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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Gastrointestinal system-Physiology. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (463 pages)
    Edition: 1st ed.
    ISBN: 9783642778148
    Series Statement: Handbook of Experimental Pharmacology Series ; v.106
    DDC: 612.32
    Language: English
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  • 2
    Online Resource
    Online Resource
    La Vergne :Royal Society of Chemistry, The,
    Keywords: Chemistry, Metallurgic. ; Nervous system -- Degeneration. ; Electronic books.
    Description / Table of Contents: This book will appeal to both chemists and biologists at the post graduate and research level.
    Type of Medium: Online Resource
    Pages: 1 online resource (295 pages)
    Edition: 1st ed.
    ISBN: 9781847555311
    DDC: 546.3
    Language: English
    Note: Metallochemistry Of Neurodegeneration -- Contents -- Chapter 1 Introduction -- 1.1 General Model for Protein Misfolding, Aggregation, Amyloid Formation and Neurodegeneration -- 1.2 Specificity of Molecular Mechanisms in Major Neurodegenerative Diseases -- 1.2.1 Alzheimer Disease (AD) -- 1.2.2 Parkinson Disease -- 1.2.3 Amyotrophic Lateral Sclerosis -- 1.2.4 Prions Diseases -- 1.3 Models of Amyloid Seeding in Neurodegenerative Diseases -- References -- Chapter 2 Blood-Brain Barrier and Roots of Entry of Metal Ions into the Brain. Metal Ion Transport and Distribution in the Brain -- 2.1 General Features of Blood-Brain Barrier -- 2.2 Iron and Aluminium -- 2.3 Manganese -- 2.4 Lead and Mercury -- 2.5 The Olfactory Pathway of Metal Entry into the Brain -- 2.6 Astroglia and Metal Accumulation -- References -- Chapter 3 Metal Ion-Induced Redox Reactions, Oxidative Stress and Possible Impact on Neurodegeneration -- 3.1 Metal Induced Production of ROS -- 3.2 Nitric Oxide -- 3.3 Oxidative Stress and Aging -- 3.4 ROS, Protein Oxidation and Aberrant Protein Interactions -- 3.5 Peroxidation of Lipids in Aging Brain -- 3.6 Impact of Oxidative Stress on DNA -- 3.7 ROS and Cell Death -- References -- Chapter 4 Copper Metabolism in the Brain -- 4.1 Introduction -- 4.2 Models of Copper Metabolism -- 4.3 Mammalian Copper Homeostasis -- 4.4 Mammalian Cellular Copper Metabolism -- 4.5 Neurodegenerative Diseases and Copper -- 4.6 Wilson's and Menkes' Diseases -- 4.7 Familial Amyotrophic Lateral Sclerosis -- 4.8 Conclusions -- References -- Chapter 5 Lithium, A Neuroprotective Element -- 5.1 IMPase -- 5.2 GSK-3 -- References -- Chapter 6 Neurotoxicity of Aluminium -- 6.1 Neurochemistry of Aluminum -- 6.2 Aluminum and the Etiology of Alzheimer's Disease -- References -- Chapter 7 Manganese in the Brain Functioning -- 7.1 Introduction -- 7.2 Manganese Absorption. , 7.3 Manganese Transport to the Brain -- 7.4 Manganese Uptake in the Brain -- 7.5 Proteins that Utilise Manganese -- 7.6 Manganese Neurotoxicity -- 7.7 Effects on Brain Function -- 7.8 Neurological Disease Related to Manganese -- 7.9 Conclusions -- References -- Chapter 8 Alzheimer's Disease: Which Metal Now? -- 8.1 Amyloid Precursor Protein -- 8.2 Cleavage of APP and Formation of β-Amyloid -- 8.3 Neurofibrillary Tangles -- 8.4 Copper, APP and Aβ -- 8.5 Metals and Alzheimer's Disease -- 8.6 A Balance Between Copper and Zinc -- 8.7 The Rise of Iron -- 8.8 Any More Metals in Alzheimer's Disease? -- 8.9 Coordination Chemistry of Metal Ions Interacting with APP -- References -- Chapter 9 Prion Diseases and Redox Active Metals -- 9.1 Introduction -- 9.2 Cu-Binding to PrPc -- 9.3 Details of Cu2+ Co-Ordination to Mammalian PrPC and its Fragments -- 9.3.1 Binding of Cu2+ Ion by a Single Octapeptide Repeat Pro-His-Gly-Gly-Gly-Trp-Gly-Gln -- 9.3.2 pH-Dependence of Cu2+ Binding to Octapeptide Fragment -- 9.3.3 Binding of Cu2+ Ions to Dimeric and Tetrameric Octapeptide Fragments -- 9.4 The Fifth and Sixth Binding Sites Located in N-Terminal Domain -- 9.5 Binding of Cu2+ and Other Metals to PrP91-126 Region Cu(II) Coordination to PrP106-126 (KTNMKHMAGAAAAGAVVGGLG) -- 9.5.1 Involvement of His-96 in the Interaction of Cu(II) with the Neurotoxic Peptide Fragment -- 9.5.2 The Comparison of the Binding Abilities of Octameric and Neurotoxic Regions Toward Cu2+ Ions -- 9.6 Cu2+ Coordination to Chicken PrP -- 9.7 Copper Mediated PrP Internalization -- 9.8 Copper Transport -- 9.9 PrP as an Antioxidant -- 9.10 Manganese Binding -- 9.11 Cell Death and Metals -- 9.11.1 Direct Effects -- 9.11.2 Indirect Effects -- 9.11.3 Combined Effects -- 9.11.4 Age Effects -- 9.12 Metal Changes in TSEs -- 9.13 Copper and Mutant Prions -- 9.14 Conclusions -- References. , Chapter 10 Are Metals Involved in Cu-Zn Superoxide Dismutase-Related Familial Amyotrophic Lateral Sclerosis -- References -- Chapter 11 Parkinson's Disease: Any Role for Metals -- 11.1 Introduction -- 11.2 Cell Death in Parkinson's Disease -- 11.3 Genetics of Parkison's Disease -- 11.4 The Proteins Associated with Parkinson's Disease -- 11.4.1 Parkin -- 11.4.2 α-Synuclein -- 11.5 