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  • Blackwell Science Ltd  (11)
  • Blackwell Publishing Ltd  (7)
  • Berlin, Heidelberg :Springer Berlin / Heidelberg,  (2)
  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Aging-Molecular aspects-Congresses. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (212 pages)
    Edition: 1st ed.
    ISBN: 9783642842245
    Series Statement: Sitzungsberichte der Heidelberger Akademie der Wissenschaften Series ; v.1990 / 1990/2
    DDC: 574.372
    Language: English
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  • 2
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Population aging -- Germany. ; Population aging -- Social aspects. ; Aging -- Health aspects. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (178 pages)
    Edition: 1st ed.
    ISBN: 9783642143533
    Series Statement: Schriften der Mathematisch-Naturwissenschaftlichen Klasse Series ; v.21
    DDC: 612.67
    Language: German
    Note: Intro -- Vorwort -- Inhaltsverzeichnis -- Autorenverzeichnis -- Einleitung -- Teil I - Festvortrag -- Müssen, dürfen, sollen, können, oder wollen ältere Menschen noch arbeiten? -- 1 Müssen ältere Menschen noch arbeiten? -- 2 Dürfen ältere Menschen noch arbeiten? -- 3 Sollen ältere Menschen noch arbeiten? -- 4 Können ältere Menschen noch arbeiten? -- 5 Wollen ältere Menschen noch arbeiten? -- 6 Fazit -- Literaturhinweise -- Teil II - Prävention und Regeneration -- Mit körperlicher Aktivität das Altern gestalten -- 1 Perspektiven des Themas -- 2 Die Konstrukte -- 2.1 Gelingend Altern -- 2.2 Körperliche Aktivität -- 3 Präventive Wirkungen der körperlichen Aktivität im Alter -- 3.1 Aktivität, Aktivität im Alter und Sterblichkeit -- 3.2 Anpassungsvorgänge und gesteigerte Funktionstüchtigkeit -- 3.3 Körperliche Aktivität, psychische Gesundheit und Wohlbefinden -- 3.4 Körperliche Aktivität und „Teilhabe am Leben" -- 4 Ein Zwischenstand -- 5 Aktivitätsempfehlungen -- 6 Fazit -- Literaturverzeichnis -- Neuronale Plastizität bei gesundem und pathologischem Altern -- 1 Strukturelle und funktionelle Veränderungen im gesunden alternden Gehirn -- 2 Strukturelle Veränderungen im Gehirn bei gesundem Altern -- 3 Strukturelle Veränderungen bei MCI/AD -- 4 Funktionelle Veränderungen im Gehirn bei gesundem Altern -- 5 Funktionelle Veränderungen bei MCI/AD -- 6 Inhibition im Alter -- 7 Sensorik und Sensomotorik im Alter -- 8 Kann die kognitive Leistungsfähigkeit im Alter erhalten oder verbessert werden? -- 9 Kognitive Trainings bei gesundem Altern -- 10 Kognitive Trainings bei leichter kognitiver Beeinträchtigung im Alter und bei Demenz -- 11 Körperliche Aktivität im Alter -- 12 Körperliche Trainings bei gesundem Altern -- 13 Körperliche Aktivität bei leichter kognitiver Beeinträchtigung im Alter und bei Demenz. , 14 Synergieeffekte von kombiniertem kognitiven und körperlichen Training -- 15 Sensorische und sensorimotorische Trainings -- 16 Zusammenfassung und Ausblick -- Literaturverzeichnis -- Teil III - Biologische und technischeAssistenzsysteme -- Das Altern im Spiegelbild der Stammzellen - Irrwege und Auswege -- 1 Stammzellen als Hoffnungsträger der modernen Medizin -- 2 Entwicklung der Stammzellforschung -- 3 Kampf der Kulturen - Adulte und embryonale Stammzellen -- 4 Die Heilkraft adulter Stammzellen -- 5 Einsatz von Stammzellen in der Regenerativen Medizin -- 6 Regeneration von Gewebe im Reagenzglas -- 7 Stammzellen und Altern -- 8 Interaktion mit der Stammzellnische -- 9 Induzierte Pluripotente