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

10 Fibro-Friendly Foods with a Bonus: Beautiful Skin

Studies Show that Magnesium L-threonate Improves Brain Plasticity, Leading to Direct and Significant...

Clary Sage Oil May Be Pricey, but Its Benefits Are Priceless

Component of red wine, grapes can help to reduce inflammation, study finds

Poly MVA: A Novel Therapy for Increasing Energy, Repairing DNA, and Promoting Overall Health

Pumpkin Pie Turmeric Breakfast Smoothie - Vegan + Gluten-Free

Vitamin D supplementation extends life in mouse model of Huntington's disease

Omega-3 fatty acid stops known trigger of lupus

Conquer Your Email Inbox, Increase Productivity and Reduce Stress

The Significance of Selenium

Print Page
Email Article

Alzheimer's: New findings resolve long dispute about how the disease might kill brain cells

  [ 10 votes ]   [ Discuss This Article ]
By University of Michigan, Ann Arbor • • April 16, 2009

“Amyloid-beta peptides prick pores into brain cell membranes, opening channels where calcium ions can rush in.” (Suggesting ion channel blocker research.)

For a decade, Alzheimer's disease researchers have been entrenched in debate about one of the mechanisms believed to be responsible for brain cell death and memory loss in the illness.

Now researchers at the University of Michigan and the University of California, San Diego have settled the dispute. Resolving this controversy improves understanding of the disease and could one day lead to better treatments.

Michael Mayer, an assistant professor in the U-M departments of Biomedical Engineering and Chemical Engineering, and Jerry Yang, an assistant professor in the Department of Chemistry and Biochemistry at UCSD, and their colleagues found a flaw in earlier studies supporting one side of the debate. Their findings are published online in the Journal of Neurotoxicity Research. ["Amyloid-beta- induced ion flux in artificial lipid bilayers and neuronal cells: Resolving a controversy." To view the article free, click here.]

Their results clarify how small proteins called amyloid-beta peptides damage brain cell membranes, allowing extra calcium ions to enter the neurons. An ion is an electrically-charged particle. An ion imbalance in a cell can trigger its suicide.

Amyloid-beta peptides are the prime suspects for causing cell death in Alzheimer's, although other mechanisms could also be to blame. The disease is not well understood.

The researchers confirmed evidence found by others that amyloid-beta peptides prick pores into brain cell membranes, opening channels where calcium ions can rush in.

This was one mechanism the field had contemplated, but other evidence suggested a different scenario. Some researchers believed that the peptide caused a general thinning of the cell membranes and these thinned membranes lost their ability to keep calcium ions out of brain cells. Mayer and Yang disproved this latter theory.

"When you understand these mechanisms better, you have a better chance of being able to pharmaceutically counteract them as a possible treatment. For instance, if amyloid-beta thins membranes, this general effect might be difficult to treat.

"On the other hand, if it forms pores, this effect might be treatable with pore blockers. Ion channel blockers are medications sold today to treat a variety of diseases," Mayer said.

He cautions that much research is needed before it is known whether such medications are effective and safe to treat Alzheimer's.

Mayer and Yang were able to explain the other experimental results that blamed cell membrane thinning for uncontrolled calcium ion fluctuations. It turns out that in these studies, trace amounts of residual solvent used to prepare the peptide had a dramatic effect. The Michigan- and UCSD-led team reproduced these experimental results using only the solvent, without the peptide. The solvent is called Hexafluoroisopropanol, or HFIP.

"HFIP is a good solvent used to break up clumps of the peptide to prepare for experiments, but it's toxic and membrane-active. What we found was that the reported preparation procedure did not remove the solvent effectively," Mayer said. "Our findings are watertight since we could reproduce the thinning effect in the absence of amyloid-beta peptides by this solvent alone."

Yang and Mayer carried out these experiments by examining how the electric current fluctuates across artificial membranes and live human cancer cell membranes in the presence of the amyloid-beta peptide. (Cancer cells are often used in biological experiments because they reproduce rapidly.) They also measured the fluctuation of ions in mouse brain cells and in genetically-modified mouse brain cells that produce human amyloid-beta peptide.

In all these trials, the electrodes measuring across the cell membrane registered spikes in electric current consistent with what researchers would expect from the formation of pores in the cell membrane and not from thinning of membranes.

"This ongoing controversy has slowed our own progress in Alzheimer's research as well as progress in other labs," Mayer said.

"It is our hope that putting this disagreement to rest by showing that amyloid beta peptides do not thin membranes but instead form discrete pores in membrane can help the field move forward at a more rapid pace."
Source: University of Michigan, Ann Arbor, news release Apr 15, 2009

Post a Comment

Featured Products From the ProHealth Store
Vitamin D3 Extreme™ Ultra EPA  - Fish Oil Mitochondria Ignite™ with NT Factor®

Looking for Vitamins, Herbs and Supplements?
Search the ProHealth Store for Hundreds of Natural Health Products

Article Comments

Be the first to comment on this article!

Post a Comment

Natural Pain Relief Supplements

Featured Products

FibroSleep™ FibroSleep™
The All-in-One Natural Sleep Aid
Ultra EPA  - Fish Oil Ultra EPA - Fish Oil
Ultra concentrated source of essential fish oils
Energy NADH™ 12.5mg Energy NADH™ 12.5mg
Improve Energy & Cognitive Function
Ultra ATP+, Double Strength Ultra ATP+, Double Strength
Get energized with malic acid & magnesium
Vitamin D3 Extreme™ Vitamin D3 Extreme™
50,000 IU Vitamin D3 - Prescription Strength

Natural Remedies

Milk Thistle: Trusted Support for Health & Healing in a Toxic World Milk Thistle: Trusted Support for Health & Healing in a Toxic World
Strontium - The Missing Mineral for Strong Bones Strontium - The Missing Mineral for Strong Bones
The Crucial Role CoQ10 Plays in Fibromyalgia and ME/CFS The Crucial Role CoQ10 Plays in Fibromyalgia and ME/CFS
Relief for Dry, Itchy Skin Caused by Fibromyalgia Relief for Dry, Itchy Skin Caused by Fibromyalgia
Reversing Neurodegeneration with a New Magnesium Compound Reversing Neurodegeneration with a New Magnesium Compound

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

· Become a Wholesaler
· Vendor Inquiries
· Affiliate Program
Credit Card Processing
Be the first to know about new products, special discounts and the latest health news. *New subscribers only

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

© 2016 ProHealth, Inc. All rights reserved. Pain Tracker App  |  Store  |  Customer Service  |  Guarantee  |  Privacy  |  Contact Us  |  Library  |  RSS  |  Site Map