Molecular mechanisms involved in neuronal apoptosis induced by soluble oligomers of β-amyloid peptide: identification and functional validation of cellular targets.
Identifieur interne : 000423 ( Main/Exploration ); précédent : 000422; suivant : 000424Molecular mechanisms involved in neuronal apoptosis induced by soluble oligomers of β-amyloid peptide: identification and functional validation of cellular targets.
Auteurs : Ihsen Youssef [France]Source :
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English descriptors
Abstract
Aging of population is correlated to the increase of neurodegenerative disease, more particularly Alzheimer disease. Defining early diagnostic markers and new therapeutic strategies are highly relevant. Among the molecular pathways which are currently developed, N-terminal-truncated forms of amyloid-ß (Aß) peptide have been recently suggested to play a pivotal role in the disease. Among them, Aß3(pE) 42 peptide is the dominant Aß species in amyloid plaques. We first investigated the effects of soluble oligomeric Aß3(pE) 42 after intracerebroventricular injection on mice learning capacities and the molecular mechanisms of in vitro neurotoxicity. Mice injected with soluble Aß3(pE) 42 displayed impaired spatial working memory and delayed memory acquisition. These cognitive alterations were associated with free radical overproduction in hippocampus and olfactory bulbs. In vitro, Aß3(pE) 42 oligomers induced a redox-sensitive neuronal apoptosis involving caspase activation and an arachidonic acid-dependent pathway. The second goal of this work was to investigate the protective effects of the apoptosis rescue endogenous peptide humanin (HN) and its S14G mutant (HNG). In vitro, we measured their inhibitory effect on neuronal death and apoptotic events resulting from soluble Ab oligomer treatment. What's of particular interest is the in vivo restoration of soluble Aß3(pE) 42 oligomer-induced mnesic impairment. Thus, HN peptides might serve as new drug candidates for treatment or prevention of early cellular damages linked to soluble Aß oligomers.
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Affiliations:
- France
- Grand Est, Lorraine (région)
- Nancy
- Institut national polytechnique de Lorraine, Université de Lorraine
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transduction du signal</term><term>apoptose</term><term>apprentissage</term><term>comportement</term><term>humanine</term><term>maladie d'Alzheimer</term><term>mémoire</term><term>neurodégénérescence</term><term>neurotoxicité</term><term>oligomères solubles</term><term>peptide β-amyloïde</term><term>stratégies
thérapeutique</term><term>stratégies
thérapeutique.</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aging of population is correlated to the increase of neurodegenerative disease, more particularly Alzheimer disease. Defining early diagnostic markers and new therapeutic strategies are highly relevant. Among the molecular pathways which are currently developed, N-terminal-truncated forms of amyloid-ß (Aß) peptide have been recently suggested to play a pivotal role in the disease. Among them, Aß3(pE) 42 peptide is the dominant Aß species in amyloid plaques. We first investigated the effects of soluble oligomeric Aß3(pE) 42 after intracerebroventricular injection on mice learning capacities and the molecular mechanisms of in vitro neurotoxicity. Mice injected with soluble Aß3(pE) 42 displayed impaired spatial working memory and delayed memory acquisition. These cognitive alterations were associated with free radical overproduction in hippocampus and olfactory bulbs. In vitro, Aß3(pE) 42 oligomers induced a redox-sensitive neuronal apoptosis involving caspase activation and an arachidonic acid-dependent pathway. The second goal of this work was to investigate the protective effects of the apoptosis rescue endogenous peptide humanin (HN) and its S14G mutant (HNG). In vitro, we measured their inhibitory effect on neuronal death and apoptotic events resulting from soluble Ab oligomer treatment. What's of particular interest is the in vivo restoration of soluble Aß3(pE) 42 oligomer-induced mnesic impairment. Thus, HN peptides might serve as new drug candidates for treatment or prevention of early cellular damages linked to soluble Aß oligomers.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement><orgName><li>Institut national polytechnique de Lorraine</li><li>Université de Lorraine</li></orgName></list><tree><country name="France"><region name="Grand Est"><name sortKey="Youssef, Ihsen" sort="Youssef, Ihsen" uniqKey="Youssef I" first="Ihsen" last="Youssef">Ihsen Youssef</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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