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Fw: Breast cancer, Space Station research

Submitted by Arthur - N1ORC

> NASA Marshall Space Flight Center
> Huntsville, Ala. 35812
> For Release: May 2, 2002
> RELEASE: 02-110
> American Cancer Society funds Space Station scientist who studies how
> cells turn bad
>         Every second, your body's cells get instructions on what they
> supposed to do from DNA  -- the double-helix strand of deoxyribonucleic
> acid that is the genetic ingredient essential for life. 
> In healthy cells, proteins manufacture DNA and remove or repair any
> strands.  When proteins fail to repair damaged DNA, good cells may turn
> bad, resulting in a plethora of diseases, including cancer. 
> Yearly mammograms and daily inspections for lumps make women intimately
> aware that bad cells form tumors. According to the America Cancer
> in 2001 almost 200,000 women were diagnosed with new cases of breast
> cancer -- and some 40,000 women were killed by the disease.
> To understand how these basic molecular processes cause breast cancer,
> American Cancer Society has awarded a $768,000, four-year grant to 
> Dr. Gloria Borgstahl, a biochemist at the University of Toledo in Ohio.
> Borgstahl's grant proposal to the American Cancer Society was rated
> of 57 submissions to the Genetic Mechanisms in Cancer grant selection
> committee.
> "I am not discovering a cure for cancer," cautioned Borgstahl, "but the
> American Cancer Society and NASA recognize that understanding basic
> molecular processes in the body will ultimately provide the knowledge
> researchers need to get closer to that cure."  
> Right now, Borgstahl is doing related experiments on the International
> Space Station. She is in her first year of research funded by a
> three-year, $830,000-grant awarded by NASA's Office of Biological and
> Physical Research as part of the Macromolecular Biotechnology Program
> NASA's Marshall Space Flight Center in Huntsville, Ala. 
> On April 19, the Space Shuttle Atlantis returned with the first
> crystals that she grew on the Space Station.
> The American Cancer Society funding will help Borgstahl study
> Protein A, know as RPA, and another protein called Rad52. Scientists
> discovered RPA and learned it is a protein essential for synthesizing
> copying DNA so it can become part of new cells and for repairing DNA.
> interacts with Rad52, which was first recognized for its importance in
> helping yeast survive when exposed to radiation. Familial breast cancer
> genes, BRCA1 and BRCA2, are related genes that, when damaged or
> can greatly increase a woman's risk of getting breast cancer.
> "Everyone thinks of protein as a nutritional requirement -- like a
> said Borgstahl. "But what we are talking about are the molecules of
> The chemistry of life is conducted by individual protein molecules that
> make up DNA and carry out cellular processes."
> How do scientists see these microscopic interactions inside our cells? 
>  "It is like cooking, you mix solutions A, B and C, and -- if you're
> -- they form crystals of the protein you are studying," explained
> Borgstahl.  "Then we can use X-rays to study the crystal and determine
> three-dimensional structure of the protein." 
> The difficult part is getting the recipe right.  There are thousands of
> different types of proteins in the human body alone, and scientists
> only been able to determine the structure of a mere 1 percent of them.
> Scientists start with a purified, contamination-free protein, which is
> sometimes costly and difficult to prepare. The protein is mixed with a
> precipitant, usually a salt that removes water from the protein
> and causes crystals to form. Much in the same way rock candy is made.
> The problem is, proteins -- like people -- are not alike.  Finding
> how much salt to mix with protein, and the best way to mix the
> to get a good crystal, is challenging. 
> "Different techniques work for different proteins," said Dr. Edward
> a crystallographer at the Structural Biology Laboratory at the Marshall
> Center, who collaborates with Borgstahl. "That is why researchers are
> using a number of devices to grow crystals on the Space Station. Just
> you bake some dishes and boil others, you process crystals in different
> ways to get the best results."
> In ground-based laboratories, like Borgstahl's at the University of
> Toledo, researchers mix up and try out thousands of recipes at a time -
> trying to coax proteins to form crystals that will reveal how they are
> made. 
> So why use an orbiting laboratory hundreds of miles away in space?
> Some proteins form crystals perfectly on the ground. Some form small,
> irregular crystals that are difficult to study and won't reveal how
> proteins are made. Some won't form crystals at all.
> In the microgravity environment created as the Space Station orbits
> crystals float in their solutions - much like the astronauts float
> the Station. On Earth, the heavy crystals sediment, or sink, to the
> of flasks and often stick together. This sometimes results in small,
> cracked, poorly formed crystals.
> Borgstahl and Snell got their first taste of success on the STS-95
> Shuttle mission in October 1998 when U.S. Sen. John Glenn of Ohio
> grow crystals of insulin in microgravity for the Hauptman-Woodward
> Research Institute in Buffalo, New York.  Snell and Borgstahl analyzed
> quality of the insulin crystals. They found the space-grown crystals
> 34 times larger than those grown on the ground. (Acta Crystallographic,
> 2001, D57, 254-259) 
> "More importantly than being large, the crystals had better internal
> order," said Snell. "Our thorough analysis showed microgravity passed
> test, providing the best environment for growing macromolecules of
> proteins."
> Better internal order means that scientists can fire X-ray beams at the
> crystal and learn how it is made at the atomic an/or electronic level.
> is like working a puzzle backwards.  You have a crystal - the completed
> puzzle -- but you need to learn how the pieces - in this case the
> molecules - fit together to form the crystal and make each unique
> So you shoot X-rays at the crystal. This produces a diffraction pattern
> that can be reconstructed to create a three-dimensional computer model
> the protein's macromolecular structure. Scientists use the model to
> understand exactly how proteins work in the body or don't work -
> how medicines interact with proteins.
> Snell, Borgstahl and her team at the University of Toledo will soon be
> busy analyzing a new batch of 35 experiments fresh from the Space
> These crystals are of Manganese Superoxide Dismutase, or MnSOD, an
> that is an anti-oxidant and plays a role in diseases associated with
> such as diabetes, cancer and neurodegenerative disorders.  
> Analysis in her Ohio laboratory and flying samples on future Space
> expeditions will bring Borgstahl closer to learning how good cells turn
> bad.
> Contact
> Steve Roy
> Media Relations Department
> NASA Marshall Space Flight Center
> (256) 544-0034
> Steve.Roy@msfc.nasa.gov
> Tobin J. Klinger
> Senior Media Relations Coordinator
> The University of Toledo
> (419) 530-4279
> tobin.klinger@utoledo.edu
> _______
> The Web
> News release
> http://www1.msfc.nasa.gov/NEWSROOM/news/releases/2002/02-110.html
> Photos
> <http://www1.msfc.nasa.gov/NEWSROOM/news/photos/2002/photos02-110.htm>
> Animation
> http://www1.msfc.nasa.gov/NEWSROOM/news/video/2002/video02-110.htm
> American Cancer Society
> <http://www.cancer.org/>
> Other NASA Breast Cancer Research
> <http://www.nasa.gov/women/health/cancer.html>
> Biological Crystal Growth in Space
> <http://crystal.nasa.gov/>
> University of Toledo
> <http://sbl.chem.utoledo.edu/>
> Office of Biological and Physical Science
> http://spaceresearch.nasa.gov/
> ISS Science Operations 
> <http://www.scipoc.msfc.nasa.gov/>
> Microgravity Science
> <http://www.microgravity.nasa.gov>
> Marshall Space Flight Center
> Media Relations Department
> (256) 544-0034
> (256) 544-5852 (fax)
> www.msfc.nasa.gov/news

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