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  • 2000-2004
  • 1980-1984  (2)
  • 1965-1969
  • 1984  (2)
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  • 2000-2004
  • 1980-1984  (2)
  • 1965-1969
Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 19 (1984), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Natural killer (NK) cell aciiviiy in experimental murine amyloidosis was studied. In CBA/J mice, which show a high incidence of amyloidosis. NK activity was significantly decreased after 1 week of casein treatment. In C3H mice, which show a low incidence of amyloidosis, NK activity was not changed by casein treatment. Pretreatment with lipopolysaccharide in vivo enhanced the NK activities in CBA/J and C3H mice. These increases were not observed after casein treatment. The lowered NK activity of cells from CBA/J mice after casein treatment was restored to the normal range by indomethacine in vitro. Depletion of adherent cells from the spleen cells treated with casein had no effect on NK activity. Single-cell assay showed that casein treatment impaired the killing but not the binding of NK cells to target cells. After casein treatment, the splenic serum amyloid A (SAA) level gradually increased in CBA/J mice but remained low in C3H mice. NK activity was suppressed by the addition of serum obtained from CBA/J mice treated with casein but not by normal control serum. And partially purified AA protein obtained from the spleen of CBA/J mice treated with casein also suppressed NK activity in vitro.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Ca++-ATPase ; K+-NPPase ; Na+-K+ATPase ; Ultracytochemistry ; Photoreceptor cells, retinal ; Guinea pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Ca++-ATPase activity was demonstrated histochemically at light- and electron-microscopic levels in inner and outer segments of retinal photoreceptor cells of the guinea pig with the use of a newly developed one-step lead-citrate method (Ando et al. 1981). The localization of ouabain-sensitive, K+-dependent p-nitrophenylphosphatase (K+-NPPase) activity, which represents the second dephosphorylative step of the Na+-K+-ATPase system, was studied by use of the one-step method newly adapted for ultracytochemistry (Mayahara et al. 1980). In retinal photoreceptor cells fixed for 15 min in 2% paraformaldehyde the electron-dense Ca++-ATPase reaction product accumulated significantly on the inner membranes of the mitochondria but not on the plasmalemma or other cytoplasmic elements of the inner segments. The membranes of the outer segments remained unstained except the membrane arrays in close apposition to the retinal pigment epithelium. The cytochemical reaction was Ca++- and substrate-dependent and showed sensitivity to oligomycin. When Mg++-ions were used instead of Ca++-ions, a distinct reaction was also found on mitochondrial inner membranes. In contrast to the localization of the Ca++ -ATPase activity, the K+-NPPase activity was demonstrated only on the plasmalemma of the inner segments, but not on the mitochondria, other cytoplasmic elements or the outer segment membranes. This reaction was almost completely abolished by ouabain or by elimination of K+ from the incubation medium.
    Type of Medium: Electronic Resource
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