Abstract

Endothelial lipase (EL) is an enzyme capable of HDL phospholipids hydrolysis. Its action leads to a reduction in the serum high-density lipoprotein concentration, and thus, it exerts a pro-atherogenic effect. This study examines the impact of a single bout exercise on the gene and protein expression of the EL in skeletal muscles composed of different fiber types (the soleus—mainly type I, the red gastrocnemius—mostly IIA, and the white gastrocnemius—predominantly IIX fibers), as well as the diaphragm, and the heart. Wistar rats were subjected to a treadmill run: (1) t = 30 [min], V = 18 [m/min]; (2) t = 30 [min], V = 28 [m/min]; (3) t = 120 [min], V = 18 [m/min] (designated: M30, F30, and M120, respectively). We established EL expression in the total muscle homogenates in sedentary animals. Resting values could be ordered with the decreasing EL protein expression as follows: endothelium of left ventricle > diaphragm > red gastrocnemius > right ventricle > soleus > white gastrocnemius. Furthermore, we observed that even a single bout of exercise was capable of inducing changes in the mRNA and protein level of EL, with a clearer pattern observed for the former. After 30 min of running at either exercise intensity, the expression of EL transcript in all the cardiovascular components of muscles tested, except the soleus, was reduced in comparison to the respective sedentary control. The protein content of EL varied with the intensity and/or duration of the run in the studied whole tissue homogenates. The observed differences between EL expression in vascular beds of muscles may indicate the muscle-specific role of the lipase.

Highlights

  • The highest expression of endothelial lipase was detected in t at 100 arbitrary units (AU)

  • In comparison to the control group, we found that 30 min run with both moderate and high intensity reduced the expression of mRNA for endothelial lipase (EL)

  • We demonstrated that even a single run can differently affect the expression pattern of quite a few enzymes involved in the heart lipid metabolism, i.e., adipose triglyceride lipase (ATGL), CGI-58, and

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Summary

Introduction

Serum lipoproteins are important carriers of lipids in the blood. Studies have focused on endothelial lipase (gene nomenclature, LIPG; protein, EL), i.e., a phospholipase with high affinity for phospholipids carried by high-density lipoprotein, and relatively low activity for its (HDL) TGs. Studies have focused on endothelial lipase (gene nomenclature, LIPG; protein, EL), i.e., a phospholipase with high affinity for phospholipids carried by high-density lipoprotein, and relatively low activity for its (HDL) TGs As a result, it primarily hydrolyses the first (sn-1) ester bond of phospholipids and releases free fatty acids. It primarily hydrolyses the first (sn-1) ester bond of phospholipids and releases free fatty acids It reduces the size of phospholipids in each class of lipoproteins with HDL being a preferred substrate [3,4]. In contrast to other triacylglycerol lipases, EL is synthetized by vascular endothelial cells ( it has been termed endothelial lipase) and to a lesser extent by smooth muscle cells and macrophages

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