Sonal Josan1, 2, Tao Xu3, Yi-Fen Yen4, Ralph Hurd4, Julio Ferreira5, Che-Hong Chen5, Adolf Pfefferbaum1, 6, Dirk Mayer1, 2, Daniel Spielm
1Neuroscience Program, SRI International, Menlo Park, CA, United States; 2Radiology, Stanford University, Stanford, CA, United States; 3Electrical Engineering, Stanford University, Stanford, CA, United States; 4Applied Science Laboratory, GE Healthcare, Menlo Park, CA, United States; 5Chemical and Systems Biology, Stanford University, Stanford, CA, United States; 6Psychiatry and Behavioral Sciences, Stanford University, Stanford, CA, United States
Aldehyde dehydrogenase-2 (ALDH2) enzyme is important for eliminating toxic aldehydes that accumulate in several diseases. It is also used in ethanol metabolism in the liver, producing NADH in the process. This work investigates using hyperpolarized [1-13C]-pyruvate MRSI for in vivo measurement of ALDH2 activity. Two different doses of ALDH2 inhibitor disulfiram were used to reduce ALDH2 activity in two groups with another group acting as control. Using ethanol metabolism to modulate the NADH availability in rat liver, the resulting change in pyruvate-to-lactate conversion was measured with 13C MRSI and correlated with ALDH2 enzyme activity.