Response 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
نویسندگان
چکیده
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 Pathology and Cell Biology Program, Case Western Reserve University, Cleveland, OH 44106, USA *Correspondence: [email protected] DOI 10.1016/j.neuron.2007.01.024
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 کاملPresenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLP
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 N...
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rEFErENcES Belyaev ND et al (2009) EMBO Rep 10: 94–100 Belyaev ND et al (2010) J Biol Chem 285: 41443–41454 clark rD et al (2009) Genet Med 11: 769–775 goate a et al (1991) Nature 349: 704–706 goodger zV et al (2009) J Cell Biol 122: 3703–3714 Huysseune S et al (2009) FASEB J 23: 4158–4167 pardossi-piquard r et al (2005) Neuron 46: 541–554 Wang X et al (2006) Proc Natl Acad Sci USA 103: 17284–1...
متن کاملThe β-secretase-derived C-terminal fragment of βAPP, C99, but not Aβ, is a key contributor to early intraneuronal lesions in triple-transgenic mouse hippocampus.
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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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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ورودعنوان ژورنال:
- Neuron
دوره 53 شماره
صفحات -
تاریخ انتشار 2007