RESUMO

Amyloid precursor protein (APP) is a key player in Alzheimer's disease. The proteolytic cleavage of APP results in various short peptide fragments including the toxic amyloid-beta peptide, which is a main component of senile plaques. However, the functions of APP and its processed fragments are not yet well understood. Here, using real-time polymerase chain reaction, we demonstrate that exogenous expression of APP, its mutant form APP-Swedish, or two truncated forms in Drosophila melanogaster causes a significant (P ≤ 0.05) drop in the mRNA levels of the presynaptic proteins synaptotagmin-1 and neuronal synaptobrevin. The results obtained from this study suggest a potential role of APP or its fragments in the regulation of synaptic gene transcription.

Assuntos

Precursor de Proteína beta-Amiloide/genética , Drosophila melanogaster/genética , Expressão Gênica , Neurônios/metabolismo , Terminações Pré-Sinápticas/metabolismo , RNA Mensageiro/genética , Precursor de Proteína beta-Amiloide/metabolismo , Animais , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/metabolismo , Humanos , Presenilinas/genética , Presenilinas/metabolismo , Proteínas R-SNARE/genética , Proteínas R-SNARE/metabolismo , Sinaptotagmina I/genética , Sinaptotagmina I/metabolismo