Printer Friendly
The Free Library
23,375,127 articles and books


Alzheimer's disease enzyme identified.

Researchers at the University of Texas Southwestern Medical Center in Dallas have defined a key step in the production of beta-amyloid, a short protein that is thought to be responsible for the development of Alzheimer's disease.

In Alzheimer's disease, too much beta-amyloid is produced by an enzyme that has many other essential roles. As a result, simply blocking the whole enzyme knocks out many of its other functions, which is fatal to the organism.

Using cultured human cells, as well as test-tube assays, university researchers singled out how just one portion of the enzyme, a protein called nicastrin, is involved in the pathway that produces beta-amyloid, thereby leading to Alzheimer's disease.

"The work provides an attractive potential strategy for developing treatment for Alzheimer's disease," said Dr. Gang Yu, senior author of the study. The research uncovered an "unprecedented mechanism of biochemistry," Dr. Yu said.

Nicastrin is a large protein that is a component of an enzyme called gamma-secretase, which is lodged in the cell's membrane. When it is at the cell surface, nicastrin sticks out into the area outside the cell. It was thought to play a key role in the creation of amyloid-beta, although the exact mechanism was unknown.

Dr. Yu and his colleagues discovered that nicastrin binds to several proteins lodged in the cell's membrane, including one called amyloid precursor protein, or APP. Nicastrin then guides membrane-bound proteins to the active area of gamma-secretase, which then splits the proteins.

APP, for example, is chopped into two parts: amyloid-beta is shipped to the outside of the cell, and another part remains inside. Amyloid-beta forms the plaques seen in the brains of patients with Alzheimer's disease.

Now that nicastrin's function has been ascertained, it opens a way to block just the splitting of APP, leaving all the enzyme's other functions intact. For instance, it may be possible to generate chemical compounds that specifically prevent nicastrin from latching on to APP. If APP does not attach to nicastrin, APP remains intact and harmless. Meanwhile, nicastrin would be free to bind all the other essential proteins that it works on.

"We want to find a particular way to block the recognition of APP but not the others," he said.

(Source: Cell, August 12, 2005.)
COPYRIGHT 2005 Vegetus Publications
No portion of this article can be reproduced without the express written permission from the copyright holder.
Copyright 2005 Gale, Cengage Learning. All rights reserved.

 Reader Opinion

Title:

Comment:



 

Article Details
Printer friendly Cite/link Email Feedback
Publication:Nutrition Health Review
Article Type:Disease/Disorder overview
Geographic Code:1USA
Date:Mar 22, 2005
Words:372
Previous Article:EU reacts unfavorably to feeding practices.
Next Article:Brains of lovers differ from those of brokenhearted.
Topics:



Related Articles
Enzyme offers promise of Alzheimer's drugs.
Debate over Alzheimer's enzyme flares up.
Enzyme counters Alzheimer's-like snarls. (Untangling the Brain).
Alzheimer's linked to insulin enzyme.
AXONYX REPORTS GOOD EFFECTS OF PHENSERINE ON ALZHEIMERS'.
Chronic stress steals years from caregivers.
Alzheimer's mystery protein unmasked.
Mechanism that protects against development of Alzheimer's identified.

Terms of use | Copyright © 2014 Farlex, Inc. | Feedback | For webmasters