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Abstract #4769

Quantitative modeling and detection of flux through pyruvate dehydrogenase in human myocardium

Jeffry R. Alger1, Jian-xiong Wang1, Jeannie Baxter1, Jeff Liticker2, Crystal Harrison1, Vlad Zaha3, Albert Chen4, Salvador Pena1, Lucy Christie1, Richard Martin1, Kelley Derner1, Carol Parcel1, A. Dean Sherry1, and Craig R. Malloy1

1Advanced Imaging Research Center, UT Southwestern Medical Center, Dallas, TX, United States, 2Simmons Cancer Center, UT Southwestern Medical Center, Dallas, TX, United States, 3Internal Medicine, UT Southwestern Medical Center, Dallas, TX, United States, 4University of Toronto, Toronto, ON, Canada

Flux through pyruvate dehydrogenase, a key regulatory enzyme, may be detected in human myocardium by hyperpolarization (HP) technology. A previously-validated model for quantitation of pyruvate metabolism in isolated hearts was extended to human myocardium. HP [13C]bicarbonate and HP[1-13C]lactate were detected from heart muscle after injection of ~0.43 mL/kg of 250mM HP[1-13C]pyruvate in four healthy subjects. All subjects tolerated the procedure well. Kinetic modeling yielded a rate constant for oxidation of pyruvate to bicarbonate of 0.005 sec-1, lower than that reported for isolated rodent hearts. Assessment of PDH flux in human myocardium is feasible with hyperpolarization technology.

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