Key result
Beta-hydroxybutyrate inhibited lactate oxidation by 30-60% and markedly decreased palmitate oxidation in isolated heart myocytes, supporting its role as a physiologic regulator of metabolism.
Why the study?
Does beta-hydroxybutyrate regulate myocardial substrate oxidation in isolated heart myocytes?
Does beta-hydroxybutyrate regulate myocardial substrate oxidation in isolated heart myocytes?
Beta-hydroxybutyrate acts as a physiologic regulator of myocardial substrate metabolism by inhibiting lactate and palmitate oxidation in isolated myocytes.
Answers are grounded in this paper and cite their sources.
Beta-hydroxybutyrate may regulate myocyte substrate oxidation in vitro; leaves open its physiologic role in vivo and any clinical relevance.
The role of ketone bodies in myocardial substrate oxidation was examined using freshly isolated Ca2+-tolerant heart myocytes, beta-hydroxybutyrate (beta OHB) inhibited lactate oxidation by the myocytes by 30-60%, and the inhibition was concentration dependent. Palmitate oxidation was also markedly decreased, whereas octanoate oxidation was only minimally affected by the presence of beta OHB. Lactate, octanoate, or palmitate had little, if any, effect on beta OHB oxidation. beta OHB oxidation was reduced by 22-28% in myocytes isolated from chronically diabetic rats, whereas the oxidation of palmitate remained similar to the controls. However, beta OHB still inhibited palmitate oxidation to the same extent as in the control cells. Our data support the role of beta OHB as a physiologic regulator of myocardial substrate metabolism.
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Chen et al. (1984) studied Myocardial substrate metabolism. beta-hydroxybutyrate (beta OHB) vs. Absence of beta OHB / control cells was evaluated on Lactate and palmitate oxidation. Beta-hydroxybutyrate inhibited lactate oxidation by 30-60% and markedly decreased palmitate oxidation in isolated heart myocytes, supporting its role as a physiologic regulator of metabolism.
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