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  • Electronic Resource  (2)
  • 38 000 Mr autoantigen  (1)
  • Cholangiocellular carcinoma  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Trisomy 1 and 8 occur frequently in hepatocellular carcinoma but not in liver cell adenoma and focal nodular hyperplasia. A fluorescence in situ hybridization study (1995)
    Springer
    Virchows Archiv 427 (1995), S. 373-378 
    Details
    ISSN: 1432-2307
    Keywords: Hepatocellular carcinoma ; Cholangiocellular carcinoma ; Cytogenetics ; Chromosome 1 ; Fluorescence in situ hybridization (FISH)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Conventional cytogenetic studies revealed gains and structural aberrations of chromosome 1 to be the most consistent chromosomal aberrations in hepatocellular carcinoma (HCC). We investigated touch preparations of eight HCC, five cholangiocellular carcinomas (CCC), five liver cell adenomas (LCA), four focal nodular hyperplasias (FNH) as well as nine specimens of normal liver tissue using fluorescence in situ hybridization (FISH) with centromere specific probes for chromosomes 1 and 8. Polysomies of chromosome 1, especially trisomy 1, were found in five of eight HCC and four of five CCC but in no normal liver tissue or benign tumour. Only three of seven cases of HCC revealed trisomy 8 whereas the five benign liver tumours and all normal liver tissues examined had disomy 8. Our results confirm conventional cytogenetic findings in terms of chromosome 1 aberrations in HCC although they are not specific for these types of malignant liver tumours. Since α-satellite probes were used in our study, only gains or losses including the centromeric regions of the chromosomes 1 and 8 could be detected. Nevertheless, our findings suggest that FISH may help in the differential diagnosis of malignant versus benign neoplasms of the liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00199385
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Peptide mapping and characterisation of glycation patterns of the glima 38 antigen recognised by autoantibodies in Type I diabetic patients (2000)
    Springer
    Diabetologia 43 (2000), S. 598-608 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Type I diabetes ; immunology ; autoantibodies ; target autoantigen ; 38 000 Mr autoantigen ; glima 38 ; proteolytic cleavage ; peptide mapping ; lectin binding ; deglycation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. Glima 38 is an N-glycated neuroendocrine membrane protein of Mr 38 000, which is recognised by autoantibodies in approximately 20 % of patients with Type I (insulin-dependent) diabetes mellitus. The aim of this study was to characterise the carbohydrate moiety and generate peptide maps of glima 38. Methods. Sera of high immunoreactivity to glima 38 were used to isolate 35-S methionine-labelled protein from βTC-3 cells and a neuronal cell line GT1.7. Tunicamycin was used to inhibit N-glycation of glima 38 and define the core protein. The carbohydrate moiety was characterised for tunicamycin sensitivity, lectin binding and susceptibility to different endoglycosidases. The protein moiety was subjected to digestion by proteases to define peptide maps. Results. The autoreactive epitopes in glima 38 recognised by Type I diabetic sera are conformational and independent of the carbohydrate moiety. Inhibition of N-glycation of glima 38 in vivo, shows a protein core of Mr 22 000 in both pancreatic β-(βTC3) and neuronal (GT1.7) cell lines. The carbohydrate moieties in the two cell types are distinct but contain a similar amount of terminal sialic acid residues and at least five oligosaccharide chains Glima 38 binds Triticum vulgare and Ricinus communis I lectins. Endoproteinase treatment of the Mr 22 000 core protein results in peptides of Mr 4500 and Mr 20 000 with Lys-C, and peptides of Mr 4 000 and Mr 11 000–12 000 with Glu-C/V8 and Asp-N proteases. Conclusion/interpretation. The biochemical properties of glima 38 define it as a new autoantigen in Type I diabetes and provide a basis for its purification. [Diabetologia (2000) 43: 598–608]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051349
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    Paper (German National Licenses)
    Fulltext
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