Effect of Fatty Acids, Ketone Bodies, Diabetes and Starvation on Pyruvate Metabolism in Rat Heart and Diaphragm Muscle

Nature ◽  
1962 ◽  
Vol 195 (4839) ◽  
pp. 381-383 ◽  
Author(s):  
P. B. GARLAND ◽  
E. A. NEWSHOLME ◽  
P. J. RANDLE
Keyword(s):  
Fatty Acids ◽  
Rat Heart ◽  
Ketone Bodies ◽  
Diaphragm Muscle ◽  
Pyruvate Metabolism

Inhibition of the Phosphofructokinase Reaction in Perfused Rat Heart by Respiration of Ketone Bodies, Fatty Acids and Pyruvate

Nature ◽  
1962 ◽  
Vol 193 (4812) ◽  
pp. 270-271 ◽  
Author(s):  
E. A. NEWSHOLME ◽  
P. J. RANDLE ◽  
K. L. MANCHESTER
Keyword(s):  
Fatty Acids ◽  
Rat Heart ◽  
Ketone Bodies ◽  
Perfused Rat Heart

Regulation of lysophosphatidylcholine-metabolizing enzymes in isolated myocardial cells from rat heart

1985 ◽  
Vol 63 (8) ◽  
pp. 944-951 ◽  
Author(s):  
David L. Severson ◽  
Thea Fletcher
Keyword(s):  
Fatty Acids ◽  
Palmitic Acid ◽  
Free Fatty Acids ◽  
Rat Heart ◽  
Marked Reduction ◽  
Myocardial Cells ◽  
Acyltransferase Activity ◽  
Metabolizing Enzymes ◽  
Enzymatic Pathways ◽  
Lysophospholipase Activity

Enzymatic pathways involved in the metabolism of lysophosphatidylcholine were investigated in rat heart myocardial cells. Acyl CoA-dependent acyltransferase activity was localized in microsomes, and was much greater than lysophospholipase activity in either cytosolic or microsomal fractions. The cytosolic lysophospholipase was more sensitive to inhibition by palmitylcarnitine in comparison to free fatty acids. In contrast, free fatty acids (oleate and palmitate) produced a greater inhibition of the microsomal acyltransferase and lysophospholipase than did palmitylcarnitine. A reduction in the assay pH to 6.5 resulted in an increase in microsomal acyltransferase and cytosolic lysophospholipase activities, but brought about a marked reduction in the microsomal lysophospholipase activity. At pH 6.5, the percentage inhibition of the microsomal acyltransferase by palmitylcarnitine was reduced, whereas the inhibition by palmitic acid was enhanced. The inhibition of the microsomal lysophospholipase by both palmitylcarnitine and palmitic acid was reduced at pH 6.5. With respect to myocardial ischemia, the inhibition of microsomal acyltransferase by free fatty acids and the reduction in microsomal lysophospholipase activity due to acidosis may contribute to the elevation of cellular lysophosphoglycerides which are arrhythmogenic.

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