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  • Glial fibrillary acidic protein  (2)
  • Colon tumour  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Focal ependymal differentiation in the choroid plexus of human newborn brain confirmed by immunohistochemistry with monoclonal antibodies (1987)
    Springer
    Acta neuropathologica 73 (1987), S. 409-410 
    Details
    ISSN: 1432-0533
    Keywords: “Ependymzotte” ; Glial fibrillary acidic protein ; Choroid plexus epithelium ; Immunoperoxidase ; Cytokeratin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Ependymal proliferation [“Ependymzotten”, G. Becker, Beitr Pathol Anat Allg Pathol 103:457–477 (1939)], found in choroid plexus of newborns, can be made easily visible by immunostaining with antiglial fibrillary acidic protein (GFAP) antibodies. The expression of both GFAP and cytokeratin is an unusual feature of these structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688270
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunodetection of epithelial mucin (MUC1, MUC3) and mucin-associated glycotopes (TF, Tn, and sialosyl-Tn) in benign and malignant lesions of colonic epithelium: apolar localization corresponds to malignant transformation (1997)
    Springer
    Virchows Archiv 431 (1997), S. 159-166 
    Details
    ISSN: 1432-2307
    Keywords: Key words  Mucin ; Thomsen-Friedenreich antigen ; Carbohydrate ; Carcinogenesis ; Colon tumour
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Epithelial mucins are present at the apical membranes of gastrointestinal epithelial cells or in their secretions. In this study, we examined the occurrence of peptide epitopes of the mucins MUC1 and MUC3 and of three mucin-associated glycotopes (TF, Tn, and s-Tn) in a series of colorectal tissue samples (normal colon, adenomas with different grades of dysplasia, carcinoma in situ, and invasive carcinomas). A new monoclonal antibody to a conformation-dependent peptide epitope of MUC1 was employed, which does not react with the fully glycosylated mucin as found in normal gastrointestinal mucosa. We found that adenomas acquired the ability to expose Tn, s-Tn, TF and MUC1 epitopes, and this correlated with increasing malignant potential. The secretory mucin, MUC3, revealed a different pattern: it was detectable in all sections, with maximum expression in adenomas and decrease in carcinomas. Most importantly, normal mucosa and benign lesions showed supranuclear and/or apical distribution of these antigens, but malignant lesions and lesions with a very high risk of malignancy revealed diffuse cytoplasmic and basolateral membrane localization. The immunohistological response to a combination of MUC1-related antibodies may assist in assessing the malignant potential and status of lesions of the colon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050083
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Coexpression of cytokeratin and vimentin in Rathke's cysts of the human pituitary gland (1988)
    Springer
    Cell & tissue research 253 (1988), S. 419-424 
    Details
    ISSN: 1432-0878
    Keywords: Pituitary gland, pars intermedia ; Rathke's cysts ; Immunohistochemistry ; Cytokeratin ; Glial fibrillary acidic protein ; Vimentin ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunohistochemistry with monoclonal and polyclonal antibodies revealed the presence of cytokeratins in epithelial cells of Rathke's cysts in the pars intermedia of the human pituitary gland. With monoclonal antibodies specific for individual cytokeratins, the expression of CK 18, CK 8, CK 7, and CK 19 could be shown in these cells. Within the hypophysis, CK 19 and CK 7 were restricted to Rathke's cysts and a few epithelial cell clusters in the pars tuberalis, whereas other cytokeratins were also present in endocrine cells of the pars distalis. Furthermore, vimentin and, focally, glial fibrillary acidic protein (GFAP) were detected in the cystic epithelia. By double labelling, coexpression of cytokeratin and vimentin, GFAP and cytokeratin, and GFAP and vimentin could be demonstrated. Compiled data of all known cases of coexpression of cytokeratin and vimentin in normal cells reveal physiological correlations and suggest a functional significance of this rare type of coexpression of intermediate filament proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00222299
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    Paper (German National Licenses)
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