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  • 1
    Electronic Resource
    Electronic Resource
    In Vitro Phosphorylation of the Cytoplasmic Domain of the Amyloid Precursor Protein by Glycogen Synthase Kinase-3β (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The two pathological lesions found in the brains of Alzheimer's disease patients, neurofibrillary tangles and neuritic plaques, are likely to be formed through a common pathway. Neurofibrillary tangles are intracellular aggregates of paired helical filaments, the main component of which is hyperphosphorylated forms of the microtubule-associated protein τ. Extracellular neuritic plaques and diffuse and vascular amyloid deposits are aggregates of β-amyloid protein, a 4-kDa protein derived from the amyloid precursor protein (APP). Using conditions in vitro under which two proline-directed protein kinases, glycogen synthase kinase-3β (GSK-3β) and mitogen-activated protein kinase (MAPK), were able to hyperphosphorylate τ, GSK-3β but not MAPK phosphorylated recombinant APPcyt. The sole site of phosphorylation in APPcyt by GSK-3β was determined by phosphoamino acid analysis and phosphorylation of APPcyt mutant peptides to be Thr743 (numbering as for APP770). This site was confirmed by endoproteinase Glu-C digestion of APPcyt and peptide sequencing. The ability of GSK-3β to phosphorylate APPcyt and τ provides a putative link between the two lesions and indicates a critical role of GSK-3β in the pathogenesis of Alzheimer's disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67020699.x
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  • 2
    Electronic Resource
    Electronic Resource
    Evaluation of Cathepsins D and G and EC 3.4.24.15 as Candidate β-Secretase Proteases Using Peptide and Amyloid Precursor Protein Substrates (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 66 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: No single protease has emerged that possesses all the expected properties for β-secretase, including brain localization, appropriate peptide cleavage specificity, and the ability to cleave amyloid precursor protein exactly at the amino-terminus of β-amyloid peptide. We have isolated and purified a brain-derived activity that cleaves the synthetic peptide substrate SEVKMDAEF between methionine and aspartate residues, as required to generate the amino-terminus of β-amyloid peptide. Its molecular size of 55–60 kDa and inhibitory profile indicate that we have purified the metalloprotease EC 3.4.24.15. We have compared the sequence specificity of EC 3.4.24.15, cathepsin D, and cathepsin G for their ability to cleave the model peptide SEVKMDAEF or related peptides that contain substitutions reported to modulate β-amyloid peptide production. We have also tested the ability of these enzymes to form carboxy-terminal fragments from full-length, membrane-embedded amyloid precursor protein substrate or amyloid precursor protein that contains the Swedish KM → NL mutation. The correct cleavage was tested with an antibody specific for the free amino-terminus of β-amyloid peptide. Our results exclude EC 3.4.24.15 as a candidate β-secretase. Although cathepsin G cleaves the model peptide correctly, it displays poor ability to cleave the Swedish KM → NL peptide and does not generate carboxy-terminal fragments that are immunoreactive with amino-terminal-specific antiserum. Cathepsin D does not cleave the model peptide or show specificity for wild-type amyloid precursor protein; however, it cleaves the Swedish “NL peptide” and “NL precursor” substrates appropriately. Our results suggest that cathepsin D could act as β-secretase in the Swedish type of familial Alzheimer's disease and demonstrate the importance of using full-length substrate to verify the sequence specificity of candidate proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.66062436.x
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  • 3
    Electronic Resource
    Electronic Resource
    Selective Aggregation of Endogenous β-Amyloid Peptide and Soluble Amyloid Precursor Protein in Cerebrospinal Fluid by Zinc (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: Zinc added to buffered solutions of synthetic β-amyloid peptide (Aβ) has been reported to induce accelerated formation of insoluble aggregates. This observation suggests that zinc may play a role in the formation of senile plaques, which contain Aβ, in Alzheimer's disease. To test this hypothesis under conditions more representative of the brain, we investigated the ability of zinc to induce aggregation of Aβ in freshly drawn canine CSF, which contains the same sequence as human Aβ. Aggregates were separated from CSF by ultracentrifugation before and after incubation with zinc and assayed by quantitative western blotting and ELISA. We found that zinc induced the rapid aggregation of endogenous Aβ in CSF, with an EC50 of 120–140 µM. The reaction was specific, because most (≥95%) CSF protein remained soluble under conditions where most Aβ was insoluble, as assayed by scanning densitometry of Coomassie-stained gels. Staining of the precipitated material resulted in the visualization of punctate regions that were thioflavin positive or birefringent when stained with Congo red, suggesting the formation of amyloid-related structures. These results suggest that zinc could play a role in amyloid deposition, because there is overlap between the regions of the brain where zinc concentrations are highest and regions with the highest amyloid content. It is surprising that zinc induced the aggregation of endogenous soluble APP at lower concentrations than required for Aβ (EC50 80 µM). The possibility that zinc-induced aggregation of APP may precede the deposition of Aβ into plaques is discussed. Investigation of aggregation of Aβ in CSF will aid in assessing the biological relevance of other agents that have been reported to accelerate amyloid formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69031204.x
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  • 4
    Electronic Resource
    Electronic Resource
    Metronidazole and risk of acute pancreatitis: a population-based case–control study (2005)
    Oxford, UK : Blackwell Science Ltd
    Alimentary pharmacology & therapeutics 21 (2005), S. 0 
    Details
    ISSN: 1365-2036
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background : Use of metronidazole has been suggested to be associated with an increased risk of acute pancreatitis in case reports.Aim : To examine this issue within a proper epidemiological design.Methods : We identified 3083 incident cases of acute pancreatitis from Hospital Discharge Registries in three Danish counties and 30 830 matched population controls. From prescription databases, we extracted information on use of metronidazole with or without concomitant use of proton-pump inhibitors and/or amoxicillin, macrolides or tetracycline.Results : Adjusted odds ratios for acute pancreatitis in study subjects who redeemed a prescription for metronidazole within 30, 31–180, or 181–365 days before hospitalization or index date among controls were 3.0 [95% confidence interval (CI): 1.4–6.6], 1.8 (95% CI: 1.2–2.9) and 1.1 (95% CI: 0.6–1.8), respectively. Among subjects with a concomitant prescription for proton-pump inhibitors and/or amoxicillin, macrolides or tetracycline within 30, 31–180, or 181–365 days before hospitalization, or index date among controls, adjusted odds ratios were 8.3 (95% CI: 2.6–26.4), 2.7 (95% CI: 1.4–5.5), and 1.7 (95% CI: 0.6–4.8), respectively.Conclusion : Metronidazole may increase the risk of acute pancreatitis. However, the risk seems mainly to increase when metronidazole is used in combination with other drugs used for Helicobacter pylori eradication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2036.2005.02344.x
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  • 5
    Electronic Resource
    Electronic Resource
    Regulation of Ribonucleic Acid Metabolism by Plant Hormones (1977)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 28 (1977), S. 537-564 
    Details
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pp.28.060177.002541
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  • 6
    Electronic Resource
    Electronic Resource
    Mechanisms of mutagenesis by the vinyl chloride metabolite chloroacetaldehyde. Effect of gene-targeted in vitro adduction of M13 DNA on DNA template activity in vivo and in vitro (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 496-504 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00454a025
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  • 7
    Electronic Resource
    Electronic Resource
    Ultrapure Hydrogen Generator for Gas Chromatography. (1965)
    s.l. : American Chemical Society
    Analytical chemistry 37 (1965), S. 319-320 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60221a055
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  • 8
    Electronic Resource
    Electronic Resource
    Simple solid-state pH meter (1966)
    s.l. : American Chemical Society
    Analytical chemistry 38 (1966), S. 1975-1975 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac50155a095
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  • 9
    Electronic Resource
    Electronic Resource
    Pipette Used in Titration of Oils for Acidity. (1918)
    s.l. : American Chemical Society
    Industrial & engineering chemistry 10 (1918), S. 633-633 
    Details
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ie50104a032
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  • 10
    Electronic Resource
    Electronic Resource
    Blood tests before elective surgery (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Anaesthesia 42 (1987), S. 0 
    Details
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2044.1987.tb02952.x
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