Searching for just a few words should be enough to get started. If you need to make more complex queries, use the tips below to guide you.
Issue title: Oxidative Stress in Aging and Neurodegenerative Diseases: From Biology to Therapy, Perugia, Italy, May 2003
Guest editors: M. Cristina Polidori
Article type: Research Article
Authors: Popescu, Bogdan O. | Ankarcrona, Maria; *
Affiliations: Karolinska Institutet, Neurotec, Section of Experimental Geriatrics, Novum, Huddinge, Sweden | Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, D-40225 Düsseldorf, Germany Tel.: +49 211 811 5358; Fax: +49 211 811 3029; E-mail: polidori@uni-duesseldorf.de
Correspondence: [*] Corresponding author: Maria Ankarcrona, PhD., Karolinska Institutet, Neurotec, KFC, Novum, 4th floor, SE-141 86 Huddinge, Sweden. Tel.: +46 8 58583622; Fax: +46 8 58583610; E-mail: maria.ankarcrona@neurotec.ki.se.
Abstract: Presenilins are often mutated in familial forms of Alzheimer's disease (AD). Such mutations sensitize cells in culture to different apoptotic stimuli eg. staurosporine, calcium ionophore, growth factor withdrawal. The altered responses to apoptotic stimuli in cells carrying presenilin mutations include increased intracellular calcium concentrations and enhanced production of reactive oxygen species. Presenilin mutations also result in increased production of amyloid β (Aβ) indicating that presenilins participate in the cleavage of amyloid β-protein precursor (AβPP). In fact, presenilin is part of the γ-secretase complex which together with β-secretase cleaves AβPP and produce Aβ, later forming the senile plaques typical for AD pathology. Here we review the current knowledge about the mechanisms of cell death in AD with focus on the role of presenilin and presenilin mutations in apoptosis. It appears that presenilin and its different fragments, generated after proteolytic cleavage, have a regulatory role in apoptosis. In addition, different studies show that the cellular levels of presenilin are controlled by proteasomal degradation both under normal and stress conditions.
Keywords: Alzheimer's disease, presenilin, apoptosis, proteasome
DOI: 10.3233/JAD-2004-6203
Journal: Journal of Alzheimer's Disease, vol. 6, no. 2, pp. 123-128, 2004
IOS Press, Inc.
6751 Tepper Drive
Clifton, VA 20124
USA
Tel: +1 703 830 6300
Fax: +1 703 830 2300
sales@iospress.com
For editorial issues, like the status of your submitted paper or proposals, write to editorial@iospress.nl
IOS Press
Nieuwe Hemweg 6B
1013 BG Amsterdam
The Netherlands
Tel: +31 20 688 3355
Fax: +31 20 687 0091
info@iospress.nl
For editorial issues, permissions, book requests, submissions and proceedings, contact the Amsterdam office info@iospress.nl
Inspirees International (China Office)
Ciyunsi Beili 207(CapitaLand), Bld 1, 7-901
100025, Beijing
China
Free service line: 400 661 8717
Fax: +86 10 8446 7947
china@iospress.cn
For editorial issues, like the status of your submitted paper or proposals, write to editorial@iospress.nl
如果您在出版方面需要帮助或有任何建, 件至: editorial@iospress.nl