Monomeric ß-amyloid interacts with type-1 ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Monomeric ß-amyloid interacts with type-1 insulin-like growth factor receptors to provide energy supply to neurons
Auteur(s) :
Giuffrida, Maria L. [Auteur]
Tomasello, Marianna F. [Auteur]
Pandini, Giuseppe [Auteur]
Caraci, Filippo [Auteur]
Istituti di Ricovero e Cura a Carattere Scientifico [IRCCS]
Battaglia, Giuseppe [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Busceti, Carla [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Di Pietro, Paola [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Pappalardo, Giuseppe [Auteur]
Attanasio, Francesco [Auteur]
Chiechio, Santina [Auteur]
Bagnoli, Silvia [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Nacmias, Benedetta [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Sorbi, Sandro [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Vigneri, Riccardo [Auteur]
Rizzarelli, Enrico [Auteur]
Nicoletti, Ferdinando [Auteur]
Università degli Studi di Roma "La Sapienza" = Sapienza University [Rome] [UNIROMA]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Copani, Agata [Auteur]
Tomasello, Marianna F. [Auteur]
Pandini, Giuseppe [Auteur]
Caraci, Filippo [Auteur]
Istituti di Ricovero e Cura a Carattere Scientifico [IRCCS]
Battaglia, Giuseppe [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Busceti, Carla [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Di Pietro, Paola [Auteur]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Pappalardo, Giuseppe [Auteur]
Attanasio, Francesco [Auteur]
Chiechio, Santina [Auteur]
Bagnoli, Silvia [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Nacmias, Benedetta [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Sorbi, Sandro [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Vigneri, Riccardo [Auteur]
Rizzarelli, Enrico [Auteur]
Nicoletti, Ferdinando [Auteur]
Università degli Studi di Roma "La Sapienza" = Sapienza University [Rome] [UNIROMA]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Copani, Agata [Auteur]
Titre de la revue :
Frontiers in Cellular Neuroscience
Numéro :
9
Date de publication :
2015-08-07
ISSN :
1662-5102
Mot(s)-clé(s) en anglais :
Alzheimer’s disease
ß-amyloid
glucose
IGF-IR
Glut3
ß-amyloid
glucose
IGF-IR
Glut3
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
ß-amyloid (Aß1−42) is produced by proteolytic cleavage of the transmembranetype-1 protein, amyloid precursor protein. Under pathological conditions,Aß1−42self-aggregates into oligomers, which cause synaptic dysfunction ...
Lire la suite >ß-amyloid (Aß1−42) is produced by proteolytic cleavage of the transmembranetype-1 protein, amyloid precursor protein. Under pathological conditions,Aß1−42self-aggregates into oligomers, which cause synaptic dysfunction and neuronalloss, and are considered the culprit of Alzheimer’s disease (AD). However, Aß1−42ismainly monomeric at physiological concentrations, and the precise role of monomericAß1−42in neuronal function is largely unknown. We report that the monomer ofAß1−42activates type-1 insulin-like growth factor receptors and enhances glucoseuptake in neurons and peripheral cells by promoting the translocation of theGlut3 glucose transporter from the cytosol to the plasma membrane. In neurons,activity-dependent glucose uptake was blunted after blocking endogenous Aßproduction, and re-established in the presence of cerebrospinal fluid Aß. APP-nullneurons failed to enhance depolarization-stimulated glucose uptake unless exogenousmonomeric Aß1−42was added. These data suggest that Aß1−42monomers werecritical for maintaining neuronal glucose homeostasis. Accordingly, exogenous Aß1−42monomers were able to rescue the low levels of glucose consumption observed in brainslices from AD mutant mice.Lire moins >
Lire la suite >ß-amyloid (Aß1−42) is produced by proteolytic cleavage of the transmembranetype-1 protein, amyloid precursor protein. Under pathological conditions,Aß1−42self-aggregates into oligomers, which cause synaptic dysfunction and neuronalloss, and are considered the culprit of Alzheimer’s disease (AD). However, Aß1−42ismainly monomeric at physiological concentrations, and the precise role of monomericAß1−42in neuronal function is largely unknown. We report that the monomer ofAß1−42activates type-1 insulin-like growth factor receptors and enhances glucoseuptake in neurons and peripheral cells by promoting the translocation of theGlut3 glucose transporter from the cytosol to the plasma membrane. In neurons,activity-dependent glucose uptake was blunted after blocking endogenous Aßproduction, and re-established in the presence of cerebrospinal fluid Aß. APP-nullneurons failed to enhance depolarization-stimulated glucose uptake unless exogenousmonomeric Aß1−42was added. These data suggest that Aß1−42monomers werecritical for maintaining neuronal glucose homeostasis. Accordingly, exogenous Aß1−42monomers were able to rescue the low levels of glucose consumption observed in brainslices from AD mutant mice.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Glycostress
Date de dépôt :
2020-02-12T15:12:23Z
2021-05-07T12:30:04Z
2021-05-07T12:30:04Z
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