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BackgroundRecent experimental studies have revealed that n-3 fatty acids, such as eicosapentaenoic acid (EPA) regulate postprandial insulin secretion, and correct postprandial glucose and lipid abnormalities. However, the effects of 6-month EPA treatment on postprandial hyperglycemia and hyperlipidemia, insulin secretion, and concomitant endothelial dysfunction remain unknown in patients with impaired glucose metabolism (IGM) and coronary artery disease (CAD).Methods and resultsWe randomized 107 newly diagnosed IGM patients with CAD to receive either 1800 mg/day of EPA (EPA group, n = 53) or no EPA (n = 54). Cookie meal testing (carbohydrates: 75 g, fat: 28.5 g) and endothelial function testing using fasting-state flow-mediated dilatation (FMD) were performed before and after 6 months of treatment. The primary outcome of this study was changes in postprandial glycemic and triglyceridemic control and secondary outcomes were improvement of insulin secretion and endothelial dysfunction. After 6 months, the EPA group exhibited significant improvements in EPA/arachidonic acid, fasting triglyceride (TG), and high-density lipoprotein cholesterol (HDL-C). The EPA group also exhibited significant decreases in the incremental TG peak, area under the curve (AUC) for postprandial TG, incremental glucose peak, AUC for postprandial glucose, and improvements in glycometabolism categorization. No significant changes were observed for hemoglobin A1c and fasting plasma glucose levels. The EPA group exhibited a significant increase in AUC-immune reactive insulin/AUC-plasma glucose ratio (which indicates postprandial insulin secretory ability) and significant improvements in FMD. Multiple regression analysis revealed that decreases in the TG/HDL-C ratio and incremental TG peak were independent predictors of FMD improvement in the EPA group.ConclusionsEPA corrected postprandial hypertriglyceridemia, hyperglycemia and insulin secretion ability. This amelioration of several metabolic abnormalities was accompanied by recovery of concomitant endothelial dysfunction in newly diagnosed IGM patients with CAD.Clinical Trial Registration UMIN Registry number: UMIN000011265 (https://www.upload.umin.ac.jp/cgi-open-bin/ctr/ctr.cgi?function=brows&action=brows&type=summary&recptno=R000013200&language=E)Electronic supplementary materialThe online version of this article (doi:10.1186/s12933-016-0437-y) contains supplementary material, which is available to authorized users.

We report a (29)Si NMR study on the pressure-induced superconductivity (SC) in an antiferromagnetic (AFM) heavy-fermion compound CeIrSi(3) without inversion symmetry. In the SC state at P = 2.7-2.8 GPa, the temperature (T) dependence of the nuclear-spin lattice relaxation rate 1/T(1) below T(c) exhibits a T(3) behavior without any coherence peak just below T(c), revealing the presence of line nodes in the SC gap. In the normal state, 1/T(1) follows a square root T-like behavior, suggesting that the SC emerges under the non-Fermi-liquid state dominated by AFM spin fluctuations enhanced around a quantum critical point. The reason why the maximum T(c) in CeIrSi(3) is relatively high among the Ce-based heavy-fermion superconductors may be the existence of the strong AFM spin fluctuations. We discuss the comparison with the other Ce-based heavy-fermion superconductors.

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Two forms of DNA polymerase II (⑀) of Saccharomyces cerevisiae, Pol II* and Pol II, were purified to near homogeneity from yeast cells. Pol II* is a four-subunit complex containing a 256-kDa catalytic polypeptide, whereas Pol II consists solely of a 145-kDa polypeptide derived from the N-terminal half of the 256-kDa polypeptide of Pol II*. We show that Pol II* and Pol II are indistinguishable with respect to the processivity and rate of DNA-chain elongation. The equilibrium dissociation constants of the complexes of Pol II* and Pol II with the DNA template showed that the stability of these complexes is almost the same. However, when the rates of dissociation of the Pol II* and Pol II from the DNA template were measured using single-stranded DNA as a trap for the dissociated polymerase, Pol II* dissociated 75-fold faster than Pol II. Furthermore, the rate of dissociation of Pol II* from the DNA template became faster as the concentration of the single-stranded DNA was increased. These results indicate that the rapid dissociation of Pol II* from the DNA template is actively promoted by single-stranded DNA. The dissociation of Pol II from the DNA template was also shown to be promoted by single-stranded DNA, although at a much slower rate. These results suggest that the site for sensing single-stranded DNA resides within the 145-kDa Nterminal portion of the catalytic subunit and that the efficiency for sensing single-stranded DNA by this site is positively modulated by either the C-terminal half of the catalytic subunit and/or the other subunits.In Saccharomyces cerevisiae, DNA polymerase II (⑀), as well as DNA polymerases I (␣) and III (␦), are required for DNA replication (1, 2). Deletion of the POL2 gene, which codes for the catalytic subunit of DNA polymerase II, causes cell death with a terminal dumbbell morphology, the hallmark of a defect in DNA replication (3). Direct measurements of in vivo DNA synthesis in temperature-sensitive pol2 mutants revealed that chromosomal DNA replication ceases at the restricted temperature (4, 5). The observation that a pol2 mutant defective in 3Ј35Ј exonuclease activity exhibits a mutator phenotype at a variety of genetic markers throughout the genome supports the idea that participation of the polymerase in chromosomal DNA replication is not restricted to certain sites on the genome (6). Recent work by Aparicio et al. (7) revealed that DNA polymerase II is recruited to the origin at the time of initiation of DNA replication and proceeds along the DNA with the replication fork. This finding, together with others, strongly supports the idea that DNA polymerase II is a component of the replication apparatus and that it is responsible for DNA synthesis on either the leading or lagging strand. However, whereas DNA polymerase I is responsible for laying down RNA-DNA primers, specific roles for DNA polymerases II and III at the fork have not been determined (8, 9).DNA repair is another cellular process for which the function of DNA polymerase II might be required. Among the DNA po...