Primary structure of the site on bovine hormone-sensitive lipase phosphorylated by cyclic AMP-dependent protein kinase

FEBS Letters ◽  
1988 ◽  
Vol 229 (1) ◽  
pp. 68-72 ◽  
Author(s):  
Andrew J. Garton ◽  
David G. Campbell ◽  
Philip Cohen ◽  
Stephen J. Yeaman
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Primary Structure ◽  
Hormone Sensitive Lipase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Hormone Sensitive

scholarly journals Hormone-sensitive lipase in differentiated 3T3-L1 cells and its activation by cyclic AMP-dependent protein kinase.

1981 ◽  
Vol 78 (2) ◽  
pp. 732-736 ◽  
Author(s):  
M. Kawamura ◽  
D. F. Jensen ◽  
E. V. Wancewicz ◽  
L. L. Joy ◽  
J. C. Khoo ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Hormone Sensitive Lipase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Hormone Sensitive

scholarly journals Expression of hormone-sensitive lipase and its regulation by adrenaline in skeletal muscle

1999 ◽  
Vol 340 (2) ◽  
pp. 459-465 ◽  
Author(s):  
Jozef LANGFORT ◽  
Thorkil PLOUG ◽  
Jacob IHLEMANN ◽  
Michele SALDO ◽  
Cecilia HOLM ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Soleus Muscle ◽  
Lipase Activity ◽  
Glycogen Phosphorylase ◽  
Hormone Sensitive Lipase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Hormone Sensitive ◽  
Neutral Lipase

The enzymic regulation of triacylglycerol breakdown in skeletal muscle is poorly understood. Western blotting of muscle fibres isolated by collagenase treatment or after freeze-drying demonstrated the presence of immunoreactive hormone-sensitive lipase (HSL), with the concentrations in soleus and diaphragm being more than four times the concentrations in extensor digitorum longus and epitrochlearis muscles. Neutral lipase activity determined under conditions optimal for HSL varied directly with immunoreactivity. Expressed relative to triacylglycerol content, neutral lipase activity in soleus muscle was about 10 times that in epididymal adipose tissue. In incubated soleus muscle, both neutral lipase activity against triacylglycerol (but not against a diacylglycerol analogue) and glycogen phosphorylase activity increased in response to adrenaline (epinephrine). The lipase activation was completely inhibited by anti-HSL antibody and by propranolol. The effect of adrenaline could be mimicked by incubation of crude supernatant from control muscle with the catalytic subunit of cAMP-dependent protein kinase, while no effect of the kinase subunit was seen with supernatant from adrenaline-treated muscle. The results indicate that HSL is present in skeletal muscle and is stimulated by adrenaline via β-adrenergic activation of cAMP-dependent protein kinase. The concentration of HSL is higher in oxidative than in glycolytic muscle, and the enzyme is activated in parallel with glycogen phosphorylase.

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