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  1. Kawana A, Toyota E, Kobayashi N, Kudo K, Genka I, Aoki M, et al.
    Kansenshogaku Zasshi, 1998 Mar;72(3):238-44.
    PMID: 9585697
    The prevalence of mycobacterial infection in AIDS patients has increased in Japan. This report describes details of the clinical and radiological features of eight AIDS patients with mycobacterial disease (6 with M. tuberculosis infection and 2 with M. kansasii infection) in our hospital during the period from October 1995 through February 1997. Six of the 8 were men, and two were women. The mean age was 36.5 years. Six were Japanese, one was from Myanmar, and one was Malaysian. The median CD4 positive T lymphocyte counts (CD4 count) at the time of diagnosis of the M. tuberculosis was 75.5 (range 14-569/microliter, and the M. kansasii was 21.5 (range 19-24)/microliter. Clinical findings and symptoms of all patients were non-specific, but almost all patients had a cough and fever. In the radiographic findings, the patients of the M. tuberculosis group presented multiple hilar and mediastinal lymphadenopathy, miliary shadow, and obstructive pneumonia. Both M. kansasii patients showed a multiple infiltration shadow. There were no drug resistant strains in M. tuberculosis except on isolate with moderate resistant. to Streptomycin. These observations suggest that AIDS-associated mycobacterial disease shows atypical clinical and radiological features in some cases, especially in advanced stages of AIDS. Therefore, we need to recognize the characteristics of the clinical and radiological features of the patients with mycobacterial diseases and AIDS.
  2. Ishima Y, Mimono A, Tuan Giam Chuang V, Fukuda T, Kusumoto K, Okuhira K, et al.
    IUBMB Life, 2020 04;72(4):641-651.
    PMID: 31794135 DOI: 10.1002/iub.2203
    Deposition of amyloid protein, particularly Aβ1-42 , is a major contributor to the onset of Alzheimer's disease (AD). However, almost no deposition of Aβ in the peripheral tissues could be found. Human serum albumin (HSA), the most abundant protein in the blood, has been reported to inhibit amyloid formation through binding Aβ, which is believed to play an important role in the peripheral clearance of Aβ. We identified the Aβ binding site on HSA and developed HSA mutants with high binding capacities for Aβ using a phage display method. HSA fragment 187-385 (Domain II) was found to exhibit the highest binding capacity for Aβ compared with the other two HSA fragments. To elucidate the sequence that forms the binding site for Aβ on Domain II, a random screening of Domain II display phage biopanning was constructed. A number of mutants with higher Aβ binding capacities than the wild type were identified. These mutants exhibited stronger scavenging abilities than the wild type, as revealed via in vitro equilibrium dialysis of Aβ experiments. These findings provide useful basic data for developing a safer alternative therapy than Aβ vaccines and for application in plasma exchange as well as extracorporeal dialysis.
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