Presenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLP
نویسندگان
چکیده
Raphaëlle Pardossi-Piquard,1 Agnès Petit,1 Toshitaka Kawarai,2 Claire Sunyach,1 Cristine Alves da Costa,1 Bruno Vincent,1 Sabine Ring,3 Luciano D’Adamio,4,5 Jie Shen,6 Ulrike Müller,3 Peter St. George Hyslop,2 and Frédéric Checler1,* 1Institut de Pharmacologie Moléculaire et Cellulaire Centre National de la Recherche Scientifique UMR6097 CNRS/UNSA Valbonne 06560 France 2Centre for Research in Neurodegenerative Diseases Department of Medicine University of Toronto and University Health Network Toronto Western Hospital Research Institute 6 Queen’s Park Crescent Toronto, Ontario M5S 3H2 Canada 3 Institute for Pharmacy and Molecular Biotechnology University of Heidelberg 69120 Heidelberg Germany 4Albert Einstein College of Medicine New York, New York 5Dipartimento di Biochimica e Biotecnologie Mediche Universita’ Degli Studi di Napoli Federico II Napoli Italy 6Center for Neurologic Diseases Harvard Medical School Boston, Massachusetts
منابع مشابه
Response to: Pardossi-Piquard et al., “Presenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLP.” Neuron 46, 541–554
Pardossi-Piquard et al. (2005) recently reported that the processing of APP by the presenilin/g-secretase complex to release the APP intracellular domain (AICD) allows the latter to upregulate the cellular expression of neprilysin. The authors emphasized the biological elegance of thisnovel feedbackmechanism in that a by-product (AICD) of thegeneration of amyloid b protein (Ab) increases the le...
متن کاملResponse to Correspondence: Pardossi-Piquard et al., “Presenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLP.” Neuron 46, 541–554
Raphaëlle Pardossi-Piquard, Julie Dunys, Toshitaka Kawarai, Claire Sunyach, Cristine Alves da Costa, Bruno Vincent, Jean Sévalle, Sanjay Pimplikar, Peter St George-Hyslop, and Frédéric Checler* 1 IPMC, UMR6097 CNRS/UNSA, Equipe labellisée FRM, 660 Route des Lucioles, 06560 France Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, ON, M5S 3H2 Canada Department of ...
متن کاملAPP intracellular domain derived from amyloidogenic β- and γ-secretase cleavage regulates neprilysin expression
Alzheimer's disease (AD) is characterized by an accumulation of Amyloid-β (Aβ), released by sequential proteolytic processing of the amyloid precursor protein (APP) by β - and γ-secretase. Aβ peptides can aggregate, leading to toxic Aβ oligomers and amyloid plaque formation. Aβ accumulation is not only dependent on de novo synthesis but also on Aβ degradation. Neprilysin (NEP) is one of the maj...
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Triple-transgenic mice (3xTgAD) overexpressing Swedish-mutated β-amyloid precursor protein (βAPP(swe)), P310L-Tau (Tau(P301L)), and physiological levels of M146V-presenilin-1 (PS1(M146V)) display extracellular amyloid-β peptides (Aβ) deposits and Tau tangles. More disputed is the observation that these mice accumulate intraneuronal Aβ that has been linked to synaptic dysfunction and cognitive d...
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Amyloid-β proteins (Aβ) of 42 (Aβ42) and 40 aa (Aβ40) accumulate as senile plaques (SP) and cerebrovascular amyloid protein deposits that are defining diagnostic features of Alzheimer's disease (AD). A number of rare mutations linked to familial AD (FAD) on the Aβ precursor protein (APP), Presenilin-1 (PS1), Presenilin- 2 (PS2), Adamalysin10, and other genetic risk factors for sporadic AD such ...
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عنوان ژورنال:
- Neuron
دوره 46 شماره
صفحات -
تاریخ انتشار 2005