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Release: Immediate

UI researcher receives $6.3 million NIH grant to study hemoglobin

IOWA CITY, Iowa -- A University of Iowa researcher is leading a $6.3 million investigation into how hemoglobin functions at the atomic level and hopes the study's findings lead to a better understanding of how mutated forms of the molecule cause certain conditions.

"This basic research should result in new insights into the way in which hemoglobin transports oxygen throughout the body," said Arthur Arnone, Ph.D., UI professor of biochemistry. "It also may provide for better understanding and treatment of diseases involving hemoglobin and for the design of improved blood substitutes."

Arnone is the principal investigator for the five-year, six-institution study that began in January. The National Institute of General Medical Science, a sub-unit of the National Institutes of Health, is funding the project that, including direct and indirect costs, totals $6.3 million.

Every red blood cell contains 300 million molecules of hemoglobin. Hemoglobin is a blood protein that binds oxygen in the lungs then delivers the oxygen to all the tissues in the body. Considered a very efficient oxygen transporter, each hemoglobin molecule contains four oxygen-binding sites. Once the first molecules of oxygen bind to hemoglobin, the subsequent molecules bind much more readily. The same efficiency occurs in reverse when the hemoglobin releases the oxygen into tissues.

However, one in every 300 individuals has a naturally occurring hemoglobin mutation. Although most mutations do not affect how the molecules work, some -- such as the mutation that causes sickle cell anemia -- can be very serious. By understanding the basic mechanism by which normal hemoglobin transports oxygen, researchers can better understand the dysfunctions that result from mutations, Arnone said.

Arnone and other researchers in his laboratory are using X-ray crystallography (a form of high-resolution microscopy) to see individual molecules of hemoglobin. Using this technology, the research team will determine the atomic structures of a large number of hemoglobin mutations that will be made in the lab by a technique called site-directed mutagenesis.

Researchers at the collaborating institutions will use various complementary technologies to determine how these mutations alter the hemoglobin's oxygen-binding efficiency. The other sites involved include labs at Northwestern University, the University of Pennsylvania, the State University of New York - Buffalo, Albert Einstein College of Medicine in New York City and the University of Parma in Italy.

2/11/99