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DISMED Verbund: Molekulare Mechanismen der Interaktion von AD-Genen : final scientific report (2002)

Beyreuther, Konrad

Heidelberg [and others] : ZMBH [and others]

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Schlagwort(e): Forschungsbericht

Materialart: Online-Ressource

Seiten: Online-Ressource ([33] p., 1,71 Mb.) , ill., graphs

Ausgabe: [Elektronische Ressource]

Serie: Joint German-Israeli research projects

URL: https://edocs.tib.eu/files/e01fb02/356463702.pdf

URL: https://edocs.tib.eu/files/e01fb02/356463702l.pdf

Sprache: Englisch , Deutsch

Anmerkung: Contract BMBF 01 GA 9805 3. - Differences between the printed and electronic version of the document are possible. - nBibliography p. 7. - nIndex p. 26 - 27 , Also available as printed version , Systemvoraussetzungen: Acrobat Reader.

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Digitale Medien

Altered glycosylation of acetylcholinesterase in APP (SW) Tg2576 transgenic mice occurs prior to amyloid plaque deposition (2002)

Fodero, Lisa R. ; Sáez-Valero, Javier ; McLean, Catriona A. ; [weitere]

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 81 (2002), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Previous studies have shown that a minor glycoform of acetylcholinesterase (AChE) is increased in Alzheimer's disease brain and cerebrospinal fluid. This glycoform can be distinguished from other AChE species by its lack of binding to concanavalin A (Con A). In this study, the temporal relationship between AChE glycosylation and Aβ deposition was examined in Tg2576 mice. There was a significant (p 〈 0.05) difference in AChE glycosylation in Tg2576 mice compared with age-matched background strain control mice at 4 months of age. This difference in glycosylation was also observed in 8- and 12-month-old Tg2576 mice. In contrast, Aβ plaques were only seen in the Tg2576 mice at 12 months of age, and were not detected at 4 and 8 months of age. Soluble human-sequence Aβ was detected as early as 4 months of age in the transgenic mice. The altered AChE glycosylation was due to an increase in a minor AChE isoform, which did not bind Con A, similar to that previously observed to be increased in Alzheimer's disease brain and cerebrospinal fluid. The results demonstrate that in transgenic mice altered AChE glycosylation is associated with very early events in the development of AD-like pathology. The study supports the possibility that glycosylation may also be a useful biomarker of AD.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1471-4159.2002.00902.x

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Digitale Medien

The solubility of α-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease (2001)

Campbell, Bruce C. V. ; McLean, Catriona A. ; Culvenor, Janetta G. ; [weitere]

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 76 (2001), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Intracellular inclusions containing α-synuclein (αSN) are pathognomonic features of several neurodegenerative disorders. Inclusions occur in oligodendrocytes in multiple system atrophy (MSA) and in neurons in dementia with Lewy bodies (DLB) and Parkinson's disease (PD). In order to identify disease-associated changes of αSN, this study compared the levels, solubility and molecular weight species of αSN in brain homogenates from MSA, DLB, PD and normal aged controls. In DLB and PD, substantial amounts of detergent-soluble and detergent-insoluble αSN were detected compared with controls in grey matter homogenate. Compared with controls, MSA cases had significantly higher levels of αSN in the detergent-soluble fraction of brain samples from pons and white matter but detergent-insoluble αSN was not detected. There was an inverse correlation between buffered saline-soluble and detergent-soluble levels of αSN in individual MSA cases suggesting a transition towards insolubility in disease. The differences in solubility of αSN between grey and white matter in disease may result from different processing of αSN in neurons compared with oligodendrocytes. Highly insoluble αSN is not involved in the pathogenesis of MSA. It is therefore possible that buffered saline-soluble or detergent-soluble forms of αSN are involved in the pathogenesis of other αSN-related diseases.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1471-4159.2001.00021.x

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Digitale Medien

Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: possible risk factors in the Alzheimer's-type neurodegenerative pathways (2001)

White, Anthony R. ; Huang, Xudong ; Jobling, Michael F. ; [weitere]

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 76 (2001), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Oxidative stress may have an important role in the progression of neurodegenerative disorders such as Alzheimer's disease (AD) and prion diseases. Oxidative damage could result from interactions between highly reactive transition metals such as copper (Cu) and endogenous reducing and/or oxidizing molecules in the brain. One such molecule, homocysteine, a thiol-containing amino acid, has previously been shown to modulate Cu toxicity in HeLa and endothelial cells in vitro. Due to a possible link between hyperhomocysteinemia and AD, we examined whether interaction between homocysteine and Cu could potentiate Cu neurotoxicity. Primary mouse neuronal cultures were treated with homocysteine and either Cu (II), Fe (II or III) or Zn (II). Homocysteine was shown to selectively potentiate toxicity from low micromolar concentrations of Cu. The toxicity of homocysteine/Cu coincubation was dependent on the ability of homocysteine to reduce Cu (II) as reflected by the inhibition of toxicity with the Cu (I)-specific chelator, bathocuproine disulphonate. This was supported by data showing that homocysteine reduced Cu (II) more effectively than cysteine or methionine but did not reduce Fe (III) to Fe (II). Homocysteine also generated high levels of hydrogen peroxide in the presence of Cu (II) and promoted Aβ/Cu-mediated hydrogen peroxide production and neurotoxicity. The potentiation of metal toxicity did not involve excitotoxicity as ionotropic glutamate receptor antagonists had no effect on neurotoxicity. Homocysteine alone also had no effect on neuronal glutathione levels. These studies suggest that increased copper and/or homocysteine levels in the elderly could promote significant oxidant damage to neurons and may represent additional risk factor pathways which conspire to produce AD or related neurodegenerative conditions.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1471-4159.2001.00178.x

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Digitale Medien

Substrate-Bound β-Amyloid Peptides Inhibit Cell Adhesion and Neurite Outgrowth in Primary Neuronal Cultures (2000)

Postuma, Ronald B. ; He, Weilan ; Nunan, Janelle ; [weitere]

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 74 (2000), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Accumulation of theβ-amyloid protein (Aβ) in the brain is an important step in the pathogenesis of Alzheimer's disease. However, the mechanism of Aβ toxicity remains unclear. Aβ can bind to the extracellular matrix, a structure that regulates adhesive events such as neurite outgrowth and synaptogenesis. The binding of Aβ to the extracellular matrix suggests that Aβ may disrupt cell-substrate interactions. Therefore, the effect of substrate-bound Aβ on the growth of isolated chick sympathetic and mouse cortical neurons was examined. Aβ1-40 and Aβ1-42 had dose-dependent effects on cell morphology. When tissue culture plates were coated with 0.1-10 ng/well Aβ, neurite outgrowth increased. Higher amounts of Aβ peptides (≥μg/well) inhibited outgrowth. The inhibitory effect was related to aggregation of the peptide, as preincubation of Aβ1-40 for 24 h at 37 °C (a process known to increase amyloid fibril formation) was necessary for inhibition of neurite outgrowth. Aβ29-42, but not Aβ1-28, also inhibited neurite outgrowth at high concentrations, demonstrating that the inhibitory domain is located within the hydrophobic C-terminal region. Aβ1-40, Aβ1-42, and Aβ29-42 also inhibited cell-substrate adhesion, indicating that the effect on neurite outgrowth may have been due to inhibition of cell adhesion. The results suggest that accumulation of Aβ may disrupt cell-adhesion mechanisms in vivo.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1471-4159.2000.741122.x

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