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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 80 (1990), S. 597-603 
    ISSN: 1432-0533
    Keywords: Choroid plexus ; Amyloid ; Intracellular inclusions ; Ultrastructure ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Intracellular inclusions with staining properties of amyloid are very common in the aging choroid plexus epithelial cells. In many ways these inclusions show similarities with the neurofibrillary tangles, found in cerebral cortical neurons in patients with Alzheimer's dementia. We have now designed a purification method for choroid plexus amyloid and performed a transmission and scanning electron miscroscopic study. This shows that one form of choroid plexus inclusions, the Biondi ring, is a homogeneous globule covered with a thin layer of amyloid fibrils. Partial immunochemical characterization of the choroid plexus amyloid reveals that it is different from the neurofibrillary tangles although there are similarities.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0428
    Keywords: Islet amyloid polypeptide ; Pancreatic islets ; B cells ; Ultrastructure ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Islet amyloid polypeptide is a novel 37 amino-acid-residues polypeptide which has been isolated from amyloid deposits in an insulinoma, and in human and cat islets of Langerhans. The molecule has 46% homology with the calcitonin gene-related peptide. Light microscopy examination of the pancreas shows that islet amyloid polypeptide immunoreactivity is restricted to the islet B cells. The present study utilized a rabbit antiserum against a synthetic peptide corresponding to positions 20–29 of islet amyloid polypeptide, a sequence without any amino-acid identity with calcitonin gene-related peptide. By applying the immunogold technique at the ultrastructural level, it was shown that both insulin and islet amyloid polypeptide immunoreactivity occurs in the central granular core of the human B cell secretory granules, while the A cells remain unlabelled. The demonstration that islet amyloid polypeptide is a granular protein of the B cells may indicate that it is released together with insulin. Further studies are necessary to evaluate the functional role of islet amyloid polypeptide.
    Type of Medium: Electronic Resource
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