Introduction: Helicobacter pylori (H. pylori) infection is positively associated with cardiovascular diseases, but the involvement of lipids in this association remains unclear. The present study reviewed the changes in circulating lipid levels following H. pylori eradication. Methods: A PubMed database was searched until December 2020 to identify randomized control trials (RCTs) and non-RCTs investigating the effect of H. pylori eradication on the lipid levels in inverse variance-weighted, random-effects meta-analyses. Results: A total of 24 studies (four RCTs and 20 non-RCTs) with 5270 participants were identified. The post-eradication levels were increased for high-density lipoprotein cholesterol (HDL-C; mean difference (MD) 2.28 mg/dL, 95% confidence interval (CI) 1.90 to 2.66) and triglyceride (TG; MD 3.22 mg/dL, 95% CI 1.13 to 5.31) compared with the pre-eradication levels. H. pylori eradication resulted in little to no difference in the low-density lipoprotein-cholesterol levels (MD −2.33 mg/dL, 95% CI −4.92 to 0.26). In the analyses of RCTs only, the findings for elevated HDL-C levels, but not TG, were robust. Conclusions: H. pylori eradication increases the HDL-C levels. Further studies are needed to elucidate the effects of lipid changes following H. pylori eradication on cardiovascular diseases.

Nucleic acid amplification-based diagnostics is known as one of the molecular diagnostic systems that allows higher sensitive detection of pathogens than test methods such as immunoassay. However, it has not been widely used because it is complicated to use and takes a long time to generate results. on the other hand, development of fully automated molecular diagnostic systems has been growing around the world as demand for such systems from physicians and laboratory technicians has increased. to meet this demand, we have developed the "Simprova" fully automated molecular diagnostic system, which takes advantage of LAMP (Loop-mediated Isothermal Amplification), a method eiken chemical co., Ltd. invented. Simprova comprises a master unit that controls the entire system and a test unit that extracts and purifies nucleic acid from samples (pretreatment), and uses the LAMp method to detect and amplify nucleic acid. Users can obtain test results automatically by simply installing a pretreatment cartridge, a multi-well testing chip and the sample in the test unit. The multi-well testing chip has 25 reaction wells connected by channels and enables simultaneous testing of multiple targets with one sample. Turnaround time for one test is approximately 30 minutes. Since a conventional extraction and purification method using magnetic-bead separation is used for the pretreatment, nucleic acid can be extracted from serum, plasma, whole blood, urine, and sputum, for example. In addition, the system can perform random-access testing by connecting four test units to the master unit to realize near-the-patient testing. Simprova is therefore a robust and useful system for a wide variety of applications.

PhoPop5 and PhoRpp30 in the hyperthermophilic archaeon Pyrococcus horikoshii, homologues of human ribonuclease P (RNase P) proteins hPop5 and Rpp30, respectively, fold into a heterotetramer [PhoRpp 30(PhoPop5) 2 PhoRpp30], which plays a crucial role in the activation of RNase P RNA (PhopRNA). Here, we examined the functional implication of PhoPop5 and PhoRpp30 in the tetramer. Surface plasmon resonance (SPR) analysis revealed that the tetramer strongly interacts with an oligonucleotide including the nucleotide sequence of a stem-loop SL3 in PhopRNA. In contrast, PhoPop5 had markedly reduced affinity to SL3, whereas PhoRpp30 had little affinity to SL3. SPR studies of PhoPop5 mutants further revealed that the C-terminal helix (a4) in PhoPop5 functions as a molecular recognition element for SL3. Moreover, gel filtration indicated that PhoRpp30 exists as a monomer, whereas PhoPop5 is an oligomer in solution, suggesting that PhoRpp30 assists PhoPop5 in attaining a functionally active conformation by shielding hydrophobic surfaces of PhoPop5. These results, together with available data, allow us to generate a structural and mechanistic model for the PhopRNA activation by PhoPop5 and PhoRpp30, in which the two Cterminal helices (a4) of PhoPop5 in the tetramer whose formation is assisted by PhoRpp30 act as binding elements and bridge SL3 and SL16 in PhopRNA.Keywords: archaea/proteinRNA interaction/ Pyrococcus horikoshii/ribonuclease P/surface plasmon resonance.Abbreviations: 3-D, three-dimensional; PhopRNA, ribonuclease P RNA from P. horikoshii; pre-tRNA, precursor tRNA; RNase P, ribonuclease P; RNP, ribonucleoprotein; RRM, RNA recognition motif; SL3, stem-loop containing P3 helix; SL16, stem-loop containing P16 helix; SPR, surface plasmon resonance.Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that catalyses the processing of 5 0 leader sequences from tRNA precursors (pre-tRNA) and other noncoding RNAs in all living cells (1, 2). In contrast to eubacterial RNase P RNAs, the RNA components in archaea and eukaryotes alone have little catalytic activity in vitro and function in cooperation with protein subunits in substrate recognition and catalysis (3). Hence, archaeal and eukaryotic RNase Ps may serve as a model ribonucleoprotein (RNP) for studying how a functional RNA can be activated by protein cofactors and how the RNP enzymes catalyse biological processes.We earlier found that RNase P RNA (PhopRNA) and five proteins in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 reconstituted RNase P activity that exhibits enzymatic properties like those of the authentic enzyme (4, 5). The P. horikoshii RNase P proteins were designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30 and PhoRpp38, according to their sequence homology with the human RNase P proteins hPop5, Rpp21, Rpp29, Rpp30 and Rpp38, respectively (6). Biochemical and structural studies revealed that PhoPop5 and PhoRpp21 form a complex with PhoRpp30 and PhoRpp29, and the resulting complexes, PhoPop5PhoRpp30 and Pho Rpp21PhoRpp29, are involved i...

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Measurement of the Electron Cyclotron Emission (ECE) spectrum is one of the most popular electron temperature diagnostics in nuclear fusion plasma research. A 2-dimensional ECE imaging system was developed with an adaptive-array approach. A radio-frequency (RF) heterodyne detection system with Software Defined Radio (SDR) devices and a phased-array receiver antenna was used to measure the phase and amplitude of the ECE wave. The SDR heterodyne system could continuously measure the phase and amplitude with sufficient accuracy and time resolution while the previous digitizer system could only acquire data at specific times. Robust streaming phase measurements for adaptive-arrayed continuous ECE diagnostics were demonstrated using Fast Fourier Transform (FFT) analysis with the SDR system. The emission field pattern was reconstructed using adaptive-array analysis. The reconstructed profiles were discussed using profiles calculated from coherent single-frequency radiation from the phase array antenna.