Title :

Monomeric ß-amyloid interacts with type-1 insulin-like growth factor receptors to provide energy supply to neurons

Author(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]
Istituto Neurologico Mediterraneo [NEUROMED I.R.C.C.S.]
Università degli Studi di Roma "La Sapienza" = Sapienza University [Rome] [UNIROMA]
Copani, Agata [Auteur]

Journal title :

Frontiers in Cellular Neuroscience

Volume number :

9

Publication date :

2015-08-07

ISSN :

1662-5102

English keyword(s) :

Alzheimer’s disease
ß-amyloid
glucose
IGF-IR
Glut3

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Glycostress

Submission date :

2020-02-12T15:12:23Z
2021-05-07T12:30:04Z