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  • Arthritis  (1)
  • Membrane Proteins  (1)
  • Neurofibromatosis  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 63 (1984), S. 269-275 
    ISSN: 1432-0533
    Keywords: Neurofibromatosis ; Cell culture ; Cell surface ; Cytoskeleton ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Structural proteins of cultured neurofibromatosis (NF) tumor and skin cells were studied with reference to control skin fibroblasts. In polyacrylamide gel electrophoresis (PAGE)/fluorography the banding patterns of the cell lysates were markedly similar. NF tumor cells, however, produced a 60 kD band with a stronger and a 48 kD band with a lighter protein staining and metabolic labeling intensity. Furthermore, skin cells were also characterized by a 26 kD protein and the tumor cells by a 22 kD protein with high metabolic labeling intensity. Neuraminidase/galactose oxidase/NaB3H4-labeled NF skin and control skin cells possessed a 220 kD protein that was less intensively labeled in the tumor cells. The banding pattern of the skin cells was also characterized by a protein with slightly lower molecular weight (86 kD) than that of the tumor cell lysates (90 kD). In all cell lines studied indirect immunofluorescence stainings revealed bright arrays of vimentin type intermediary filaments but no desmin, cytokeratin, glial fibrillary acidic protein (GFAP), or neurofilament proteins. NF skin and control skin cells possessed well developed actin-containing bundles of microfilaments, while those of the tumor cells lacked a typical stress-fiber organization. The general morphology of the tumor cell cultures was also irregular. Transmission electron microscopy revealed no basic differences in the structure of intermediary filaments or microfilaments. The present data provide basic knowledge of neurofibromatosis skin and tumor cells and demonstrate that cultured cells originating from neurofibromas are defective in both their intracellular and extracellular organization.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 434-441 
    ISSN: 1420-9071
    Keywords: Arthritis ; rheumatoid ; cell membranes ; etiology ; immune regulation ; membrane proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Definite genetic associations with immunological cooperative HLA-D(R) antigens have been demonstrated for rheumatoid arthritis (RA). Microbial etiology has not been proven, but some hope for the supporters of this view is still given by small viruses, plasmids of enteric bacteria or perhaps oncogen-like DNA-sequences. Yet, electrophoretical analysis of membrane proteins or surface glycoproteins of RA synovial cells does not show any differences compared to reference cells. Autoimmunity to several tissue elements has been demonstrated, but most of it is of secondary nature. Antigenicities of type II and III collagens are probably only contributory factors for HLA-DR4 positive individuals. Proteoglycans or minor cartilage collagens have not been extensively studied, so far. Endocrine, dietary or psychological influences might be triggering events for otherwise ‘preloaded’ individuals.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Clinical rheumatology 2 (1983), S. 153-158 
    ISSN: 1434-9949
    Keywords: Rheumatoid Arthritis ; Cell Membrane ; Polyacrylamide Gel Electrophoresis ; Membrane Proteins ; Surface Labelling NaB3H4 ; Synovitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Fibroblast cultures were started from synovial tissue samples of 12 rheumatoid arthritic, 9 non-rheumatoid synovitic and 6 control patients. External galactose units of plasma membrane glycoproteins of confluent cells were labelled using the galactose oxidase-tritiated borohydride method. These surface-labelled cells were analyzed for possible differences in their glycoproteins by electrophoresis in SDS-containing polyacrylamide gradient gels. Total cell lysates were separated into 50–60 polypeptide bands. Fluorography of the gels revealed about 20 labelled plasma membrane glycoproteins. Some strain-specific differences were detected between the samples in all the groups, but no correlation with rheumatoid arthritis could be demonstrated.
    Type of Medium: Electronic Resource
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