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  • 1
    Online Resource
    Online Resource
    Abeta Peptide and Alzheimer’s Disease : Celebrating a Century of Research (2007)
    London : Springer-Verlag London Limited
    Details Availability
    Keywords: Medicine ; Human genetics ; Neurosciences ; Biochemistry ; Neurology ; Neurosurgery ; Medicine & Public Health ; Biochemistry ; Human genetics ; Medicine ; Neurology ; Neurosciences ; Neurosurgery ; Alzheimer Disease metabolism ; Alzheimer Disease etiology ; Amyloid beta-Protein metabolism ; Amyloid beta-protein ; Alzheimer's disease Molecular aspects ; Alzheimerkrankheit
    Description / Table of Contents: Recent advances in genetics and brain biochemistry point to the Abeta peptide as the major culprit in causing neurodegeneration in Alzheimer's Disease (AD). This book summarizes current knowledge of the Abeta peptide and its role in AD. Written by specialists in this fast moving area, the book covers fundamental biochemical studies on this peptide, the genetic impact on Abeta expression and processing, and various AD therapeutic strategies that target Abeta.
    Type of Medium: Online Resource
    Pages: Online-Ressource (XI, 298 p, digital)
    ISBN: 9781846284403
    Series Statement: SpringerLink
    URL: https://doi.org/10.1007/978-1-84628-440-3
    URL: http://dx.doi.org/10.1007/978-1-84628-440-3
    URL: https://swbplus.bsz-bw.de/bsz262064537cov.jpg
    URL: https://swbplus.bsz-bw.de/bsz262064537vor.htm
    URL: http://www.gbv.de/dms/bowker/toc/9781852339616.pdf
    DOI: 10.1007/978-1-84628-440-3
    RVK:
    YG 4000
    Language: English
    Note: Includes bibliographical references and index , Preface; CONTENTS; Contributors; 1 A Brief Introduction to the History of the ß-Amyloid Protein (Aß) of Alzheimer's Disease; 2. The Aßcentric Pathway of Alzheimer's Disease; 3. The Function of the Amyloid Precursor Protein Family; 4. The Involvement of Aß in the Neuroinflammatory Response; 5. Amyloid ß-Peptide(1-42), Oxidative Stress, and Alzheimer's Disease; 6. Amyloid Toxicity, Synaptic Dysfunction, and the Biochemistry of Neurodegeneration in Alzheimer's Disease; 7. Aß Variants and Their Impact on Amyloid Formation and Alzheimer's Disease Progression , 8. Copper Coordination by ß-Amyloid and the Neuropathology of Alzheimer's Disease9. Cholesterol and Alzheimer's Disease; 10. Amyloid ß-Peptide and Central Cholinergic Neurons: Involvement in Normal Brain Function and Alzheimer's Disease Pathology; 11. Physiologic and Neurotoxic Properties of Aß Peptides; 12. Impact of ß-Amyloid on the Tau Pathology in Tau Transgenic Mouse and Tissue Culture Models; 13. Glial Cells and Aß Peptides in Alzheimer's Disease Pathogenesis; 14. The Role of Presenilins in Aß-Induced Cell Death in Alzheimer's Disease , 15. Immunotherapeutic Approaches to Alzheimer's Disease16. Mouse Models of Alzheimer's Disease; Subject Index; Author Index
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of dimeric and tetrameric acetylcholinesterase isoforms on the surface of cultured bovine adrenal chromaffin cells (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 398-407 
    Details
    ISSN: 0730-2312
    Keywords: protein transport ; chromaffin cell ; organophosphorus ; GPI-linked ; phosphatidyl-inositol-specific phospholipase C ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Acetylcholinesterase is a highly polymorphic enzyme, which can be anchored to the cell surface through several different mechanisms. Dimeric (G2) acetylcholinesterase isoforms are attached by a glycosylphosphatidyl-inositol (GPI) linkage, whereas tetrameric (G4) forms are linked through a 20 kilodalton hydrophobic subunit. Although cells of haemopoietic origin contain large amounts of G2 GPI-linked acetylcholinesterase, most tissues express only trace amounts of this isoform. We examined the expression of acetylcholinesterase isoforms in cultured bovine adrenal medullary chromaffin cells. Two major isoforms (G2 and G4) were identified on the cell surface. The G2 isoform, which accounted for approximately half the cell-surface enzyme activity, was linked to the membrane through a GPI anchor. After treatment with diisopropylfluorophosphate to completely inhibit cellular acetylcholinesterase, the G4 isoform was found to be resynthesised and transported to the cell surface more rapidly than the G2 isoform. As the addition of GPI anchors is known to be a very rapid step, this finding suggested that the G2 and G4 isoforms might be transported to the cell surface by two different mechanisms. This conclusion was supported by results from subcellular fractionation experiments. The ratio of G4/G2 membrane-bound acetylcholinesterase varied between different subcellular fractions. The membrane-bound G2 isoform was greatly enriched in a high-speed “microsomal” fraction. G4 acetylcholinesterase is known to be actively secreted by chromaffin cells in culture. Although the G4 isoform was present on the cell surface, most of the secreted enzyme was derived from an intracellular pool. Thus, it is unlikely that the cell-surface G4 isoform contributes significantly to the pool of secreted enzyme. Instead, the expression of two different membrane-bound isoforms may provide a means by which chromaffin cells can target the enzyme to different locations on the cell surface. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240550318
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