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  • 1
    Electronic Resource
    Electronic Resource
    Mobilization of aged cadmium deposits by dithiocarbamates (1983)
    Springer
    Archives of toxicology 54 (1983), S. 235-242 
    Details
    ISSN: 1432-0738
    Keywords: Cadmium ; Chronic toxicity ; Dithiocarbamates ; Chelating agents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Mice with chronic cadmium intoxication were given low levels (0.6 mm/kg) of several dithiocarbamates (parent compounds: dihydroxyethylamine, iminodiacetic acid, methylhydroxyethylamine and sarcosine) in an attempt to reduce the cadmium present in the liver and kidney. Comparing the results with those obtained with the less polar sodium diethyldithiocarbamate (NaDDTC), only ammonium di(hydroxyethyl)dithiocarbamate (NH4DHE-DTC) possessed a similar ability to reduce kidney cadmium levels. Under the experimental conditions employed, the reduction obtained with NH4DHE-DTC was less than that effected by a comparable dose of NaDDTC. A subsequent dose-dependence study showed, however, that sodium di(hydroxyethyl)dithiocarbamate (NaDHE-DTC) is quite effective at higher dosage levels (up to 5.5 mmoles/kg) where substantial reductions in both kidney (89% mobilization) and liver (38% mobilization) stores of cadmium were observed. High doses of the NaDHE-DTC are well tolerated as the LD50 of this compound in mice is greater than 19.8 mmoles/kg.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01239207
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  • 2
    Electronic Resource
    Electronic Resource
    Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis (2005)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 93 (2005), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mutations in copper/zinc superoxide dismutase (SOD1) account for 10–20% of a familial form of amyotrophic lateral sclerosis (ALS). A common feature of SOD1 mutants is abnormal aggregation of the aberrant SOD1 in neurons and glia. We now report that in ALS transgenic mouse models the constitutively expressed heat shock protein 70 (Hsp70) is mislocalized into aggregates together with mutant SOD1 and ubiquitin. Forcing increased synthesis of Hsp70 ameliorates both aggregate formation and toxicity in primary motor neurons in culture. However, chronic increase in an inducible form of Hsp70 to about 10-fold its normal level is shown here not to affect disease course or pathology developed in mice from accumulation of any of three familial ALS causing SOD1 mutants with different underlying biochemical characteristics. Therefore, increasing Hsp70 to a level that is protective in mouse models of acute ischemic insult and selected neurodegenerative disorders is not sufficient to ameliorate mutant SOD1-mediated toxicity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2005.03054.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Evidence of Increased Oxidative Damage in Both Sporadic and Familial Amyotrophic Lateral Sclerosis (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Some cases of autosomal dominant familial amyotrophic lateral sclerosis (FALS) are associated with mutations in the gene encoding Cu/Zn superoxide dismutase (SOD1), suggesting that oxidative damage may play a role in ALS pathogenesis. To further investigate the biochemical features of FALS and sporadic ALS (SALS), we examined markers of oxidative damage to protein, lipids, and DNA in motor cortex (Brodmann area 4), parietal cortex (Brodmann area 40), and cerebellum from control subjects, FALS patients with and without known SOD mutations, SALS patients, and disease controls (Pick's disease, progressive supranuclear palsy, diffuse Lewy body disease). Protein carbonyl and nuclear DNA 8-hydroxy-2′-deoxyguanosine (OH8dG) levels were increased in SALS motor cortex but not in FALS patients. Malondialdehyde levels showed no significant changes. Immunohistochemical studies showed increased neuronal staining for hemeoxygenase-1, malondialdehyde-modified protein, and OH8dG in both SALS and FALS spinal cord. These studies therefore provide further evidence that oxidative damage may play a role in the pathogenesis of neuronal degeneration in both SALS and FALS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69052064.x
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    Paper (German National Licenses)
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