Stammzellen -- 10 Lektionen aus der Stammzellforschung -- 11 Fazit und Ausblick -- Literaturverzeichnis -- Elektronische Systeme zum Ersatz der defizienten Hörleistung -- 1 Funktionen des Hörens -- 2 Lärmexposition als Ursache der Schwerhörigkeit -- 3 Ausfall des cochleären Verstärkers -- 4 Implantierbare Hörsysteme -- 5 Teilimplantierbare Hörsysteme -- 6 Ausfall der Transduktion: Cochlea Implantat -- 7 Hörverlust im Alter -- 8 Hybridversorgung bei erhaltenem Tiefton-Restgehör -- 9 Zusammenfassung -- Literaturverzeichnis -- Endoprothetik und Alter - Lebensqualität oder Übertherapie? -- 1 Einführung -- 2 Endoprothetische Ersatzoperation bei Verschleißerkrankungen großer Gelenke -- 2.1 Hüftgelenk -- 2.2 Kniegelenk -- 2.3 Schultergelenk -- 2.4 Ellbogengelenk -- 2.5 Sprunggelenke -- 3 Endoprothetische Ersatzoperationen bei frischer Gelenkverletzung oder posttraumatischer Arthrose -- 3.1 Hüftgelenk -- 3.2 Kniegelenk -- 3.3 Schultergelenk -- 3.4 Ellbogengelenk -- 3.5 Sprunggelenk -- 4 Zusammenfassung -- Literaturverzeichnis -- Teil IV - Unterstützende Systeme in Technik, Umwelt und Pflege -- Fahrzeugentwicklung für eine Gesellschaft im demografischen Wandel. , 1 Einleitung -- 2 Mobilität im Alter -- 2.1 Bedeutung des Individualverkehrs -- 2.2 Verkehrsauffälligkeit in Abhängigkeit vom Alter -- 3 Automobilentwicklung für ältere Fahrzeugführer -- 3.1 Herausforderungen und Innovationsfelder -- 3.2 Hilfsmittel bei der Fahrzeugentwicklung -- 3.3 Angebote zur Unterstützung älterer Fahrzeugführer -- 4 Neuartiger ganzheitlicher Entwicklungsansatz -- 4.1 Strategien zur Kompensation der kognitiven und reaktiven Defizite von Fahrzeugführern -- 4.2 Sensierung fahrerischer Defizite -- 4.2.1 Bestimmung fahrerischer Defizite mittels Probandenbefragungenund Messfahrten -- 4.2.2 Bestimmung altersbedingter Sehdefizite -- 4.3 Entwicklung einer Korrektur-Methodik -- 5 Zusammenfassung und Ausblick -- Literatur/Quellen -- Wohnen im Alter - Herausforderung für Stadtplanung, Architektur und Wohnungswirtschaft -- 1 Einleitung -- 2 Altersgerecht - barrierearm - barrierefrei -- 3 Versorgungssicherheit im Quartier -- 4 Zurück in die Stadt? -- 5 NeueWohnformen -- 6 Zusammenfassung -- Literaturverzeichnis -- Pflegerische Versorgung und Erhalt der Selbständigkeit im Alter -- 1 Einleitung -- 2 Altern und Gewinn an Gesundheit -- 3 Altern und Pflegebedürftigkeit als besondere Anforderung an die Versorgung -- 4 Pflegerische Versorgungsanforderungen und Erhalt der Selbständigkeit -- 5 Fazit -- Literaturverzeichnis -- Teil V - Einblick und Ausblick -- Chancen gesunden Alterns aus soziologischer Sicht -- 1 Einleitung -- 2 Gesundheitliche Ungleichheit im höheren Lebensalter -- 3 Hemmnisse auf dem Weg zu gesundem Altern -- 4 Gesellschaftspolitische Folgerungen -- 5 Zusammenfassung -- Literaturverzeichnis -- Menschliches Sozialverhalten von der Jugend bis ins Alter - Genetische und Gehirnmechanismen -- 1 Neurogenetik des menschlichen Sozialverhaltens -- 2 Ein instruktives „Experiment der Natur": das Williams-Beuren-Syndrom. , 3 Häufige genetische Varianten beeinflussen menschliche Gewaltbereitschaften -- 4 Mechanismen von Gen-Umwelt-Interaktionen -- 5 Verarbeitung des sozialen Status im menschlichen Gehirn -- 6 Gehirnmechanismen des Sozialverhaltens im Alter -- 7 Fazit -- Literaturverzeichnis -- Cicero, Jacob Grimm, Ernst Bloch - Drei Bilder von derWürde des Alters -- 1 Cicero: Die erste Altersstudie -- 2 Jacob Grimm: Vom Glück des Älterwerdens -- 3 Ernst Bloch: Zeit der Ernte -- Literaturverzeichnis.