Metals in Parkinson's Disease -- 11.6 Bioinorganic Chemistry in Parkinson Disease -- 11.6.1 Binding of Copper Ions to α-Synuclein and its Fragments -- 11.7 Metal Ions and Catecholamines -- 11.8 The Neuromelanin of Substantia Nigra and Metal Ions -- 11.9 Conclusions -- References -- Chapter 12 Chelating Agents in Metal Neurotoxicity -- 12.1 Copper -- 12.2 Lead -- 12.3 Mercury -- 12.4 Iron -- References -- Chapter 13 Metal Complexes in the Brain Imaging and Diagnosis -- 13.1 Gadolinium Compounds -- 13.2 Monocrystalline Iron Oxide Nanocompounds -- 13.3 Delivery of MRI Contrast Agents -- 13.4 MRI Staining of the Hippocampal System -- 13.5 Contrast Agents in Stem Cells Therapy -- 13.6 Thallium Autometallography -- 13.7 Targeting of Contrast Agents to AD Amyloid Plaques -- References -- Subject Index.
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  • 3
    Keywords: Electronic books.
    Description / Table of Contents: This book will appeal to both chemists and biologists at the post graduate and research level.
    Type of Medium: Online Resource
    Pages: 1 online resource (295 pages)
    Edition: 1st ed.
    ISBN: 9781847555311
    Language: English
    Location Call Number Limitation Availability
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  • 4
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 110 (1988), S. 2743-2748 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 95 (1991), S. 10065-10070 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 90 (1986), S. 1129-1133 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 87 (2003), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The prion protein is a copper (Cu)-binding protein. The abnormal isoform of this protein is associated with the transmissible spongiform encephalopathies or prion diseases. In prion diseases, the prion protein loses its Cu binding capacity. The effect of prion protein expression on the Cu content of the brain was investigated. Transgenic mice, either overexpressing the prion protein or expressing a mutant form lacking the Cu-binding region of the protein, were compared with wild-type mice and mice in which expression of the protein was knocked out. Age-dependent differences in Cu content of the brain were detected. Also, synaptosomal fractions from the brains of the mice showed different Cu content depending on the expression of the prion protein. Mice expressing prion protein, but without the Cu-binding domain showed reduced Cu content. Mice overexpressing the prion protein showed little difference in Cu in the brain compared with wild type but also the prion protein expressed by the mice showed a reduction in the level of Cu bound. These results confirm that prion protein expression modulates the Cu level found at the synapse and this effect is dependent on its Cu binding capacity. Loss of normal Cu binding by the prion protein altered age-related increases in metals in the brain. This may explain why many forms of human prion disease do not develop until late in life.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Although minor abnormalities have been reported in prion protein (PrP) knock-out (Prnp−/–) mice, the normal physiological function of PrP, the causative agent implicated in transmissible spongiform encephalopathies (TSE), remains unresolved. Since there are increasing correlations between oxidative stress and amyloidoses, we decided to investigate whether PrP plays a role in oxidative modulation. We found higher levels of oxidative damage to proteins and lipids in the brain lysates of Prnp−/– as compared to wild-type (WT) mice of the same genetic background. These two indicators, protein oxidation and lipid peroxidation, are hallmarks of cellular oxidative damage. Elevated levels of ubiquitin-protein conjugates were also observed in Prnp−/– mice, a probable consequence of cellular attempts to remove the damaged proteins as indicated by increased proteasome activity. Taken together, these findings are indicative of a role for PrP in oxidative homeostasis in vivo.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 76 (2001), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We have developed a method to affinity-purify mouse prion protein (PrPc) from mouse brain and cultured cells. PrPc from mouse brain bound three copper atoms; PrPc from cultured cells bound between one and four copper atoms depending on the availability of copper in the culture medium. Purified PrPc exhibited antioxidant activity, as determined by spectrophotometric assay. Incubation of PrPc with the neurotoxic peptide, PrP106-126, inactivated the superoxide dismutase-like activity. Culture experiments showed that PrPc protects cells against oxidative stress relative to the amount of copper it binds. These results suggest that PrPc is a copper-binding protein which can incorporate varying amounts of copper and exhibit protective antioxidant activity.
    Type of Medium: Electronic Resource
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