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  • 1
    Electronic Resource
    Electronic Resource
    The La antigen shuttles between the nucleus and the cytoplasm in CV-1 cells (1989)
    Springer
    Molecular and cellular biochemistry 85 (1989), S. 103-114 
    Details
    ISSN: 1573-4919
    Keywords: La-protein ; snRNAs ; scRNAs ; autoantibody ; nucleocytoplasmic transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Recently we established a monoclonal antibody against the La-protein (Bachmannet al., Proc. Natl. Acad. Sci. USA, 83, 7770, 1986). The antibody gives a nuclear speckled type staining and, in addition, a perinuclear cytoplasmic staining on cultured cells in immunofluorescence microscopy. After inhibition of RNA synthesis the La-protein is transported into the cytoplasm. After prolonged inhibition it returns into the nucleus forming large growing speckles. The transport into the nucleus apparently depends on glycosylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00577106
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Frequency and significance of antibodies to asialoglycoprotein receptor in type 1 autoimmune hepatitis (1996)
    Springer
    Digestive diseases and sciences 41 (1996), S. 1733-1740 
    Details
    ISSN: 1573-2568
    Keywords: asialoglycoprotein receptor ; autoantibodies ; autoimmune hepatitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Antibodies to asialoglycoprotein receptor have diagnostic specificity for autoimmune hepatitis, but it is uncertain if they are complementary or redundant markers of the disease. Our aims were to assess their frequency and significance in type 1 autoimmune hepatitis and determine their contribution to the evaluation of these patients. Sear from 54 well-characterized patients were evaluated for antibodies to asialoglycoprotein receptor by a radioimmunofiltration assay based on rabbit-derived protein. Forty-four patients (82%) were seropositive. Seropositive patients were distinguished from seronegative counterparts by having higher serum gamma globulin (3.7±0.2 g/dl vs 2.3±0.3 g/dl,P=0.0007) and immunoglobulin G levels (3707±179 mg/dl vs 2203±263 mg/dl,P=0.0005) at presentation and a greater frequency of relapse after drug withdrawal (88% vs 33%,P=0.01). Seropositivity for smooth muscle and/or antinuclear antibodies did not define treatment outcomes and antinuclear antibodies occurred less frequently than the other markers. Concurrent testing for antibodies to asialoglycoprotein receptor and smooth muscle identified all patients. We conclude that antibodies to asialoglycoprotein receptor are common in type 1 autoimmune hepatitis and they identify patients with a high frequency of relapse after corticosteroid withdrawal. Concurrent testing for these antibodies and smooth muscle antibodies has the same diagnostic sensitivity as testing for antinuclear and smooth muscle antibodies but a greater prognostic implication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02088738
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  • 3
    Electronic Resource
    Electronic Resource
    Kinetics of expression of prion protein in uninfected and scrapie-infected N2a mouse neuroblastoma cells (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 11 (1993), S. 1-11 
    Details
    ISSN: 0263-6484
    Keywords: Prion protein ; prion gene expression ; scrapie ; N2a cells ; mouse neuroblastoma cells ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The scrapie prion protein, PrPSc, is formed from its isoform, the cellular PrPc. There is evidence available indicating that PrPSc is necessary component of the infectious prion particle to cause a series of transmissible spongiform encephalopathies. We have used immunocytochemistry and RNA blotting techniques to investigate if infection with prions results in an increased PrP gene expression. For the experiments we used N2a cells which had been infected with prions (ScN2a cells). We demonstrated by confocal laser scanning microscopy that PrP-protein was present in the nucleus (predominantly in the nucleoli) of ScN2a cells. Analysis of the PrP-mRNA levels both in N2a- and in ScN2a cells using cDNA encoding PrPc revealed no marked alteration of the mRNA steady state level between the two cell strains. Likewise, in run-off experiments no changes in either PrP-specific transcription or in general transcriptional activity were found. The half-life of PrP-mRNA was found to be identical in both cell strains (7 h). Taken together, these results show that PrPSc and /or PrPc is present in the nucleus (nucleoli) of ScN2a cells but does not display and effect on the expression of the PrP gene.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290110102
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