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  • 3
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The binding of the amyloid protein precursor (APP) to heparan sulfate proteoglycans has been shown to stimulate the neurite-promoting activity of APP. In this study, proteoglycans that bind with high affinity to APP were characterized. Conditioned medium from cultures of postnatal day 3 mouse brain cells was applied to an affinity column containing a peptide homologous to a heparin-binding domain of APP. A fraction 17-fold enriched in proteoglycans was recovered by elution with a salt gradient. APP bound saturably and with high affinity to the affinity-purified proteoglycan fraction. Scatchard analysis of the binding showed that APP bound to high- and low-affinity sites with equilibrium dissociation constants of 1.4 × 10−11 and 6.5 × 10−10M, respectively. APP, in conjunction with the affinity-purified proteoglycan fraction, promoted neurite outgrowth. The affinity-purified proteoglycan fraction contained a heparan sulfate proteoglycan and a chondroitin sulfate proteoglycan. Digestion of the affinity-purified fraction with heparitinase I revealed a core protein of 63–69-kDa molecular mass, whereas digestion with chondroitinase ABC revealed a core protein of 100–110 kDa. The results suggest that expression of specific APP-binding proteoglycans may be an important step in the regulation of the neurite outgrowth-promoting activity of APP.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The major component of the amyloid deposition that characterizes Alzheimer's disease is the 4-kDa βA4 protein, which is derived from a much larger amyloid protein precursor (APP). A procedure for the complete purification of APP from human brain is described. The same amino terminal sequence of APP was found in two patients with Alzheimer's disease and one control subject. Two major forms of APP were identified in human brain with apparent molecular masses of 100–110 kDa and 120–130 kDa. Soluble and membrane fractions of brain contained nearly equal amounts of APP in both humans and rats. Immunoprecipitation with carboxyl terminus-directed antibodies indicates that the soluble forms of APP are truncated. Carboxyl terminus truncation of membrane-associated forms of human brain APP was also found to occur during postmortem autolysis. The availability of purified human brain APP will facilitate the investigation of its normal function and the events that lead to its abnormal cleavage in patients with Alzheimer's disease.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Recent studies have shown that the binding of the amyloid protein precursor (APP) of Alzheimer's disease to heparan sulfate proteoglycans (HSPGs) can modulate a neurite outgrowth-promoting function associated with APP. We used three different approaches to identify heparin-binding domains in APP. First, as heparin-binding domains are likely to be within highly folded regions of proteins, we analyzed the secondary structure of APP using several predictive algorithms. This analysis showed that two regions of APP695 contain a high degree of secondary structure, and clusters of basic residues, considered mandatory for heparin binding, were found principally within these regions. To determine which domains of APP bind heparin, deletion mutants of APP695 were prepared and analyzed for binding to a heparin affinity column. The results suggested that there must be at least two distinct heparin-binding regions in APP. To identify novel heparin-binding regions, peptides homologous to candidate heparin-binding domains were analyzed for their ability to bind heparin. These experiments suggested that APP contains at least four heparin-binding domains. The presence of more than one heparin-binding domain on APP suggests the possibility that APP may interact with more than one type of glycosaminoglycan.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: One of the characteristic changes that occurs in Alzheimer's disease is the loss of acetylcholinesterase (AChE) from both cholinergic and noncholinergic neurons of the brain. However, AChE activity is increased around amyloid plaques. This increase in AChE may be of significance for therapeutic strategies using AChE inhibitors. The aim of this study was to examine the effect of amyloid β-protein (Aβ), the major component of amyloid plaques, on AChE expression. Aβ peptides spanning residues 1–40 or 25–35 increased AChE activity in P19 embryonal carcinoma cells. A peptide containing a scrambled Aβ25–35 sequence did not stimulate AChE expression. To examine the possibility that the increase in AChE expression was mediated by an influx of calcium through voltage-dependent calcium channels (VDCCs), drugs acting on VDCCs were tested for their effects. Inhibitors of L-type VDCCs (diltiazem, nifedipine, and verapamil), but not N- or P- or Q-type VDCCs, resulted in a decrease in AChE expression. Agonists of L-type VDCCs (maitotoxin and S(−)-Bay K 8644) increased AChE expression. As L-type VDCCs are known to be modulated by cyclic AMP-dependent protein kinase, the effect of the adenylate cyclase activator forskolin was also examined. Forskolin stimulated AChE expression, an action that was blocked by the L-type VDCC antagonist nifedipine. The Aβ25–35-induced increase in AChE expression was mediated by an L-type VDCC, as the effect was also blocked by nifedipine. The results suggest that the increase in AChE expression around amyloid plaques could be due to a disturbance in calcium homeostasis involving the opening of L-type VDCCs.
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  • 8
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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