Alzheimer Disease: Therapeutic Strategies
Since the apoE4 allele is a risk factor or susceptibility gene in late-onset familial and sporadic AD, the mechanism of disease expression may involve metabolic effects that are isoform specific. Isoform-specific interactions of apoE therefore become critical in the mechanism of AD pathogenesis. Det...
Gespeichert in:
| Weitere Verfasser: | , |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Boston, MA
Birkhäuser Boston
1994
|
| Schriftenreihe: | Advances in Alzheimer Disease Therapy
|
| Schlagworte: | |
| Online-Zugang: | UBR01 Volltext |
| Zusammenfassung: | Since the apoE4 allele is a risk factor or susceptibility gene in late-onset familial and sporadic AD, the mechanism of disease expression may involve metabolic effects that are isoform specific. Isoform-specific interactions of apoE therefore become critical in the mechanism of AD pathogenesis. Detailed characterization of the binding of the apoE isoforms with proteins and peptides relevant to the pathology of the disease may be critical in understanding disease pathogenesis. These critical isoform-specific interactions of apoE may involve interactions with proteins and pep tides in the defining neuropathologic lesions of the disease, the neurofibrillary tangle and senile plaque. Other possible critical isoform-specific interactions include the mechanism of internalization, intracellular trafficking, and subsequent metabolism. In addition, differential post-translational modifications of apoE isoforms may determine differences in metabolism contributing to the pathogenesis of the disease. Oxidation of apoE may confer several isoform-specific, biochemically distinct properties. Since {3A peptide binds apoE in the lipoprotein binding domain of the protein and not in the receptor-binding domain, apoE could target bound {3A4 peptide to neurons via the LRP receptor. Internalization of the apoEI {3A peptide complex into the cell, by the same route as the apoE-containing lipoproteins, would result in incorporation into primary lysosomes and pH dependent dissociation. The demonstration of apoE in the cytoplasm of neurons, with isoform-specific interactions of apoE with the microtubule-binding protein tau demonstrated in vitro, suggest additional, testable hypotheses of disease pathogenesis |
| Beschreibung: | 1 Online-Ressource (XVI, 510 p. 29 illus., 2 illus. in color) |
| ISBN: | 9781461581499 |
| DOI: | 10.1007/978-1-4615-8149-9 |
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| 520 | |a Since the apoE4 allele is a risk factor or susceptibility gene in late-onset familial and sporadic AD, the mechanism of disease expression may involve metabolic effects that are isoform specific. Isoform-specific interactions of apoE therefore become critical in the mechanism of AD pathogenesis. Detailed characterization of the binding of the apoE isoforms with proteins and peptides relevant to the pathology of the disease may be critical in understanding disease pathogenesis. These critical isoform-specific interactions of apoE may involve interactions with proteins and pep tides in the defining neuropathologic lesions of the disease, the neurofibrillary tangle and senile plaque. Other possible critical isoform-specific interactions include the mechanism of internalization, intracellular trafficking, and subsequent metabolism. In addition, differential post-translational modifications of apoE isoforms may determine differences in metabolism contributing to the pathogenesis of the disease. Oxidation of apoE may confer several isoform-specific, biochemically distinct properties. Since {3A peptide binds apoE in the lipoprotein binding domain of the protein and not in the receptor-binding domain, apoE could target bound {3A4 peptide to neurons via the LRP receptor. Internalization of the apoEI {3A peptide complex into the cell, by the same route as the apoE-containing lipoproteins, would result in incorporation into primary lysosomes and pH dependent dissociation. The demonstration of apoE in the cytoplasm of neurons, with isoform-specific interactions of apoE with the microtubule-binding protein tau demonstrated in vitro, suggest additional, testable hypotheses of disease pathogenesis | ||
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Datensatz im Suchindex
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| author2 | Giacobini, Ezio 1929- Becker, Robert E. 1934- |
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| author_facet | Giacobini, Ezio 1929- Becker, Robert E. 1934- |
| building | Verbundindex |
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| discipline | Medizin |
