Clinical, Neuropathologic, and Biochemical Profile of the Amyloid Precursor Protein 1716F Mutation

We report the clinical, pathologic, and biochemical characteristics of the recently described amyloid precursor protein (APP) 1716F mutation. We present the clinical findings of individuals carrying the APP 1716F mutation and the neuropathologic examination of the proband. The mutation was found in...

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Detalles Bibliográficos
Autores: Guardia-Laguarta, C, Pera, M, Clarimon, J, Molinuevo, JL, Sanchez-Valle, R, Llado, A, Coma, M, Gomez-Isla, T, Blesa, R, Ferrer, I, Lleo, A
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2010
País:España
Institución:Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)
Repositorio:r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
OAI Identifier:oai:iibsantpau.fundanetsuite.com:p12905
Acceso en línea:https://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=12905
Access Level:acceso abierto
Palabra clave:alpha-Synuclein
gamma-Secretase
Alzheimer disease
Amyloid
APP mutations
Genetics
Descripción
Sumario:We report the clinical, pathologic, and biochemical characteristics of the recently described amyloid precursor protein (APP) 1716F mutation. We present the clinical findings of individuals carrying the APP 1716F mutation and the neuropathologic examination of the proband. The mutation was found in a patient with Alzheimer disease with onset at the age of 31 years and death at age 36 years and who had a positive family history of early-onset Alzheimer disease. Neuropathologic examination showed abundant diffuse amyloid plaques mainly composed of amyloid-beta(42) and widespread neurofibrillary pathology. Lewy bodies were found in the amygdala. Chinese hamster ovary cells transfected with this mutation showed a marked increase in the amyloid-beta(42/40) ratio and APP C-terminal fragments and a decrease in APP intracellular domain production, suggesting reduced APP proteolysis by gamma-secretase. Taken together, these findings indicate that the APP 1716F mutation is associated with the youngest age of onset for this locus and strengthen the inverse association between amyloid-beta(42/40) ratio and age of onset. The mutation leads to a protein that is poorly processed by gamma-secretase. This loss of function may be an additional mechanism by which some mutations around the gamma-secretase cleavage site lead to familial Alzeheimer disease.