http://www.cnr.it/ontology/cnr/individuo/prodotto/ID285192
Insulin induces phosphorylation of the AMPA receptor subunit GluR1, reversed by ZIP, and over-expression of Protein Kinase M zeta, reversed by amyloid beta. (Articolo in rivista)
- Type
- Label
- Insulin induces phosphorylation of the AMPA receptor subunit GluR1, reversed by ZIP, and over-expression of Protein Kinase M zeta, reversed by amyloid beta. (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1111/jnc.12947 (literal)
- Alternative label
Adzovic L, Domenici L. (2014)
Insulin induces phosphorylation of the AMPA receptor subunit GluR1, reversed by ZIP, and over-expression of Protein Kinase M zeta, reversed by amyloid beta.
in Journal of neurochemistry
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Adzovic L, Domenici L. (literal)
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- ISTITUTO NEUROSCIENZE CNR (literal)
- Titolo
- Insulin induces phosphorylation of the AMPA receptor subunit GluR1, reversed by ZIP, and over-expression of Protein Kinase M zeta, reversed by amyloid beta. (literal)
- Abstract
- Abstract
Insulin receptor (IR) in the brain plays a role in synaptic plasticity
and cognitive functions. Phosphorylation of a-amino-3-hydroxy-
5-methylisoxazole-4-propionic acid (AMPA) receptors GluR1
subunit at Serine 831 is regulated by calcium-calmodulindependent
protein kinase II and protein kinase C that underlie
long-term potentiation and learning/memory. Recent studies
have shown that the novel Protein Kinase M zeta (PKMf)
underlies synaptic plasticity and may regulate AMPAr. In this
study, we show that insulin induces phosphorylation of Serine
831 GluR1 subunit of AMPAr and induces over-expression of
PKMf; pre-treatment with either the IR inhibitor 3-Bromo-5-tbutyl-
4-hydroxy-benzylidenemalonitrile (AG1024) or PKMf
inhibitor protein kinase C zeta pseudo-substrate inhibitor
returned the phosphorylation value of GluR1 to control level.
Amyloid beta (Ab) peptide in the form of oligomers interferes
with IR signaling. Pre-treating neuronal cultures with Ab
following incubation with insulin, we found a reduction of
insulin-dependent PKMf over-expression and MAPK/Erk (1/2)
phosphorylation, i.e., signaling pathways involved in synaptic
plasticity and learning/memory. These results indicate a new
intracellular insulin signaling pathway, and, additionally, that
insulin resistance in Alzheimer's disease is a response to the
production and accumulation of Ab. (literal)
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