Ida Stephens Owens

Ida Stephens Owens
Nationality American
Fields Physiology
Biochemistry
Institutions National Institute of Child Health and Human Development
Alma mater Duke University (Ph.D., 1967)
Thesis Amino Acid Esters as Inhibitors of Growth and of Amino Acyl-tRNA in Synthetases in Astasia Longa and Eugenia Gracilis (1967)
Doctoral advisor Jacob J. Blum
Known for Drug-detoxifying enzyme metabolism

Early life

Ida Virginia Stephens Owens grew up on a farm in Whiteville, North Carolina.[1] Her mother died when she was six years old.[1]

Education

Owens' early education was in segregated public schools.[1] Owens then attended North Carolina College, now North Carolina Central University, graduating in 1961 summa cum laude in Biology (B.S.) and Mathematics (minor).[2][3] In 1962, she began her Ph.D. studies in biochemistry and physiology at Duke University shortly after Duke racially integrated its graduate and professional schools.[2] When she graduated in 1967, she became one of two first African Americans to receive a Ph.D. from Duke University and the first woman to receive any degree in physiology from Duke.[2][4]

Scientific career

After graduating, Owens held a postdoctoral position at the National Institutes of Health (NIH) focused on how drugs are chemically processed in the body.[3] Owens then became an NIH researcher, working for the Laboratory of Developmental Pharmacology in the National Institute of Child Health and Human Development (NICHD). In 1981 her work evolved into the NICHD Section on Drug Biotransformation. Since 1988, Owens has directed NICHD's Section on Genetic Disorders of Drug Metabolism in the Program on Developmental Endocrinology and Genetics.[2][3]

Scientific advancements

Owens' postdoctoral work sparked her specific interest in a critical group of enzymes, called glucuronosyltransferases (abbreviated UGTs), responsible for detoxifying numerous drugs, toxic chemicals, and other substances.[2][3] She then designed methods to study genes that code for specific UGT enzymes. These methods allowed her to characterize UGT1A1, the gene coding for an enzyme in this family that processes the protein bilirubin, a breakdown product of hemoglobin, and to identify 12 other previously unknown and independent UGT enzymes.

Owens' research group has subsequently made multiple advancements regarding UGT enzyme biology. Her laboratory was the first to identify a genetic defect, in the gene UGT1A1, that leads to Crigler-Najjar syndrome. Crigler-Najjar syndrome is a disorder that disrupts normal processing and excretion of bilirubin, leading to jaundice.[3] Owens' research group also identified that UGT enzymes must be activated before they can detoxify foreign chemicals and that in some cases suppressing these enzymes could enhance the effects of therapeutic drugs.[5] Owens' laboratory found that activity of UGT enzymes can be lessened by kinase inhibitors and that protein kinase C and tyrosine kinase enzymes can alter the enzyme specificity, likely contributing to their ability to detoxify a wide range of foreign chemicals.[3]

Honors

Owens received the 1992 NIH Director's Award and, in 2013, the Duke University Graduate School's first Distinguished Alumni Award.[2]

References

  1. 1 2 3 Weiss, Ivan (Director) (2014). The Education of Ida Owens: Science, Civil Rights, and the Integration of Duke University. Durham, N.C.
  2. 1 2 3 4 5 6 "Ida Stephens Owens Named First Recipient of The Graduate School Distinguished Alumni Award". Duke Graduate School. 2013-03-16. Retrieved 2016-03-29.
  3. 1 2 3 4 5 6 "NICHD Staff Detail for Ida Owens". National Institute of Child Health & Human Development. Retrieved 2016-03-29.
  4. "Mrs. I. Stephens Owens to Get Ph.D. Degree from Duke Univ.". The Carolina Times. Durham. N.C. 1967-06-03. Retrieved 2016-03-30.
  5. Jr, Charles W. Carey (2008-10-23). African Americans in Science: An Encyclopedia of People and Progress. 1. ABC-CLIO. ISBN 978-1-85109-999-3.
This article is issued from Wikipedia - version of the 8/4/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.