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  • Articles: DFG German National Licenses  (2)
  • Anti-RANA antibody  (1)
  • Calcium efflux  (1)
  • 1
    ISSN: 1437-160X
    Keywords: Anti-RANA antibody ; Rheumatoid arthritis ; EB virus infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We studied antibodies to rheumatoid arthritis nuclear antigen (RANA) by the Ouchterlony method in 0.5% agarose plates, using soluble antigen extracted with 0.25 M sucrose solution from cultured Raji cells. Anti-RANA antibody was found in sera from 24 to 40 (60%) patients with rheumatoid arthritis (RA), from 4 of 20 (20%) patients with systemic lupus erythematosus (SLE), and from 2 of 30 (7%) healthy controls. When sucrose extracts from BJAB, Ramos, and JM cells were used as the cellular antigens, no anti-RANA precipitin lines were detected. Indirect immunofluorescence study, using Raji cells or human B lymphocytes transformed by EB virus as substrate tissues, demonstrated anti-RANA antibody as fine speckled nuclear staining. Although RA patients with positive anti-RANA antibody usually had high titers of anti-Epstein-Barr nuclear antigen (EBNA) and anti-viral capsid antigen (VCA) IgG antibodies, the Wilcoxon ranks sum test showed no close statistical correlation between the presence of anti-RANA antibodies and the titers of anti-EBNA or anti-VCA (IgG) antibodies. These data showed that the incidence of positivity of anti-RANA antibodies in Japanese RA patients is almost the same as that in American and European RA patients.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1437-7799
    Keywords: Key words SMP30 ; Calcium efflux ; Tubular epithelia ; Calcium pump ; Calmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background. Senescence marker protein-30 (SMP30), a calcium binding protein, is preferentially expressed in the renal proximal tubules and hepatocytes and is presumed to play a role in Ca2+ homeostasis. Methods. To explore its physiological functions in the tubular cells, we investigated the effect of SMP30 on Ca2+ efflux via the ATP-dependent plasma membrane calcium pump. LLC-PK1 cells were stably transfected with a cDNA encoding SMP30, and the established transfectants were subjected to ATP responses. Results. Overexpression of SMP30 significantly increased Ca2+ efflux under both basal and ATP-stimulated conditions. Inhibition of calmodulin by trifluoperazine abrogated the enhanced Ca2+ efflux, suggesting that SMP30 activated the calmodulin-dependent Ca2+ pump. It is known that Ca2+ superfluous influx induces cellular injury. Compared with mock-transfected cells, LLC-PK1 cells expressing SMP30 showed resistance to cellular death triggered by Ca2+ superfluous influx. Conclusion. These results suggest the possibility that, in renal tubular cells, endogenous SMP30 participates in Ca2+ efflux via activating the calmodulin-dependent Ca2+ pump and thereby confers resistance of the cells against injury caused by high intracellular Ca2+ concentrations.
    Type of Medium: Electronic Resource
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