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  • 1
    Electronic Resource
    Electronic Resource
    Nonoxidative protein glycation is implicated in familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation (2000)
    Springer
    Acta neuropathologica 100 (2000), S. 275-284 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyotrophic lateral sclerosis ; Imidazolone ; Nɛ-carboxymethyl-lysine ; Pyrraline ; Superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To assess a role for oxidative stress in the pathogenesis of amyotrophic lateral sclerosis (ALS), we analyzed the immunohistochemical localization of 8-hydroxy-2′-deoxyguanosine (OHdG) as a nucleic acid oxidation product, acrolein-protein adduct and 4-hydroxy-2-nonenal (HNE)-protein adduct as lipid peroxidation products, N ɛ-carboxymethyl-lysine (CML) as a lipid peroxidation or protein glycoxidation product, pentosidine as a protein glycoxidation product, and imidazolone and pyrraline as nonoxidative protein glycation products in the spinal cord of three familial ALS patients with superoxide dismutase-1 (SOD1) A4V mutation, six sporadic ALS patients, and six age-matched control individuals. The spinal cord sections of the control cases did not show any distinct immunoreactivities for these examined products. In the familial ALS cases, intense immunoreactivities for pyrraline and CML were confined to the characteristic Lewy body-like hyaline inclusions, and imidazolone immunoreactivity was located in the cytoplasm of the residual motor neurons. No significant immunoreactivities for other examined products were detected in the familial ALS spinal cords. In the sporadic ALS cases, intense immunoreactivities for pentosidine, CML and HNE-protein adduct were seen in the cytoplasm of the degenerated motor neurons, and OHdG immunoreactivity was located in the cell nuclei of the residual neurons and glial cells. The present results indicate that oxidative reactions are involved in the disease processes of sporadic ALS, while there is no evidence for increased oxidative damage except for CML deposition in the familial ALS spinal cords. Furthermore, it is likely that the accumulation of pyrraline and imidazolone supports a nonoxidative mechanism in SOD1-related motor neuron degeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004019900173
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  • 2
    Electronic Resource
    Electronic Resource
    Immunochemical demonstration of Eisenia tetradecapeptide, a bioactive peptide isolated from the gut of the earthworm Eisenia foetida, in tissues of the earthworm (1997)
    Springer
    Cell & tissue research 288 (1997), S. 567-573 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Eisenia tetradecapeptide ; Enzyme-linked immunosorbent assay (ELISA) ; Gut motility ; Immunohistochemistry ; Neuropeptide ; Peptide hormone ; Eisenia foetida (Annelida)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The quantity and localization of Eisenia tetradecapeptide which was isolated from the gut of the earthworm Eisenia foetida were examined in tissues of the same species by enzyme-linked immunosorbent assay and immunohistochemistry. Analysis by enzyme-linked immunosorbent assay showed that Eisenia-tetradecapeptide-like immunoreactivity was present in both the central nervous system (cerebral ganglion, subesophageal ganglion, ventral ganglia, and ventral nerve cord) and the gut (esophagus, crop, gizzard, and intestine). The central nervous system contained a higher amount of Eisenia-tetradecapeptide-like immunoreactivity (1.3 pmol/mg wet weight) than the gut (0.2–0.6 pmol/mg wet weight). Eisenia-tetradecapeptide-like immunoreactivity was scarcely detected in the body-wall muscle, nephridia, and sexual organs (testis, ovary, seminal vesicle, and ovisac). Immunohistochemical analysis demonstrated that intense Eisenia-tetradecapeptide-like immunopositive cells and nerve fibers were present in the central nervous system. Immunoreactivity was found in the epithelial cells lining the esophagus and in the submucous plexus in various parts of the gut. Thus, the present study suggests that Eisenia tetradecapeptide is a neuropeptide and/or peptide hormone present in both the central nervous system and the gut of the earthworm and that its role involves the regulation of gut motility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050842
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    Paper (German National Licenses)
    Fulltext
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