ProHealth health Vitamin and Natural Supplement Store and Health
Home  |  Log In  |  My Account  |  View Cart  View Your ProHealth Vitamin and Supplement Shopping Cart
800-366-6056  |  Contact Us  |  Help
Facebook Google Plus
Fibromyalgia  Chronic Fatigue Syndrome & M.E.  Lyme Disease  Natural Wellness  Supplement News  Forums  Our Story
Store     Brands   |   A-Z Index   |   Best Sellers   |   New Products   |   Deals & Specials   |   Under $10   |   SmartSavings Club

Trending News

Meta-analysis adds evidence to association between omega-3 supplementation and lower heart rate

Friendly User's Guide for the Timing of Nutritional Supplements

The Health Benefits of Manuka Honey

Increase Your Magnesium Intake

Vitamin D supplementation could ease IBS symptoms

Top Tips to Boost Your Immunity

Essential Oils Lower Blood Pressure

11 Amazing Health Benefits of Using Baking Soda

Nicotinamide riboside shows promise for treatment of Alzheimer’s disease

Exercise, calcium, vitamin D, and other factors linked with fewer injurious falls

 
Print Page
Email Article

New mechanism explains Alzheimer’s damage

  [ Not Yet Rated ]   [ Discuss This Article ]
By Press Release by the American Chemical Society • www.ProHealth.com • June 8, 1999


Harvard Medical School researchers say they have found a "completely new" mechanism for explaining how Alzheimer's disease damages the brain. They say a chemical reaction, involving proteins that accumulate in Alzheimer's patients' brains, produces a bleaching agent that is toxic to cells there. The scientists think the discovery could provide a unique target for new drugs to treat Alzheimer's, which causes dementia in at least four million Americans.

The findings will be in the June 15 print edition of the peer-reviewed journal Biochemistry, which is published by the American Chemical Society (ACS), the world's largest scientific society. The paper was published on the ACS Web May 27.

Currently incurable, Alzheimer's disease is the fourth leading cause of death in Western countries. Those over 85 years of age, the fastest growing portion of the U.S. population, have a 50-50 chance of developing the disease. Upon autopsy, patients' brains are typically found to be riddled with deposits of amyloid protein plaques.

Though the amyloid plaques have long been an obvious suspect as a cause of the disease pathology, exactly how they might do it has been a mystery. "We have found that the amyloid protein...binds copper and iron and produces hydrogen peroxide (H2O2) out of oxygen when doing so. Yes, bleach," says co-author Ashley I. Bush, M.D., Ph.D., who directs the Laboratory for Oxidation Biology in Massachusetts General Hospital's Psychiatry Department, a part of Harvard Medical School.

While H2O2 has previously been detected in laboratory cell cultures exposed to synthetic amyloid, researchers thought that some reaction within dying cells produced the substance. The new study is the first indication that a substantial portion of the H2O2 is being made by the plaques themselves, adding that "previously it was not shown that amyloid could produce any new chemicals."

Bush says that copper and iron, abundant in the brain, are known to be enriched in amyloid deposits. So he expects levels of hydrogen peroxide, which can easily travel from where it is produced in the plaques, to be high in other parts of patients' brains. "This is important since H2O2 can cause brain damage, and will be a source of oxidative stress in the brain," according to Bush.

Could this be the sole cause of Alzheimer's disease? Bush's answer: "The possibility that it's the most important of the chemical events to occur is difficult to judge right now, however it's the kind of chemical event that can't be ignored. Having this protein be able to produce this obviously toxic chemical out of oxygen is a property that's clearly got direct potential to harm the brain." Conclusive answers will have to wait for results of ongoing animal studies.

In the laboratory, the researchers showed that hydrogen peroxide production could be inhibited by chemicals that reacted with the copper or iron binding to the amyloid. Many well-known drugs, such as aspirin and some antibiotics, similarly target metals on the active site of a specific protein. "If we could make drugs that specifically shut down the ability of amyloid to produce H2O2 from oxygen, then we might have a new therapeutic approach to Alzheimer's disease," says Bush.

Source: American Chemical Society Press Release: June 8, 1999

Contact: Julie Malveaux, j_malveaux@acs.org, 202-872-6042



Post a Comment

Featured Products From the ProHealth Store
Ultra ATP+, Double Strength Energy NADH™ 12.5mg Vitamin D3 Extreme™


Article Comments



Be the first to comment on this article!

Post a Comment


 
Optimized Curcumin Longvida with Omega-3

Featured Products

Optimized Curcumin Longvida® Optimized Curcumin Longvida®
Supports Cognition, Memory & Overall Health
Mitochondria Ignite™ with NT Factor® Mitochondria Ignite™ with NT Factor®
Reduce Fatigue up to 45%
Energy NADH™ 12.5mg Energy NADH™ 12.5mg
Improve Energy & Cognitive Function
FibroSleep™ FibroSleep™
The All-in-One Natural Sleep Aid

Natural Remedies

Aching Muscles? Top 10 Nutrients to Take Back Your Life Aching Muscles? Top 10 Nutrients to Take Back Your Life
D-ficient? Health Risks You Need to Know About D-ficient? Health Risks You Need to Know About
More Weight Loss than Any Other Discovery in Supplement History More Weight Loss than Any Other Discovery in Supplement History
Break Free From Fibromyalgia Break Free From Fibromyalgia
Hydroxytyrosol: A Superior Antioxidant for Combatting Oxidative Stress Hydroxytyrosol: A Superior Antioxidant for Combatting Oxidative Stress

CONTACT US
ProHealth, Inc.
555 Maple Ave
Carpinteria, CA 93013
(800) 366-6056  |  Email

· Become a Wholesaler
· Vendor Inquiries
· Affiliate Program
SHOP WITH CONFIDENCE
Credit Card Processing
SUBSCRIBE TO OUR NEWSLETTERS
Get the latest news about Fibromyalgia, M.E/Chronic Fatigue Syndrome, Lyme Disease and Natural Wellness

CONNECT WITH US ProHealth on Facebook  ProHealth on Twitter  ProHealth on Pinterest  ProHealth on Google Plus

© 2018 ProHealth, Inc. All rights reserved. Pain Tracker App  |  Store  |  Customer Service  |  Guarantee  |  Privacy  |  Contact Us  |  Library  |  RSS  |  Site Map