SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
Volume 45, Issue 3
Displaying 1-3 of 3 articles from this issue
  • Taisuke Yamazaki, Susumu Sakurai, Minoru Kohno
    2001 Volume 45 Issue 3 Pages 171-175
    Published: September 15, 2001
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Staphylococcal exfoliative toxin A (ETA) was purified from the supernatant of a Staphylococcus aureus (S. aureus) ZM strain belonging to the typical phage group II and tested for its ability to induce arthritis in the ankle joints of mice that had been previously injected with bovine type II collagen (bIIC). In this experiment, inflammation was not induced after a single injection of a low dose (100μg/mouse) of bIIC. A prolonged joint inflammation in the forelimb digits of mice injected with bIIC (100μg/mouse) was induced by a single injection of ETA (50μg/mouse) 2-9 weeks after the bIIC injection. Histological studies showed the extensive deposition of fibrinous exudate in the joint space, synovial proliferation, bone resorption and marginal erosion of the cartilage in the forelimb joints. We examined the RNA levels of inflammatory cytokines using RT-PCR and Southern blot hybridization and found that the genes for inflammatory cytokines, (IL-1β, IL-6, TNF-α and IFN-γ) were activated in the inflammed ankle joints, and forelimb digit joints of mice injected with ETA after the injection of bIIC. These results suggest that ETA induces severe arthritis in the ankle joints and forelimb digit joints of mice that have been previously injected with bIIC.
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  • Iwao Koyama, Tsuyoshi Harada, Toshiyuki Matsunaga, Shigeru Hokari, May ...
    2001 Volume 45 Issue 3 Pages 177-183
    Published: September 15, 2001
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    The characteristics of alkaline phosphatase (AP) and nitric oxide synthase (NOS) in the lung were investigated using rats challenged with lipopolysaccharide (LPS). Lung homogenates and alveolar lavage fluid were prepared from rats after an intratracheal instillation of 20mg/kg body weight of LPS. AP activities in homogenates were elevated up to 2hr and had recovered to the control level by 6hr. In contrast, those in lavage fluid were significantly decreased after 30min and recovered to the control level by 6hr. Although APs in normal lavage fluid were of the membranous-type in addition to the soluble-type, APs after LPS-challenge were soluble-type only. The 75kDa AP molecule in the homogenate at 2hr after LPS-challenge was increased, in comparison with the control, as was the level of AP activity. In contrast, there was no difference in AP protein level in lavage fluid between the control and LPS-challenged rats. Inducible NOS (iNOS) was obviously induced in lung homogenates by LPS-challenge. Moreover, proteins containing nitrotyrosine as a marker of peroxynitrite were identifiable by Western blot analysis in lavage fluid from rats challenged with LPS. These results indicate that LPS-challenge directly affects the expression and secretion of APs from type II pneumocytes.
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  • Kanenobu Kubo, Yoshiyuki Morishima
    2001 Volume 45 Issue 3 Pages 185-191
    Published: September 15, 2001
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Human serum proteins including myeloma (M) proteins were analyzed by capillary zone electrophoresis (CZE) using a linear polyacrylamide-coated capillary at pH 7.4. Each of the M proteins, IgG-κ, IgA-κ, and IgA-λ, which were located on the β zone on the cellulose acetate electrophoresis (CAE), was resolved into a group of peaks with a unique profile in a wide area following the transferrin (TF) peak. While the IgG-κ showed a series of narrow peaks, IgA-κ and IgA-λ showed a wide peak with many successive spikes. On the other hand, the increased polyclonal IgA-κ and IgG-κ, which were located on the β zone on the CAE, showed only a broad peak around the TF peak. Another IgG-κ M protein, which was located on the γ zone on the CAE, did not appear on the CZE at pH 7.4, but did appear with several peaks by increasing the pH to 9.0. No peaks were observed in the area following the TF peak when healthy serum proteins including immunoglobulins (Igs) were analyzed at both pHs. The coexistence of albumin did not affect the detection of monoclonal and polyclonal Igs. These results demonstrate that the CZE system is capable of distinguishing IgG M proteins from IgA M proteins, and monoclonal Igs from polyclonal ones. Furthermore, it was found that the CZE is useful for discriminating between isoforms of IgG M proteins.
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