Please note that eDoc will be permanently shut down in the first quarter of 2021!      Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen mpi-cbg 2003     Display Documents



  history
ID: 190449.0, MPI für molekulare Zellbiologie und Genetik / Publikationen mpi-cbg 2003
Guinea pigs as a nontransgenic model for APP processing in vitro and in vivo.
Authors:Beck, Mike; Bigl, Volker; Rossner, Steffen
Date of Publication (YYYY-MM-DD):2003
Title of Journal:Neurochemical Research
Volume:28
Issue / Number:3-4
Start Page:637
End Page:644
Copyright:not available
Review Status:not specified
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Alzheimer's disease (AD) is characterized, amongst others, by the appearance of vascular and parenchymal beta-amyloid deposits in brain. Such aggregates are mainly composed of beta-amyloid peptides, which are derived by proteolytic processing of a larger amyloid precursor protein (APP). APP is highly conserved among mammalian species, but experimental studies in rodents are often hampered by the humble APP-processing in the amyloidogenic pathway and by the inability of rodent beta-amyloid peptides to form higher molecular aggregates such as soluble oligomers and insoluble beta-amyloid plaques. Thus, there is need for in vitro and in vivo model systems that allow identification of factors that increase amyloidogenic APP processing and accelerate beta-amyloid plaque formation and testing the potency of pharmacological manipulations to ameliorate beta-amyloid load in brain. Transgenic mice that overexpress human APP containing AD-associated mutations that favor the amyloidogenic pathway of APP processing represent such a model. However, mutations of the APP gene are not frequent in AD and, therefore, the mechanisms of beta-amyloid plaque formation, the composition of beta-amyloid plaques, and the accompanying tissue response in brain of these animals may be different from that in AD. In contrast, guinea pigs express beta-amyloid peptides of the human sequence and appear to represent a more physiological model to examine the long-term effects of experimental manipulations on APP processing and beta-amyloid plaque formation in vivo. Additionally, APP processing in guinea pig primary neuronal cultures has been shown to be similar to cultures of human origin. In this article we highlight the advantages and limitations of using guinea pigs as experimental models to study APP processing.
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:362
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.