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Processing of wild-type and mutant familial Alzheimer's disease-associated presenilin-1 in cultured neurons.
Weihl, C C; Ghadge, G D; Miller, R J; Roos, R P.
Afiliación
  • Weihl CC; Committee on Neurobiology, University of Chicago, Illinois 60637, USA.
J Neurochem ; 73(1): 31-40, 1999 Jul.
Article en En | MEDLINE | ID: mdl-10386952
Mutations of presenilin (PS)-1, an endoplasmic reticulum/Golgi transmembrane protein, have been associated with early-onset familial Alzheimer's disease (FAD). In mammalian brain, PS1 exists primarily as its processed fragments; however, the role of this cleavage event in PS1 function remains unclear. Although some investigators have shown that mutant PS1 processing is unaltered (with the exception of PS1-deltaE9, which lacks the cleavage site) in stably transfected cells and PS1-FAD transgenic mice, other investigators have reported altered FAD mutant PS1 and PS2 protein processing in transiently transfected cells and human FAD patients. The present study uses recombinant replication-defective adenoviral vectors to transiently express wild-type (WT) or mutant PS1 in various cells, including primary cultured hippocampal neurons. We show that in contrast to PS1-WT, overexpression of mutant PS1 results in an increased ratio of mutant holoprotein to endoproteolytic products that is dependent on cell type and differentiation state. In addition, mutant PS1 overexpression leads to an increase in caspase-type protease derived fragments above that seen with PS1-WT overexpression. Furthermore, overexpression of at least one mutant significantly alters the processing of coexpressed PS1-WT, suggesting that mutant PS1 may affect PS1-WT function. These findings suggest that a defect in PS1 holoprotein stability may be a general defect seen in cells expressing mutant PS1, especially neuronal cells, and may play a critical role in the pathogenesis of FAD.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedad de Alzheimer / Proteínas de la Membrana / Mutación Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedad de Alzheimer / Proteínas de la Membrana / Mutación Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido