Hormone-Sensitive Lipase (HSL) Expression and Regulation in Skeletal Muscle

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Abstract
Because the enzymatic regulation of muscle triglyceride metabolism is poorly understood we explored the character and activation of neutral lipase in muscle. Western blotting of isolated rat muscle fibers demonstrated expression of hormone-sensitive lipase (HSL). In incubated soleus muscle epinephrine increased neutral lipase activity by beta-adrenergic mechanisms involving cyclic AMP-dependent protein kinase (PKA). The increase was parallelled by an increase in glycogen Phosphorylase activity and could be abolished by antiserum against HSL. Electrical stimulation caused a transient increase in activity of both neutral lipase and glycogen Phosphorylase. The increase in lipase activity during contractions was not influenced by sympathectomy or Propranolol.