR, 4.320; 95% CI, 1.557-11.984) were independent predictors of overall and cancer-specific mortality, respectively. Therefore, it is concluded that being underweight and perioperative blood pressure ≥ 160/100 mmHg negatively affect cancer-specific and overall survival, respectively, while smoking status does not influence survivals in patients with renal cell carcinoma.     

Frequent DNA methylation of MiR‐129‐2 and its potential clinical implication in hepatocellular carcinoma

Hepatocellular carcinoma (HCC) is a highly malignant tumor with poor prognosis and high mortality due to a lack of effective medical treatment and apparent early stage symptoms. Understanding molecular mechanism of cancer development is crucial for HCC diagnosis, prognosis, and treatment. Recently, microRNAs have been shown to play an important role in carcinogenesis, being regulated by DNA methylation in several cases. In this study, a whole genome approach was used to identify methylation‐regulated miRNAs in HCC, finally focusing on miR‐129‐2. MiR‐129‐2 methylation and reduced expression were observed in all examined HCC cell lines but not in normal liver cells and tissues. In 39 (93%) of 42 HCC, the methylation levels of miR‐129‐2 were significantly increased in tumor tissues compared with adjacent normal tissues. Furthermore, miR‐129‐2 methylation was detectable in plasma samples from HCC patients, but not in plasma samples from healthy individuals or patients with liver cirrhosis. At a cut‐off value of ?2.36 (log2 transformation of methylation level), it was possible to distinguish HCC from healthy and cirrhotic controls with sensitivity and specificity of 88% and 100%, respectively. This study indicates that miR‐129‐2 methylation is highly accurate in distinguishing HCC patients from cirrhosis patients and healthy individuals, implying its potential utility as an early diagnostic marker for HCC. © 2013 Wiley Periodicals, Inc.     

Periodontal disease and risk of mortality and kidney function decline in advanced chronic kidney disease: a nationwide population-based cohort study

Clinical Oral Investigations - Periodontal disease is prevalent in patients with chronic kidney disease (CKD) and potentially associated with kidney function decline. However, it is uncertain...     

Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast

The definition of protein–protein interactions (PPIs) in the natural cellular context is essential for properly understanding various biological processes. So far, however, most large-scale PPI analyses have not been performed in the natural cellular context. Here, we describe the construction of a Saccharomyces cerevisiae fusion library in which each endogenous gene is C-terminally tagged with the N-terminal fragment of Venus (VN) for a genome-wide bimolecular fluorescence complementation assay, a powerful technique for identifying PPIs in living cells. We illustrate the utility of the VN fusion library by systematically analyzing the interactome of the small ubiquitin-related modifier (SUMO) and provide previously unavailable information on the subcellular localization, types, and protease dependence of SUMO interactions. Our data set is highly complementary to the existing data sets and represents a useful resource for expanding the understanding of the physiological roles of SUMO. In addition, the VN fusion library provides a useful research tool that makes it feasible to systematically analyze PPIs in the natural cellular context.Most biological processes are mediated by complicated networks of protein–protein interactions (PPIs). Thus, the identification of the occurrence and components of PPIs provides invaluable insights into the cellular functions of proteins. In addition to conventional coimmunoprecipitation techniques, several methods have been developed to study PPIs, including the yeast two-hybrid analysis (Fields and Song 1989), the split ubiquitin system (Johnsson and Varshavsky 1994), fluorescence resonance energy transfer (FRET) assays (Periasamy and Day 1999; Pollok and Heim 1999), tandem affinity purification (TAP) followed by mass spectrometry (MS) analysis (Rigaut et al. 1999), and protein fragment complementation (PFC) assays (Remy and Michnick 1999; Ghosh et al. 2000; Wehrman et al. 2002; Paulmurugan and Gambhir 2003). Recently, the bimolecular fluorescence complementation (BiFC) assay, a specialized form of the PFC assay that uses fluorescent proteins as a reporter, has been developed (Hu et al. 2002). The BiFC assay is based on the formation of a fluorescent complex when two proteins fused to nonfluorescent fragments of a fluorescent protein interact with each other. This approach enables direct visualization of the occurrence and subcellular localization of PPIs with simple equipment.The budding yeast Saccharomyces cerevisiae has been a valuable eukaryotic model system, not only for traditional molecular and cell biology but also for the fields of functional genomics and proteomics. In S. cerevisiae, several large-scale analyses of PPIs have been performed with the yeast two-hybrid method (Uetz et al. 2000; Ito et al. 2001) or TAP-MS analysis (Gavin et al. 2002, 2006; Ho et al. 2002; Krogan et al. 2006). However, these approaches do not measure PPI in the natural cellular context; the yeast two-hybrid method is not appropriate for analyzing the interactions between proteins that cannot be transported to the nucleus or that form interactions only in the presence of other stabilizing interactions, and TAP-MS analysis is not amenable to studying protein complexes that are weakly or transiently formed or that do not survive in vitro purification. Compared with the yeast two-hybrid method and TAP-MS analysis, the FRET, PFC, and BiFC assays have several advantages in that they can detect the interactions between proteins in their natural cellular environment. Recently, a large-scale PPI screen using the PFC assay based on reconstituted dihydrofolate reductase (DHFR) activity has been reported (Tarassov et al. 2008), which is the first example of genome-wide PPI analysis using the PFC assay. However, because positive PPIs are selected by methotrexate resistance in the DHFR PFC assay, it is possible that the addition of methotrexate to the assay medium may perturb cellular physiology and proper PPI networks. In this regard, large-scale PPI screens using the BiFC or FRET assay that do not require any exogenous reagents would provide more accurate information about the structural organization of PPI networks in cells. To date, however, there is no report describing the application of the BiFC or FRET assay to genome-wide PPI analyses, particularly using proteins expressed from their own native promoters.The small ubiquitin-related modifier (SUMO) proteins are ∼10 kDa in size and comprise a family of evolutionarily conserved polypeptides that are post-translationally attached to the lysine residues of target proteins to regulate their subcellular localization, stability, and activity (Kerscher et al. 2006; Geiss-Friedlander and Melchior 2007). SUMO conjugation plays a variety of important roles in diverse eukaryotic cellular processes. SUMO can also mediate the non-covalent interaction of substrate proteins with proteins containing SUMO-interacting motifs and modulate their function (Song et al. 2004). In this regard, the identification of SUMO target proteins is crucial for the elucidation of the function of SUMO. Recent genome-wide PPI screens have identified over 500 putative SUMO conjugates in S. cerevisiae (Panse et al. 2004; Wohlschlegel et al. 2004; Zhou et al. 2004; Denison et al. 2005; Hannich et al. 2005; Wykoff and O''Shea 2005). More recently, an elegant study integrating the information of PPIs and genetic interactions has been conducted and has uncovered novel functional relationships between the SUMO pathway and various biological processes (Makhnevych et al. 2009). These systematic analyses have expanded the pool of SUMO substrates and the understanding of the biological function of sumoylation. However, because SUMO substrates can undergo rapid cycles of modification and demodification, and most target proteins appear to be modified to a small percentage at steady state (Geiss-Friedlander and Melchior 2007), it is likely that many unknown SUMO substrates remain to be discovered. Moreover, previous systematic PPI screens to identify SUMO substrates have primarily been performed with the yeast two-hybrid method and TAP-MS, which do not measure PPIs in the natural cellular context. The low agreement between the data from previous systematic screens demonstrates the limitation of the experimental methods used in those analyses and indicates that no single screen has been comprehensive. For this reason, different systematic approaches, with methods that can detect the interactions between proteins in their natural cellular environment, would greatly contribute to the identification of novel SUMO substrates and thus to the understanding of the function of the SUMO pathway.In the present study, we generated a collection of yeast strains expressing full-length proteins tagged with the N-terminal fragment of Venus (VN), a yellow fluorescent protein variant, from their own native promoters. Through a systematic analysis with the VN fusion library, we identified the interactome of SUMO, comprising 367 proteins, and also obtained previously unavailable information on the subcellular localization, types, and protease dependence of SUMO interactions in living yeast cells. Our data not only highlight a novel relationship between sumoylation and various biological processes but also represent a valuable resource that can be used to study the functional roles of the SUMO pathway. This is the first report that describes the application of the BiFC assay to a genome-wide PPI analysis using proteins expressed from their own native promoters. As demonstrated here, the VN fusion library provides a useful research tool that makes it feasible to systematically analyze PPIs in the natural cellular context.     

Highly crystalline nickel hexacyanoferrate as a long-life cathode material for sodium-ion batteries

Prussian blue analogs (PBAs) are attractive cathode candidates for high energy density, including long life-cycle rechargeable batteries, due to their non-toxicity, facile synthesis techniques and low cost. Nevertheless, traditionally synthesized PBAs tend to have a flawed crystal structure with a large amount of [Fe(CN)₆]⁴⁻ openings and the presence of crystal water in the framework; therefore the specific capacity achieved has continuously been low with poor cycling stability. Herein, we demonstrate low-defect and sodium-enriched nickel hexacyanoferrate nanocrystals synthesized by a facile low-speed co-precipitation technique assisted by a chelating agent to overcome these problems. As a consequence, the prepared high-quality nickel hexacyanoferrate (HQ-NiHCF) exhibited a high specific capacity of 80 mA h g⁻¹ at 15 mA g⁻¹ (with a theoretical capacity of ∼85 mA h g⁻¹), maintaining a notable cycling stability (78 mA h g⁻¹ at 170 mA g⁻¹ current density) without noticeable fading in capacity retention after 1200 cycles. This low-speed synthesis strategy for PBA-based electrode materials could be also extended to other energy storage materials to fabricate high-performance rechargeable batteries.

A low-speed synthesis strategy was designed to fabricate Prussian blue analog based electrode materials for high-performance rechargeable batteries.