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  • 2000-2004  (1)
  • 1985-1989  (1)
  • 1
    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
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  • 2
    ISSN: 1588-2780
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract In order to describe the impact of corrosion of medical implants on the trace element balance of man samples of blood, serum and of a variety of tissues and organs were analysed for their trace element composition using instrumental neutron activation techniques. By the analysis of blood and serum the trace element status after long-term implantation as well as its dependence on time after implantation was investigated. Using autopsy samples of human organs such as heart, spleen, liver, of aorta and of lymphatic tissue from the lower pelvis transport and storage of the corrosion products was studided. These investigations were supplemented by a comprehensive study of “normal” human blood, serum, tissues and organs from patients without implants. The results demonstrate that there are high enrichments of corrosion products in several tissues and organs and that also blood and serum reveal the presence of the metal implants in the trace element levels, increasing shortly after implantation and pertaining during the entire implantation time. Thus the corrosion of metallic implants is a process not only affecting tissues from the vicinity of the implants but also influencing the trace element balance of the entire organism.
    Type of Medium: Electronic Resource
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