Type L hormone-sensitive lipase hydrolyzes endogenous triacylglycerols in muscle in exercised rats.
Lipoprotein lipase (LPL) exists in two distinct fractions in heart and skeletal muscle: LPL in capillary beds regulates the metabolism of chylomicrons and very low-density lipoproteins on the surface of the endothelial cells; in contrast, the intracellular fraction of LPL regulates endogenous triacylglycerol (TG) stores. The name of the intracellular enzyme has been changed from LPL to type L hormone-sensitive lipase (HSL) because it is responsive to epinephrine and glucagon levels in heart. In this symposium evidence will show that epinephrine also activates type L HSL in skeletal muscle. Further justification for the name change is that plasma lipoproteins do not exist in parenchymal cells of muscle and the intracellular enzyme possesses many of the classical characteristics described for LPL. Exercise activates type L HSL in heart and skeletal muscle with a concomitant decrease in muscle TG stores. These results provide evidence that under a normal physiological condition, such as exercise, type L HSL participates in the regulation of intramuscular TG stores.
D000818:Animals; D002196:Capillaries / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D004837:Epinephrine / Q000494:pharmacology; D006868:Hydrolysis; D008071:Lipoprotein Lipase / Q000502:physiology*; D008297:Male; D009132:Muscles / Q000378:metabolism*; D005082:Physical Exertion; D051381:Rats; D014280:Triglycerides / Q000378:metabolism*
D014280:Triglycerides; D008071:Lipoprotein Lipase; D004837:Epinephrine