[net-gold] BIOLOGY: RESEARCH: Molecule Repairs Alcohol Metabolism Enzyme
- From: "David P. Dillard" <jwne@xxxxxxxxxx>
- To: Net-Gold <Net-Gold@xxxxxxxxxxxxxxx>, Temple University Net-Gold Archive <net-gold@xxxxxxxxxxxxxxxxxxx>, Temple Gold Discussion Group <TEMPLE-GOLD@xxxxxxxxxxxxxxxxxxx>, Net-Gold <net-gold@xxxxxxxxxxxxxxxx>, Sean Grigsby <myarchives1@xxxxxxxxxxxxxxx>, Educator Gold <Educator-Gold@xxxxxxxxxxxxxxx>, Educator Gold <Educator-Gold@xxxxxxxxxxxxxxxx>, K12AdminLIFE <K12AdminLIFE@xxxxxxxxxxxxxxx>, Net-Platinum <net-platinum@xxxxxxxxxxxxxxx>, "Net-Gold @ Nabble" <ml-node+3172864-337556105@xxxxxxxxxxxxx>, MediaMentor <mediamentor@xxxxxxxxxxxxxxx>, Digital Divide Diversity MLS <mls-digitaldivide@xxxxxxxxxxxxxxx>, net-gold@xxxxxxxxxxxxx
- Date: Mon, 11 Jan 2010 11:49:55 -0500 (EST)
.
BIOLOGY: RESEARCH:
Molecule Repairs Alcohol Metabolism Enzyme
.
Date: Mon, 11 Jan 2010 09:01:21 -0500
From: "NIH OLIB (NIH/OD)" <olib@xxxxxxxxxx>
To: NIHPRESS@xxxxxxxxxxxx
Subject: MOLECULE REPAIRS ALCOHOL METABOLISM ENZYME
U.S. Department of Health and Human Services
NATIONAL INSTITUTES OF HEALTH NIH News
National Institute on Alcohol Abuse and Alcoholism (NIAAA)
<http://www.niaaa.nih.gov/>
Embargoed for Release: January 10, 2010, 1:00 PM, EST
CONTACT: NIAAA Press Office
301-443-3860
e-mail:
NIAAAPressOffice@xxxxxxxxxxxx
MOLECULE REPAIRS ALCOHOL METABOLISM ENZYME
An experimental compound repaired a defective alcohol metabolism enzyme
that affects an estimated 1 billion people worldwide, according to
research supported by the National Institute on Alcohol Abuse and
Alcoholism (NIAAA). The findings, published Jan. 10, 2010 in the advance
online edition of Nature Structural and Molecular Biology, suggest the
possibility of a treatment to reduce the health problems associated with
the enzyme defect.
"This intriguing finding could have broad public health implications,"
said NIAAA Acting Director Kenneth R. Warren, Ph.D. "We look forward to
further research aimed at translating these laboratory discoveries into
possible treatments for people."
"We recently identified a molecule called Alda-1 that activates the
defective enzyme, and in the current study, we determined how this
activation is achieved," said the study's senior author, Thomas D. Hurley,
Ph.D., professor and associate chairman of biochemistry and molecular
biology at Indiana University School of Medicine in Indianapolis.
Initial investigations of Alda-1 were led by co-author Daria Mochly-Rosen,
Ph.D., professor of chemical and systems biology at Stanford University
School of Medicine.
After alcohol is consumed, it is first metabolized, or broken down, into
acetaldehyde, a toxic chemical that causes DNA damage. Aldehyde
dehydrogenase 2 (ALDH2) is the main enzyme responsible for breaking down
acetaldehyde into acetate, a nontoxic metabolite in the body. It also
removes other toxic aldehydes that can accumulate in the body.
About 40 percent of the East Asian population, and many people of East
Asian descent throughout the world, carry a genetic mutation that produces
an inactive form of ALDH2. When individuals with the ALDH2 mutation drink
alcohol, acetaldehyde accumulates in the body, resulting in facial
flushing, nausea, and rapid heartbeat. In addition to its link to
increased cancer risk, the inactive form of ALDH2 also reduces the
effectiveness of nitroglycerin. Nitroglycerin is a drug to treat angina,
chest pain that occurs when the heart doesn't get enough oxygen-rich
blood.
In a series of experiments that examined the interaction between Alda-1
and the defective ALDH2 enzyme, Dr. Hurley and his colleagues found that
Alda-1 restored the structure of the inactive enzyme. The normal, active
form of ALDH2 creates a catalytic tunnel, a space within the enzyme in
which acetaldehyde is metabolized, explained Dr. Hurley. In the defective
enzyme, the tunnel does not function properly. Alda-1 binds to the
defective enzyme in a way that effectively reopens the catalytic tunnel
and thus allows the enzyme to metabolize acetaldehyde.
"The manner in which Alda-1 binds to the structure of ALDH2 provides us
with powerful insight into the relationships between activators and
inhibitors of this crucial detoxifying enzyme," says Dr. Hurley. "This
insight will lead to the modification of Alda-1 to improve its potency,
and also opens up the possibility of designing new analogs that can
selectively affect the metabolism of other molecules that are detoxified
by aldehyde dehydrogenase."
The National Institute on Alcohol Abuse and Alcoholism, part of the
National Institutes of Health, is America's authority on alcohol research
and health. The primary U.S. agency for conducting and supporting research
on the causes, consequences, prevention, and treatment of alcohol abuse,
alcoholism, and alcohol problems, NIAAA also disseminates research
findings to general, professional, and academic audiences. Additional
alcohol research information and publications are available at
<http://www.niaaa.nih.gov>
The National Institutes of Health (NIH) -- The Nation's Medical Research
Agency -- includes 27 Institutes and Centers and is a component of the
U.S. Department of Health and Human Services. It is the primary federal
agency for conducting and supporting basic, clinical and translational
medical research, and it investigates the causes, treatments, and cures
for both common and rare diseases. For more information about NIH and its
programs, visit
<http://www.nih.gov>
##
This NIH News Release is available online at:
<http://www.nih.gov/news/health/jan2010/niaaa-10.htm>
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David Dillard
Temple University
(215) 204 - 4584
jwne@xxxxxxxxxx
<http://daviddillard.businesscard2.com>
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