http://www.cnr.it/ontology/cnr/individuo/prodotto/ID5008

Nerve growth factor as a paradigm of neurotrophins related to Alzheimer's disease (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

Nerve growth factor as a paradigm of neurotrophins related to Alzheimer's disease (Articolo in rivista) (literal)

Anno

2010-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1002/dneu.20759 (literal)

Alternative label

P. Calissano,1,2; C. Matrone 1; G. Amadoro1 (2010)
Nerve growth factor as a paradigm of neurotrophins related to Alzheimer's disease
in Developmental neurobiology (Hoboken, N.J.)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

P. Calissano,1,2; C. Matrone 1; G. Amadoro1 (literal)

Pagina inizio

372 (literal)

Pagina fine

383 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

70 (literal)

Rivista

Developmental neurobiology (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

5 (literal)

Note

ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1 Institute of Neurobiology and Molecular Medicine, C.N.R. Fondazione Santa Lucia, Italy 2 European Brain Research Institute, Via Fosso del Fiorano, 64-65 00143, Roma, ItalyInstitute of (literal)

Titolo

Nerve growth factor as a paradigm of neurotrophins related to Alzheimer's disease (literal)

Abstract

Converging lines of evidence on the possible connection between NGF signaling and Alzheimer's diseases (AD) are unraveling new facets which could depict this neurotrophin (NTF) in a more central role. AD animal models have provided evidence that a shortage of NGF supply may induce an AD-like syndrome. In vitro experiments, moreover, are delineating a possible temporal and causal link between APP amiloydogenic processing and altered post-translational tau modifications. After NGF signaling interruption, the pivotal upstream players of the amyloid cascade (APP, ²-secretase, and active form of ³-secretase) are up-regulated, leading to an increased production of amyloid ² peptide (A²) and to its intracellular aggregation in molecular species of different sizes. Contextually, the A² released pool generates an autocrine toxic loop in the same healthy neurons. At the same time tau protein undergoes anomalous, GSK²-mediated, phosphorylation at specific pathogenetic sites (Ser262 and Thr 231), caspase(s) and calpain- I- mediated truncation, detachment from microtubules with consequent cytoskeleton collapse and axonal transport impairment. All these events are inhibited when the amyloidogenic processing is reduced by ² and ³ secretase inhibitors or anti-A² antibodies and appear to be causally correlated to TrkA, p75CTF, A², and PS1 molecular association in an A²-mediated fashion. In this scenario, the so-called trophic action exerted by NGF (and possibly also by other neurotrophins) in these targets neurons is actually the result of an anti-amyloidogenic activity. (literal)

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