17 research outputs found

    High Ferritin Level and Malnutrition Predict High Risk of Infection-Related Hospitalization in Incident Dialysis Patients: A Japanese Prospective Cohort Study

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    Aims: The aim of the study was to clarify the relationship between serum ferritin and infectious risks. Methods: We evaluated all hospital admissions due to infections, clinical biomarkers and nutrition status in 129 incident Japanese dialysis patients during a median follow-up of 38 months. Results: Kaplan-Meier analysis revealed that the period without infections requiring hospitalization was significantly shorter in ferritin > median (82.0 ng/ml) group than in the ferritin < median group (log-rank test 4.44, p = 0.035). High ferritin was associated with significantly increased relative risk of hospitalization for infection (Cox hazard model 1.52, 95% CI 1.06-2.17). The number of hospitalization days was gradually longer in patients with high ferritin levels and malnutrition. Conclusion: Although serum ferritin levels were low, and doses of iron administered to dialysis patients in Japan are generally lower than in Western countries, an elevated ferritin level was associated with increased risk of infection, particularly in patients with poor nutritional status.journal articl

    ヒト組織と神経芽腫におけるGATA-2の発現に関する研究

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    Globin transcription factor 2 (GATA-2) は造血細胞, 神経細胞, 泌尿生殖器細胞, 血管内皮細胞などに発現する転写調節因子 GATA family の一員である. 本研究では新たに作成された抗ヒトGATA-2抗体を用いて免疫組織学的染色を行い, ヒト成人において骨髄の前赤芽球, 骨髄芽球, 末梢血の肥満細胞, 血管内皮, 腎遠位尿細管上皮にGATA-2の発現を認めた. ヒト胎児では血管内皮, 副腎, 腎臓, 肝内造血細胞, 中枢神経細胞にGATA-2の発現を認めた. 神経芽腫ではロゼット構造をなす円形細胞の核にGATA-2の発現が高く, 分化が進んだ細線維型細胞ではGATA-2の発現は低下する傾向が強いことから, GATA-2の発現は予後を予想する因子となる可能性が示唆された. また, 4種の神経芽腫細胞株 (SH-SY5Y, GOTO, IMR-32, NB-1) の蛍光染色では核にGATA-2の発現を認めたが, GATAS-2発現のもっとも強いSH-SY5Yはオールトランスレチノイン酸を用いた分化誘導によって, GATA-2の蛋白とmRNAの発現は変化せず, 神経芽腫における分化度とGATA-2の発現の関係を再現することはできなかった. 本抗体を用いた免疫染色は神経芽腫の診断及び神経細胞や血球の分化の解析に有用と思われる.departmental bulletin pape

    民法総則と婚姻・協議離婚・養子縁組

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    Articledepartmental bulletin pape

    Basal and stimulated expression of IL-6 mRNA and protein in human colon carcinoma cell clones

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    <p><b>Copyright information:</b></p><p>Taken from "Clone-specific expression, transcriptional regulation, and action of interleukin-6 in human colon carcinoma cells"</p><p>http://www.biomedcentral.com/1471-2407/8/13</p><p>BMC Cancer 2008;8():13-13.</p><p>Published online 18 Jan 2008</p><p>PMCID:PMC2257953.</p><p></p> Additions to the culture medium were: 10M indomethacin, 10M PGE, 10M 1,25-(OH)D, 10M 17β-E, 5 ng/ml IL-1β. Upper part: Representative RT-PCR amplifications of mRNA transcripts specific for (culture time 4 h). Expression of epithelial cell marker CK8 is shown for comparison. Lower part: IL-6 release into medium during 24 h culture period. Data are means ± SD, ≥ 4. Note that changes in IL-6 secretion by COGA-13 cells are given on a logarithmic scale. Statistically significant differences: *, < 0.05; **, < 0.01; ***, < 0.001 (Student's -test)

    Effect of 1,25-(OH)D(10M) on IL-6-related proliferation of confluent Caco-2/AQ cells

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    <p><b>Copyright information:</b></p><p>Taken from "Clone-specific expression, transcriptional regulation, and action of interleukin-6 in human colon carcinoma cells"</p><p>http://www.biomedcentral.com/1471-2407/8/13</p><p>BMC Cancer 2008;8():13-13.</p><p>Published online 18 Jan 2008</p><p>PMCID:PMC2257953.</p><p></p> Culture time was 72 h. Cell growth was assayed by [H]thymidine incorporation into cellular DNA (normalised to total protein). Data are expressed as means ± SD, = 4 – 7. Statistically significant differences from controls: *, < 0.05; **, < 0.01 (Student's -test)

    (A) Effect of hIL-6 on growth rate of confluent Caco-2/AQ, COGA-1A, and COGA-13 cells

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    <p><b>Copyright information:</b></p><p>Taken from "Clone-specific expression, transcriptional regulation, and action of interleukin-6 in human colon carcinoma cells"</p><p>http://www.biomedcentral.com/1471-2407/8/13</p><p>BMC Cancer 2008;8():13-13.</p><p>Published online 18 Jan 2008</p><p>PMCID:PMC2257953.</p><p></p> Cellular proliferation was evaluated from [H]thymidine incorporation into DNA after 72 h incubation with rhIL-6 (0–100 ng/ml). Data are means ± SD (= 4 – 16) and expressed as multiples of IL-6-free controls. Statistically significant differences from controls: **, < 0.01; ***, < 0.001 (Student's -test). (B) Time-course of mRNA expression in confluent Caco-2/AQ, COGA-1A, and COGA-13 clones during incubation with 100 ng/ml rhIL-6. Expression of the epithelial cell marker CK8 is shown for comparison. (C) Densitometric evaluation of expression of in relation to CK8 as shown in (B): basal expression ratios in zero time controls were set to 1

    FcεRI positive tissue reveals IgE binding activity.

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    <p>Immunofluorescence staining of serial sections from patient No. 8 revealed IgE binding in (A) FcεRI α-chain (red) positive epithelial cells being incubated with (B) monoclonal NiP-specific humanized IgE antibodies (green). (C) Negative control with PBS. The blue fluorescence DAPI staining indicates the nuclei. Original magnification ×40.</p

    Co-expression of FcεRI α- and γ-chain, but not FcεRI α- and β-chain is observed in epithelial cells of intestinal tissue.

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    <p>In sections from cancer patient No. 23 FcεRI γ-chain (green) is found to be co-expressed in FcεRIα (red) positive epithelial cells of (A) the small intestine, as well as in (B) colon tissue and (C) tumor sample. In addition, sections from CD patient No. 8 are double-positive for FcεRI α- and γ-chain in (D) the small intestinal, (E) colon and in (F) lesional tissue. (G) Only in the subepithelial tissue FcεRI β-chain (green) positive cells are detected as shown here in the crypts of small intestinal tissue. (H) Negative control with mouse IgG2b and goat IgG isotype control antibodies. The blue fluorescence DAPI staining indicates the nuclei. Original magnification ×64.</p

    Western blot analysis reveals FcεRI in human intestinal tumor cell lines.

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    <p>(A) FcεRI α-chain and (B) FcεRI γ-chain expression is investigated in Caco2/TC7 and HCT8 subconfluent and confluent cell lines. In all experiments RBL cells transfected with the human FcεRI receptor served as positive controls and the protein expression signal was normalized to the expression of house-keeping protein actin.</p
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