592 research outputs found
S-Nitrosylation in Organs of Mice Exposed to Low or High Doses of γ-Rays: The Modulating Effect of Iodine Contrast Agent at a Low Radiation Dose
The covalent addition of nitric oxide (NO•) onto cysteine thiols, or S-nitrosylation, modulates the activity of key signaling proteins. The dysregulation of normal S-nitrosylation contributes to degenerative conditions and to cancer. To gain insight into the biochemical changes induced by low-dose ionizing radiation, we determined global S-nitrosylation by the “biotin switch” assay coupled with mass spectrometry analyses in organs of C57BL/6J mice exposed to acute 0.1 Gy of cesium-137 γ-rays. The dose of radiation was delivered to the whole body in the presence or absence of iopamidol, an iodinated contrast agent used during radiological examinations. To investigate whether similar or distinct nitrosylation patterns are induced following high-dose irradiation, mice were exposed in parallel to acute 4 Gy of cesium-137 γ rays. Analysis of modulated S-nitrosothiols (SNO-proteins) in freshly-harvested organs of animals sacrificed 13 days after irradiation revealed radiation dose- and contrast agent-dependent changes. The major results were as follows: (i) iopamidol alone had significant effects on S-nitrosylation in brain, lung and liver; (ii) relative to the control, exposure to 0.1 Gy without iopamidol resulted in statistically-significant SNO changes in proteins that differ in molecular weight in liver, lung, brain and blood plasma; (iii) iopamidol enhanced the decrease in S-nitrosylation induced by 0.1 Gy in brain; (iv) whereas a decrease in S-nitrosylation occurred at 0.1 Gy for proteins of ~50 kDa in brain and for proteins of ~37 kDa in liver, an increase was detected at 4 Gy in both organs; (v) mass spectrometry analyses of nitrosylated proteins in brain revealed differential modulation of SNO proteins (e.g., sodium/potassium-transporting ATPase subunit beta-1; beta tubulins; ADP-ribosylation factor 5) by low- and high-dose irradiation; and (vi) ingenuity pathway analysis identified major signaling networks to be modulated, in particular the neuronal nitric oxide synthase signaling pathway was differentially modulated by low- and high-dose γ-irradiation.Peer reviewe
Transcriptome/proteome analysis of Corynebacterium glutamicum
Wendisch VF, Polen T. Transcriptome/proteome analysis of Corynebacterium glutamicum. In: Yukawa H, Inui M, eds. Corynebacterium glutamicum: Biology and Biotechnology. Microbiology Monographs. Vol 23. Heidelberg, Germany: Springer; 2013: 173-216
Metabolic engineering in Corynebacterium glutamicum
Wendisch VF, Lee J-H. Metabolic engineering in Corynebacterium glutamicum. In: Inui M, Toyoda K, eds. Corynebacterium glutamicum – Biology and Biotechnology. Microbiology Monographs. Vol 23. Cham: Springer Nature Switzerland; 2020: 287-322
Characterization of adipose tissue-derived stromal cells of mice with nonalcoholic fatty liver disease and their use for liver repair
博士論文 要旨Abstract/本文Full 以下に掲載:Regenerative Therapy 18 pp.497-507 2021. Elsevier. 共著者:Masaaki Yano,Alessandro Nasti,Akihiro Seki,Kosuke Ishida,Masatoshi Yamato,Hiiro Inui,Norihiko Ogawa,Shingo Inagaki,Tuyen Thuy Bich Ho,Kazunori Kawaguchi,Taro Yamashita,Kuniaki Arai,Tatsuya Yamashita,Eishiro Mizukoshi,Oto Inoue,Shinichiro Takashima,Soichiro Usui,Masayuki Takamura,Masao Honda,Takashi Wada,Shuichi Kaneko,Yoshio Saka
Characterization of adipose tissue-derived stromal cells of mice with nonalcoholic fatty liver disease and their use for liver repair
金沢大学博士(医学)博士論文 要旨Abstract/本文Full 以下に掲載:Regenerative Therapy 18 pp.497-507 2021. Elsevier. 共著者:Masaaki Yano, Alessandro Nasti, Akihiro Seki, Kosuke Ishida, Masatoshi Yamato, Hiiro Inui, Norihiko Ogawa, Shingo Inagaki, Tuyen Thuy Bich Ho, Kazunori Kawaguchi, Taro Yamashita, Kuniaki Arai, Tatsuya Yamashita, Eishiro Mizukoshi, Oto Inoue, Shinichiro Takashima, Soichiro Usui, Masayuki Takamura, Masao Honda, Takashi Wada, Shuichi Kaneko, Yoshio Sakaidoctoral thesi
Serum Helicobacter Pylori IgG Titers are Predictive of H. pylori Infection Status
The aim of the present study was to test the hypothesis that a novel serum Helicobacter Pylori IgG kit derived from Japanese H. pylori strains, namely the Sphere Light H. pylori IgG J kit (SL-HP J), would enable discrimination of H. pylori infection status. In total, 273 patients were enrolled in the study and underwent endoscopic examination at Inui Clinic of Internal Medicine. Serum H. pylori IgG titers were measured using the SL-HP J kit. Current H. pylori infection was defined as positivity in at least one H. pylori test (rapid urease test, urease breath test, monoclonal stool antigen test, or histology), excluding serology. Naïve H. pylori infection was defined as negativity in all H. pylori tests and chronic atrophic gastritis (CAG), as determined by endoscopy. Previous H. pylori infection was defined as negativity for all H. pylori tests despite the presence of CAG. After testing, 134 patients were deemed to be naïve to H. pylori infection, 83 patients were diagnosed with current H. pylori infection, and the remaining 56 patients were diagnosed with previous H. pylori infection. Median (±quartile deviation) titers in patients with naïve, previous, and current H. pylori infection were 0.8±0.4, 2.1±2.3, and 24.8±22.7U/ml, respectively. The receiver operating characteristic (ROC) curve for naïve and previous H. pylori infection to classify naïve H. pylori infection showed an area under the curve (AUC) of 0.910, with 83% sensitivity and 82% specificity for a cut-off level of <1.6U/ml; the ROC curve for previous and current H. pylori infection to classify current H. pylori infection had an AUC of 0.969, with 96% sensitivity and 88% specificity for a cut-off level of ≥3.3U/ml. The present study shows that serum H. pylori IgG titers may be used to determine H. pylori infection status.departmental bulletin pape
Trehalose acts as a uridine 5′-diphosphoglucose-competitive inhibitor of trehalose 6-phosphate synthase in<i>Corynebacterium glutamicum</i>
Global Transcriptional Regulators Involved in Carbon, Nitrogen, Phosphorus, and Sulfur Metabolisms in Corynebacterium glutamicum
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