Cell Biology: Research & TherapyISSN: 2324-9293

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Review Article, Cell Biol Res Ther Vol: 2 Issue: 2

NGF and APP Interplay: Focus on YENPTY Motif of Amyloid Precursor Protein and Y682 Residue

Basso E1* and Matrone C2
1Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisboa, Portugal
2Department of Medical Biochemistry, University of Aarhus, 8000 Aarhus C, Denmark
Corresponding author : Elisa Basso
Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisboa, Portugal
E-mail: [email protected]
Received: July 04, 2013 Accepted: November 13, 2013 Published: November 19, 2013
Citation: Basso E, Matrone C (2013) Ngf and App Interplay: Focus on Yenpty Motif of Amyloid Precursor Protein and Y682 Residue. Cell Biol: Res Ther 2:2. doi:10.4172/2324-9293.1000106

Abstract

NGF and APP Interplay: Focus on YENPTY Motif of Amyloid Precursor Protein and Y682 Residue

Cholinergic deficits originated from NGF metabolism disruption, represent one of the early changes in Alzheimer’s disease, where abnormal deposition of β-amyloid peptide (Aβ) and phosphorylated Tau define the neuropathological hallmarks of the disorder. A failure in NGF maturation can promote pro-apoptotic pathway activation, through p75 receptor; while lack of NGF signalling can generate an atypical TrkA receptor phosphorylation resulting in neuronal cell death and Aβ toxicity. These evidences suggest a complex interaction between TrkA, p75, and Aβ, whose exact cellular mechanisms remain still elusive. Here, we provide a general overview on the current knowledge on NGF and APP interplay, focusing on the events that mediate NGF signalling impairment, and, mostly, on the role of APP Tyrosine 682 phosphorylation whose absence in APPY682G mice impairs APP/TrkA interaction and leads to cholinergicneurodegeneration.

Keywords: APP; NGF; Neurodegeneration; Tyrosine phosphorylation; Alzheimerís disease; YENPTY

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