Scientists discover novel way to remove iron from
ferritin
Research results featured in the Journal of
Biological Chemistry.
Oakland, CA - A new study led by Children's Hospital Oakland Research
Institute senior scientist, Elizabeth Theil, Ph.D., is the first to
suggest that a small protein or heptapeptide (seven amino acids wrapped
into one unit) could be used to accelerate the removal of iron from
ferritin. The results of this study may help scientists develop new
medications that dramatically improve the removal of excess iron in
patients diagnosed with blood diseases such as B-Thalassemia (Cooley's
anemia) or Sickle Cell Disease.
The study appears in this month's issue of the Journal of Biological
Chemistry and was conducted by Dr. Theil and her co-authors Xiaofeng
S. Liu, postdoctoral fellow at Children's Hospital Oakland Research
Institute, Marvin J. Miller, Ph.D. and Leslie D. Patterson, a
predoctoral student, both from the University of Notre Dame. The
scientists knew that the ferritin protein cage had pores that could
open and close. It was also known that chelators (a method to detoxify
blood) removed iron faster when the pores were open.
"We wanted to prove a hypothesis that a small protein or peptide could
bind to ferritin and could be used to regulate ferritin pores," said
Dr. Theil. "Our hypothesis was correct. We proved that when a binding
peptide of seven amino acids, a heptapeptide, is coupled with Desferal
the rate of removal of iron from ferritin is eight times faster."
Desferal is currently used to detoxify the blood of patients with iron
overload and is a common therapeutic remedy.
Ferritin is a protein that concentrates iron in its inner core or 'cage'.
It plays a critical role in understanding iron overload, which can
lead to a variety of symptoms including chronic fatigue, weakness,
joint pain and arthritis. If left untreated, iron overload can lead to
serious problems, including diabetes, liver and heart disease.
The study's results are based on laboratory tests.
The National Institutes of Health (NIH), the Cooley's Anemia
Foundation and Children's Hospital & Research Center Oakland
provided funding for this research.
Further Information and Source:
-
Korry J. Hintze, Yasutake Katoh, Kazuhiko Igarashi, and Elizabeth C.
Theil: Bach1 repression of Ferritin and thioredoxin reductase1 is
heme-sensitive in cells and in vitro, and coordinates expression
with heme oxygenase1, -globin and NADP(H) quinone (oxido)reductase1.
In: Journal of Biological Chemistry;
J. Biol. Chem; published online ahead of print October 11, 2007; doi
10.1074/jbc.M700254200
Research efforts at
Children's Hospital & Research Center Oakland are coordinated
through Children's Hospital Oakland Research Institute (CHORI).
Children's Hospital Oakland is Northern California's only
freestanding and independent children's hospital. CHORI's
internationally renowned biomedical research facility brings
together seven centers of excellence that are devoted to clinical
and basic science research to treat and prevent disease. CHORI has
approximately 300 staff members and an annual budget of more than
$49 million. The National Institutes of Health is CHORI's primary
funding source. The institute is a leader in translational research,
bringing bench discoveries to bedside applications. These include
providing cures for blood diseases, developing new vaccines for
infectious diseases and discovering new treatment protocols for
previously fatal or debilitating conditions such as cancers, sickle
cell disease and thalassemia, diabetes, asthma, HIV/AIDS, pediatric
obesity, nutritional deficiencies, birth defects, hemophilia and
cystic fibrosis.
