Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 1010K) PPT slides of all figures Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kaether, C. Articles by Haass, C. Search for Related Content PubMed PubMed Citation Articles by Kaether, C. Articles by Haass, C. Social Bookmarking                      What's this?

A lipid boundary separates APP and secretases and limits amyloid ß-peptide generation

Adolf Butenandt Institute, Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig Maximilians University, 80336 München, Germany

Correspondence to Christian Haass: chaass{at}med.uni-muenchen.de

Abstract

Millions of patients suffer from Alzheimer's disease, and intensive efforts to find a cure for this devastating disorder center on the proteases, which release the deadly amyloid ß-peptide from its precursor. The cutting procedure is thought to be cholesterol dependent and strategies to lower cholesterol as therapeutic treatment are under intensive investigation. Recent findings suggest that the complete proteolytic machinery required for amyloid ß-peptide generation is located within lipid rafts. Data by Dotti and colleagues (Abad-Rodriguez et al., 2004), in this issue, suggest that rafts isolate the cutting machinery away from its deadly substrate. These findings describe a novel mechanism for controlling proteolytic activity by building a lipid boundary between proteases and their substrates.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Sakurai, T., Kaneko, K., Okuno, M., Wada, K., Kashiyama, T., Shimizu, H., Akagi, T., Hashikawa, T., Nukina, N. (2008). Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing. JCB 183: 339-352 [Abstract] [Full Text]  
• Burton, C. R., Meredith, J. E., Barten, D. M., Goldstein, M. E., Krause, C. M., Kieras, C. J., Sisk, L., Iben, L. G., Polson, C., Thompson, M. W., Lin, X.-A., Corsa, J., Fiedler, T., Pierdomenico, M., Cao, Y., Roach, A. H., Cantone, J. L., Ford, M. J., Drexler, D. M., Olson, R. E., Yang, M. G., Bergstrom, C. P., McElhone, K. E., Bronson, J. J., Macor, J. E., Blat, Y., Grafstrom, R. H., Stern, A. M., Seiffert, D. A., Zaczek, R., Albright, C. F., Toyn, J. H. (2008). The Amyloid-{beta} Rise and {gamma}-Secretase Inhibitor Potency Depend on the Level of Substrate Expression. J. Biol. Chem. 283: 22992-23003 [Abstract] [Full Text]  
• Zhang, M., Haapasalo, A., Kim, D. Y., Ingano, L. A. M., Pettingell, W. H., Kovacs, D. M. (2006). Presenilin/{gamma}-secretase activity regulates protein clearance from the endocytic recycling compartment. FASEB J. 20: 1176-1178 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents