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Genetically Engineered Hemoglobin Brings Artificial Blood A Step Closer

Date:
November 7, 2000
Source:
American Chemical Society
Summary:
Using genetic engineering techniques, researchers have created artificial hemoglobin that could someday alleviate perennial blood bank shortages. Hemoglobin - the vital component that carries life-supporting oxygen through the body - could be used in artificial blood transfused during surgeries and transplants, said Chien Ho, lead researcher from Carnegie Mellon University in Pittsburgh, Pa.

Using genetic engineering techniques, researchers have created artificial hemoglobin that could someday alleviate perennial blood bank shortages. The achievement is reported in the November 21 issue of Biochemistry, a peer-reviewed journal of the American Chemical Society, the world's largest scientific society.

Hemoglobin - the vital component that carries life-supporting oxygen through the body - could be used in artificial blood transfused during surgeries and transplants, said Chien Ho, lead researcher from Carnegie Mellon University in Pittsburgh, Pa. The method described in the research was used to produce small amounts of hemoglobin in a laboratory and needs to be improved, said Ho. But he believes the product is likely to be part of an eventual blood substitute.

Neither artificial blood nor its components are currently available. Several potential blood substitutes are being investigated, all of which incrementally advance development of an oxygen carrier, necessary for synthetic blood that could be safely used by people, Ho said. Because the population is aging and demand for blood is increasing - for surgeries, transfusions and to treat blood disorders - the need for a substitute is becoming urgent.

"There is an SOS for blood right now and that demand will only grow in the future," Ho said. "I am very excited about this research as a potential candidate in a blood substitute system. It shows great potential as a successful oxygen carrier, and is something that could realistically be used in people one day."

The researchers overcame problems that have plagued previous attempts to create oxygen carriers by building mutations into the hemoglobin molecule to enhance functioning. They allow it to act just like the hemoglobin molecule in regular human blood, Ho said. But like human blood, artificial hemoglobin would have to be replenished frequently.

Another approach to making artificial hemoglobin is needed to provide sufficient amounts for use in people. For example, pigs or other animals could be used to produce hemoglobin in bulk, Ho said.

Different types of hemoglobin can be designed using the same techniques, Ho said. For example, they might be tailored to meet specific medical requirements for afflictions like sickle-cell anemia and other blood-related disorders.

Some 4 million Americans receive transfusions of whole blood annually, including an estimated 3 million surgery patients, according to the American Association of Blood Banks. Approximately 13 million units of blood are donated each year, according to 2000 statistics compiled by the association.

The research cited above was funded by research grants from the National Institutes of Health and the American Heart Association.

Chien Ho, Ph.D., is a professor in the department of biological sciences at Carnegie Mellon University in Pittsburgh, Pa.


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The above story is based on materials provided by American Chemical Society. Note: Materials may be edited for content and length.


Cite This Page:

American Chemical Society. "Genetically Engineered Hemoglobin Brings Artificial Blood A Step Closer." ScienceDaily. ScienceDaily, 7 November 2000. <www.sciencedaily.com/releases/2000/11/001107070452.htm>.
American Chemical Society. (2000, November 7). Genetically Engineered Hemoglobin Brings Artificial Blood A Step Closer. ScienceDaily. Retrieved August 21, 2014 from www.sciencedaily.com/releases/2000/11/001107070452.htm
American Chemical Society. "Genetically Engineered Hemoglobin Brings Artificial Blood A Step Closer." ScienceDaily. www.sciencedaily.com/releases/2000/11/001107070452.htm (accessed August 21, 2014).

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