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  • 1
    Electronic Resource
    Electronic Resource
    Antibodies to cytokeratin and vimentin in testicular tumour diagnosis (1985)
    Springer
    Virchows Archiv 408 (1985), S. 127-142 
    Details
    ISSN: 1432-2307
    Keywords: Cytokeratin ; Vimentin ; Testis ; Seminoma ; Embryonal cell carcinoma ; Endodermal sinus tumour ; Teratocarcinoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Thirteen primary and metastatic testicular germ cell tumours, including classical and anaplastic seminomas, and non-seminomatous testicular tumours were examined for their intermediate filament protein (IFP) types. The seminomas were shown to react with a monoclonal and a polyclonal antibody to bovine lens vimentin, while non-seminomatous germ cell tumours were strongly positive for a polyclonal and a monoclonal antibody to cytokeratin. In one case of seminoma with elevated serum levels ofβHCG andαFP, cytokeratin positive tumour cells were found. In the case of teratocarcinoma, several components of the tumour could be distinguished using a combination of antisera in double-label immunofluorescence microscopy. The glandular component of this tumour was positive with the polyclonal antikeratin, but also with the monoclonal cytokeratin antibody specific for glandular epithelia (RGE 53). However, the squamous component was negative with this latter antibody. Strikingly, the spindle cell component showed focal positivity for vimentin, with coexpression of cytokeratin and vimentin in some cells. Our data show that antibodies to cytokeratin and vimentin can be helpful in the diagnosis of testicular germ cell tumours, especially in the differentiation between seminomas and non-seminomatous tumours.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00707977
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  • 2
    Electronic Resource
    Electronic Resource
    GLUT-4 expression is not consistently higher in type-1 than in type-2 fibres of rat and human vastus lateralis muscles; an immunohistochemical study (2000)
    Springer
    Pflügers Archiv 441 (2000), S. 351-358 
    Details
    ISSN: 1432-2013
    Keywords: GLUT-4 Fibre type Immunofluorescence microscopy Skeletal muscle activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. In whole muscle homogenates, the glucose transporter-4 (GLUT-4) content is reported to be higher in muscles consisting predominantly of oxidative (type-1) muscle fibres than in muscles consisting predominantly of glycolytic (type-2) fibres. From these findings, it has been deduced that in rat muscle, oxidative fibres have an intrinsically higher level of GLUT-4 protein than glycolytic fibres. No data is available concerning human muscle. Moreover, the fibre-type-specific expression of GLUT-4 has not yet been examined directly. In this study, the relative abundance of GLUT-4 protein expression in individual fibres of different types within a muscle was compared directly in immunohistochemical assays. The human vastus lateralis muscle and a selection of rat muscles were studied using a novel GLUT-4 antiserum. It is concluded that the pattern of fibre-type-specific GLUT-4 expression differs between human and rats and varies between the different muscles studied, indicating that non-fibre-type-specific factor(s) affect expression of GLUT-4. The observation that within a muscle a fibre-type-specific expression of GLUT-4 was observed indicates that fibre-type-specific factors contribute to GLUT-4 expression as well. Thus, it can be postulated that both fibre-type-dependent and fibre-type-independent factors affect GLUT-4 expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240000431
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  • 3
    Electronic Resource
    Electronic Resource
    Differentiation of human skeletal muscle cells in culture: maturation as indicated by titin and desmin striation (1992)
    Springer
    Cell & tissue research 270 (1992), S. 189-198 
    Details
    ISSN: 1432-0878
    Keywords: Skeletal muscle cells ; Myofibrillogenesis ; Intermediate filaments ; Titin ; Nebulin ; Myosin ; α-Actinin ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary This report describes a phenotyping study of differentiating human skeletal muscle cells in tissue culture. Satellite cells (adult myoblasts), isolated from biopsy material, showed a proliferative behaviour in high-nutrition medium, but fused to form myotubes when grown in low-nutrition medium. The expression and structural organization of the intermediate filament proteins desmin and vimentin as well as the sarcomeric constituents α-actin, α-actinin, nebulin, myosin and especially titin during myofibrillogenesis in vitro, were studied by means of indirect immunofluorescence assays. The proliferating myoblasts contained both desmin and vimentin, α-actinin and the filamentous form of actin. Shortly after the change of medium, expression of titin, sarcomeric myosin and skeletal muscle α-actin was found in mononuclear cells in a diffuse, filamentous (titin, myosin, α-actin) or punctate (titin, myosin) pattern. Four to 10 days after the medium change, mature myotubes showed desmin, titin, α-actinin, nebulin, sarcomeric myosin and actin cross-striations, while vimentin was no longer detected. We conclude that human skeletal muscle cell cultures are an appropriate model system to study the molecular basis of myofibrillogenesis. Especially the presence of desmin in a striated fashion points to a high degree of maturation of the muscle cell cultures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00381893
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  • 4
    Electronic Resource
    Electronic Resource
    Titin expression as an early indication of heart and skeletal muscle differentiation in vitro. Developmental re-organisation in relation to cytoskeletal constituents (1996)
    Springer
    Journal of muscle research and cell motility 17 (1996), S. 23-36 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Established myogenic cell lines of different species and tissue origin have been used to study expression and organisation of muscle-specific proteins during differentiation. Furthermore, primary cultures of rat myocard cells were used to examine these same processes during dedifferentiation. In particular, we were interested in the general mechanism that underlies the changes in the supramolecular organisation of titin during in vitro myogenesis. It became obvious that in the differentiating muscle cell cultures the redistribution of desmin, actin and myosin in a typical, differentiation state dependent fashion, always showed a certain delay when compared to titin. The sequence of changes in the assembly of cytoskeletal and sarcomeric structures observed during differentiation of the cell lines was reversed during the process of dedifferentiation in cultured rat myocard cells. These results all indicate that titin is an early marker of myogenic differentiation, both in vivo and in vitro, and that the typical reorganisation of this giant molecule is independent of species or muscle cell type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00140321
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    Paper (German National Licenses)
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