| doi_str_mv | 10.1007/978-1-4615-8149-9 |
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| id | DE-604.BV046143586 |
| illustrated | Not Illustrated |
| indexdate | 2024-07-10T08:36:23Z |
| institution | BVB |
| isbn | 9781461581499 |
| language | English |
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| physical | 1 Online-Ressource (XVI, 510 p. 29 illus., 2 illus. in color) |
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| publishDate | 1994 |
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| publisher | Birkhäuser Boston |
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| series2 | Advances in Alzheimer Disease Therapy |
| spelling | Alzheimer Disease Therapeutic Strategies edited by Ezio Giacobini, Robert E. Becker Boston, MA Birkhäuser Boston 1994 1 Online-Ressource (XVI, 510 p. 29 illus., 2 illus. in color) txt rdacontent c rdamedia cr rdacarrier Advances in Alzheimer Disease Therapy Since the apoE4 allele is a risk factor or susceptibility gene in late-onset familial and sporadic AD, the mechanism of disease expression may involve metabolic effects that are isoform specific. Isoform-specific interactions of apoE therefore become critical in the mechanism of AD pathogenesis. Detailed characterization of the binding of the apoE isoforms with proteins and peptides relevant to the pathology of the disease may be critical in understanding disease pathogenesis. These critical isoform-specific interactions of apoE may involve interactions with proteins and pep tides in the defining neuropathologic lesions of the disease, the neurofibrillary tangle and senile plaque. Other possible critical isoform-specific interactions include the mechanism of internalization, intracellular trafficking, and subsequent metabolism. In addition, differential post-translational modifications of apoE isoforms may determine differences in metabolism contributing to the pathogenesis of the disease. Oxidation of apoE may confer several isoform-specific, biochemically distinct properties. Since {3A peptide binds apoE in the lipoprotein binding domain of the protein and not in the receptor-binding domain, apoE could target bound {3A4 peptide to neurons via the LRP receptor. Internalization of the apoEI {3A peptide complex into the cell, by the same route as the apoE-containing lipoproteins, would result in incorporation into primary lysosomes and pH dependent dissociation. The demonstration of apoE in the cytoplasm of neurons, with isoform-specific interactions of apoE with the microtubule-binding protein tau demonstrated in vitro, suggest additional, testable hypotheses of disease pathogenesis General Practice / Family Medicine Family medicine Therapie (DE-588)4059798-2 gnd rswk-swf Alzheimerkrankheit (DE-588)4112510-1 gnd rswk-swf Pharmakotherapie (DE-588)4076066-2 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Alzheimerkrankheit (DE-588)4112510-1 s Therapie (DE-588)4059798-2 s DE-604 Pharmakotherapie (DE-588)4076066-2 s Giacobini, Ezio 1929- (DE-588)114737282 edt Becker, Robert E. 1934- (DE-588)138028109 edt Erscheint auch als Druck-Ausgabe 9780817637576 Erscheint auch als Druck-Ausgabe 9781461581505 Erscheint auch als Druck-Ausgabe 9781461581512 https://doi.org/10.1007/978-1-4615-8149-9 Verlag URL des Erstveröffentlichers Volltext |
| spellingShingle | Alzheimer Disease Therapeutic Strategies General Practice / Family Medicine Family medicine Therapie (DE-588)4059798-2 gnd Alzheimerkrankheit (DE-588)4112510-1 gnd Pharmakotherapie (DE-588)4076066-2 gnd |
| subject_GND | (DE-588)4059798-2 (DE-588)4112510-1 (DE-588)4076066-2 (DE-588)4143413-4 |
| title | Alzheimer Disease Therapeutic Strategies |
| title_auth | Alzheimer Disease Therapeutic Strategies |
| title_exact_search | Alzheimer Disease Therapeutic Strategies |
| title_full | Alzheimer Disease Therapeutic Strategies edited by Ezio Giacobini, Robert E. Becker |
| title_fullStr | Alzheimer Disease Therapeutic Strategies edited by Ezio Giacobini, Robert E. Becker |
| title_full_unstemmed | Alzheimer Disease Therapeutic Strategies edited by Ezio Giacobini, Robert E. Becker |
| title_short | Alzheimer Disease |
| title_sort | alzheimer disease therapeutic strategies |
| title_sub | Therapeutic Strategies |
| topic | General Practice / Family Medicine Family medicine Therapie (DE-588)4059798-2 gnd Alzheimerkrankheit (DE-588)4112510-1 gnd Pharmakotherapie (DE-588)4076066-2 gnd |
| topic_facet | General Practice / Family Medicine Family medicine Therapie Alzheimerkrankheit Pharmakotherapie Aufsatzsammlung |
| url | https://doi.org/10.1007/978-1-4615-8149-9 |
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