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Institute of Medicine, Nuclear Research Center, Jülich, FRG
Department of Cardiology, University of Düsseldorf, Düsseldorf, FRG
Univeristy of Connecticut and VA Medical Center, Newington, Connecticut
Institute of Medical Radiation Physics, University of Essen, FRG
Correspondence: For reprints contact: Prof. Dr. Ludwig E. Feinendegen, Institute of Medicine, Nuclear Research Center, P.O. Box 1913, D-5170 Jülich, West Germany.
ABSTRACT
The human myocardium retains oPPA as opposed to pPPA. Therefore turnover of oPPA was compared with that of pPPA in rat hearts and in man, the latter by using substrates double-labeled with 123/131I and 14C. Moreover, substrate binding to coenzyme-A was tested in vitro. In rats, oPPA remained mainly in the pool of free fatty acids, as opposed to pPPA, which was metabolized by mitochondrial ß-oxidation. Binding to coenzyme-A at maximum was 62% for oPPA, 81% for pPPA and 90% for palmitic acid.
In man, after i.v. and intracoronary injection of double-labeled oPPA, the two radionuclides reappeared together in venous blood and in coronary sinus respectively, in an unchanged ratio but at a significantly lower rate than with pPPA. It can be concluded that oPPA is bound to coenzyme-A and is retained in the cytosolic lipid pool, while pPPA is metabolized by mitochondrial ß-oxidation. A dual-tracer application of oPPA and pPPA has the potential of being a specific probe for the function of the carnitine shuttle.
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