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Dr. Moore:

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Dr. Moore's CV in brief

Publications

Cardiovascular Biology Research Program

Dr. Moore In The News

OMRF discovery could lead to male contraceptive pill

Kevin L. Moore, M.D. Associate Member, Cardiovascular Biology Research Program Adjunct Assistant Professor, Departments of Medicine and Cell Biology, University   of Oklahoma Health Sciences Center Member, Oklahoma Center for Medical Glycobiology Fred Jones Distinguished Scientist

Research Interests
Sulfated protein tyrosine residues are formed by the action of an enzyme activity called 3’-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase, commonly called tyrosylprotein sulfotransferase (TPST, EC 2.8.2.20). In man protein-tyrosine sulfation is mediated by one of only two Golgi TPST isoenzymes (TPST-1 and TPST-2) that were first purified and cloned by our laboratory. These enzymes mediate the transfer of the 5’-sulfuryl group from the sulfate donor, 3’-phosphoadenylyl-sulfate, to the side chain hydroxyl group of protein-tyrosine residues to form protein tyrosine O4-sulfate and adenosine 3’,5’-bisphosphate. Complementary DNAs encoding TPST-1 and TPST-2 orthologs have also been identified in many vertebrate and invertebrate species. A relatively small number of proteins are known to undergo tyrosine sulfation in humans, including certain adhesion molecules, G-protein-coupled receptors, coagulation factors, serpins, extracellular matrix proteins and hormones. Many of these proteins require tyrosine sulfation for optimal function.

My laboratory is focused on two major lines of investigation that are designed to gain a comprehensive understanding of the enzymology and biology of tyrosine sulfation. In the first case, we are using classical enzyme kinetic methods to compare and contrast the kinetic mechanism and substrate specificity of TPST-1 and TPST-2. In the second case, we have generated Tpst1 and Tpst2 null mice as well as Tpst double deficient mice in order to investigate the role of tyrosine sulfation in vivo. Our initial studies have revealed distinct phenotypic differences between TPST-1 and TPST-2 deficient mice. The long-term goals of these studies are to directly link these contrasting phenotypes to defective tyrosine sulfation of proteins.

Joined OMRF Scientific Staff in 1993.

Mailing Address
Cardiovascular Biology Research Program, MS 45
Oklahoma Medical Research Foundation
825 N.E. 13th Street
Oklahoma City, Oklahoma 73104

Contact Information
Phone: (405) 271-7314
Fax: (405) 271-7417
E-mail: Kevin-Moore@omrf.org